accession
stringlengths 6
10
| name
stringlengths 6
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| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
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⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
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Q83GK3 | PDXT_TROWT | Pyridoxal 5'-phosphate synthase glutaminase subunit | Tropheryma | MTVGVLSLQGSFYEHLFILSRLNTDHIQVKTSEDLSRVTRLIIPGGESTAMLALTQKSGLFDLVRDRIMSGMPVYGTCAGMIMLSTFVEDFPNQKTLSCLDIAVRRNAFGRQINSFESEVSFLNSKITVPFIRAPKITQIGEGVDVLSRLESGDIVAVRQGNVMATAFHPELTGGAAVHEYFLHLGLE | Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Q83GK3 |
P06858 | LIPL_HUMAN | Phospholipase A1 | Homo | MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG | Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage . Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity . Mediates margination of triglyceride-rich lipoprotein particles in capillaries . Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans . | P06858 |
Q48219 | OPP2A_HAEIF | Outer membrane protein P2 | Haemophilus | MKKTLAALIVGAFAASAANAAVVYNNEGTNVELGGRLSIIAEQSNSTIKDQKQQHGALRNQSSRFHIKATHNFGDGFYAQGYLETRLVSAQSGTESDNFGHIITKYAYVTLGNKAFGEVKLGRAKTIADGITSAEDKEYGVLNNSKYIPTNGNTVGYTFKGIDGLVLGANYLLAQERYKYGGAAGGAGGAGAVAGEVYPQKISNGVQVGAKYDANNIIAGIAYGRTNYRESIHEKDLGKKQQVNGALSTLGYRFSDLGLLVSLDSGYAKTKNYKDKHEKSYFVSPGFQYELMEDTNFYGNFKYERNSVDQGKKEREQAVLFGIDHKLHKQVLTYIEGAYARTRTNDKSKAEKTEKEKSVGVGLRVYF | Forms pores that allow passive diffusion of small molecules across the outer membrane. | Q48219 |
A7HZ45 | RNPH_PARL1 | tRNA nucleotidyltransferase | Parvibaculum | MRPSGRQPQEMRTVSFEPGVAKHAEGSCLVRFGDTHVLCTASLEERVPPFLKGGGQGWVTAEYGMLPRSTHERMRREAAQGKQSGRTQEIQRLVGRSLRSVVDLKALGERQISVDCDVLQADGGTRTASITGAWVALHQCIEWMRARSMISAPVLKDHVAAISCGIYQGVPVVDLDYAEDSTADTDANFVITGKGGICEIQGTAEGEPFSDEEFLSLLALAKTSIADLVRRQKEAVSA | Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | A7HZ45 |
Q6FIV0 | LCL2_CANGA | Long chronological lifespan protein 2 | Nakaseomyces/Candida clade | MNLLMVLFVAQAHAFFFGQQQQQQQQQASYEDRVLDSGCAKYLCSDTLECVDSWKDCPCPFPKSQLKCMLPKGSNRPYVCISKPATHDEKLNLIYDDPVQGPKAAIKGMRDCGWVQQNL | Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway. | Q6FIV0 |
Q8FPD4 | RECX_COREF | Regulatory protein RecX | Corynebacterium | MTDPITPHPGENQAAKLEKLRTALEEFSRRQEEGAASSLFDREAEEKKAEVRRRALLLLDQRARSRSELQGRLGALDFDHDIIEEVLDDLTRANLINDESFAQEWVRQRAQRRGKSTRVLDRELRDKGVDAGIRARALEQIDPEDERDTARAVAVKKARSESRIPADRSDYDKALRRVVGALARRGFPAGMSMDLAREALDERIEDLRQH | Modulates RecA activity. | Q8FPD4 |
A7ZIH5 | EX7S_ECO24 | Exodeoxyribonuclease VII small subunit | Escherichia | MPKKNEAPASFEKALSELEQIVTRLESGDLPLEEALNEFERGVQLARQGQAKLQQAEQRVQILLSDNEDASLTPFTPDNE | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A7ZIH5 |
P39979 | HPA3_YEAST | Histone and other protein acetyltransferase 3 | Saccharomyces | MSNEEPEKMVNDRIVVKAIEPKDEEAWNKLWKEYQGFQKTVMPPEVATTTFARFIDPTVKLWGALAFDTETGDAIGFAHYLNHLTSWHVEEVVYMNDLYVTERARVKGVGRKLIEFVYSRADELGTPAVYWVTDHYNHRAQLLYTKVAYKTDKVLYKRNGY | N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine . Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated . D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids . | P39979 |
Q3K0P1 | MIAA_STRA1 | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Streptococcus | MRKIKLIAVVGPTAVGKTALGIELAKTFNGEIISGDSQQVYQKLDIGTAKASKEEQEQAYHHLIDVREVNENYSVYDFVKEAKVAIDTIISKGKIPIIVGGTGLYLQSLFEGYHLGGEVNQETLMAYREKLESLSDEDLFEKLTEQSIVIPQVNRRRAIRALELAKFGNDLQNSESPYDVLLIGLNDDRQVLYDRINRRVDLMIDNGLLDEAKWLYDNYPSVQASRGIGYKELFPYFSKQIPLEEAVDKLKQNTRRFAKRQLTWFRNRMNVEFIMVGEENYQQKIKRKVSDFLSSK | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | Q3K0P1 |
A6UQY1 | CDPAS_METVS | CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase | Methanococcus | MDLINLLFVSFWFILPAYTANAMACIFGGGKPVDLNKNFIDQKRLIGNGVTYRGTFFGVFFGIVTAIIQYLVSNLGFKFILSFNFTLIEYVIIGFLLSFGALFGDMFGSFLKRRLGFKQGQSAPVLDQITFIVFALIFVSYYYLVPSKISITLLILSPVVHILSNIIAYKLGLKKVWW | Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | A6UQY1 |
B9DVG6 | GATA_STRU0 | Glutamyl-tRNA(Gln) amidotransferase subunit A | Streptococcus | MSLNHKTIDELHTLLLSKEISAKELTQATLDDIKAREDAVGSFITLAEEKALSQAEAIDARGIDPNNVMSGIPFAVKDNISTEGILTTAASKMLYNYEPIFNATAIEKAYAKDMIVIGKTNMDEFAMGGSTETSYFKKTKNAWDHSKVPGGSSGGSATAVASGQVRLSLGSDTGGSIRQPAAFNGIVGMKPTYGTVSRFGLIAFGSSLDQIGPFSQTVKENAQLLNVIAGSDDKDSTSAPVQIADYTSAIGKDIKGMKIALPKEYLGEGIDPKIKENILEAAKQFEKLGATVEEVSLPHSKYGVAVYYIIASSEASSNLQRFDGIRYGYRAQDAKTLEEIYVNTRSQGFGEEVKRRIMLGTFSLSSGYYDAYFKKAGQVRTLIIQDFEKVFADYDLIIGPTAPTVAFGLDTLNHDPVSMYLADLLTIPVNLAGLPGISIPSGFVDGLPVGLQLIGPKYSEERIYQAAAAFEATTDYHKQQPVIFGGEK | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | B9DVG6 |
Q1ZXA1 | C521A_DICDI | Discodiene biosynthesis cluster protein cyp521A1 | Dictyostelium | MILLTLLYLIIFYIIIDFIKKNYKTKNQLPSPLGIALPIIGHLHLLRTDPYKTLAKASKKTEHGILKCWNGEHLMVVVDNPSIIKQMYVNTNNFTDRPQTKVFEIISRNYKNSGFANGEKWKHLRGLYAPSFTKIKSRPHENIILKYVNFEIKSLKNHAITNSIYNPFLIENINSFGTKVITEIIFGREFSENEVYSLIGPMNKLFGILDTPFPSESISFLKPFYRRSYKECDKQCEELFKLVEKVYDDHLLNLDKDNPKDVMDVMIVETDFKEKDHVICICCDLLMGTKDTFNTIVLWFFVLMINYQDVQLKGYQEIIKVLECTGRDHVTIEDIDKLPYIDGIIKEISRIHPAGPLSVPRTAINDIMINGYFIPKGCHVFQNTYGAVYNYMKESDEPCKMKPERWIENEKLRKDGKLDPTNDLALISLPFSSGIRNCPGVGFAEYELFLLFSNIILNFHLSSPNNLKLNESGHFGLTMKPFPFLVDLKLR | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the trisnorsesquiterpene discodiene which has a function during later stages of multicellular development, during the transition from fingers to Mexican hats . The terpene synthase tps8 converts its substrate farnesyl diphosphate (FDP) into the bicyclic sesquiterpene alcohol discoidol . The cytochrome P450 monooxygenase cyp521A1 then catalyzes the oxidative degradation of discoidol to form the trisnorsesquiterpene discodiene . | Q1ZXA1 |
A9B416 | RS19_HERA2 | 30S ribosomal protein S19 | Herpetosiphon | MSRSTKKGPFVDVRLLSRVETMNRGNEKRPLKTWSRDSTIFPQMVGHTIAVHDGRRHVPVYITENMVGHKLGEFAPTRTFRGHGGKKADKRGKLK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | A9B416 |
Q8Y5R6 | LEUD_LISMO | Isopropylmalate isomerase | Listeria | MEEIKVHIGKTVALMNDNIDTDQIIPKSFLKRIERTGFGEFLFDSWRYLPNRKPNPDFPLNALDRQEATILITGENFGCGSSREHAAWALLDYRFRVIIAGSYSDIFYMNCTKNGVLPIVLPREAREKLAKIAAEENVTIDLPNQQVISSVGTYPFEIDATWKNKFINGLDDIAITFEHIDAIKAYEQKVDSI | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q8Y5R6 |
Q0SS92 | COAD_CLOPS | Pantetheine-phosphate adenylyltransferase | Clostridium | MRVGVYPGSFDPITKGHLDLIERAASKFDKVIVAVLININKKGMFSIEERVNLIEKCVAKYNNVEVKSFNGLLIDFVRKEKADVIIKGLRSVTDFEYEFQMALMNRELANEVETVFMVTSPNYSYISSSAIKQVASFSGEIKNFVPKEIVEDLEERIISLRGEG | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | Q0SS92 |
P97501 | FMO3_MOUSE | Trimethylamine monooxygenase | Mus | MKKKVAIIGAGVSGLAAIRSCLEEGLEPTCFERSDDVGGLWKFSDHIEEGRASIYQSVFTNSSKEMMCFPDFPYPDDFPNFMHHSKLQEYITSFAKEKNLLKYIQFETPVTSINKCPNFSTTGKWEVTTEKHGKKETAVFDATMICSGHHIFPHVPKDSFPGLNRFKGKCFHSRDYKEPGIWKGKRVLVIGLGNSGCDIAAELSHVAQKVTISSRSGSWVMSRVWDDGYPWDMVVLTRFQTFLKNNLPTAISDWWYTRQMNARFKHENYGLVPLNRTLRKEPVFNDELPARILCGMVTIKPNVKEFTETSAVFEDGTMFEAIDCVIFATGYGYAYPFLDDSIIKSRNNEVTLYKGVFPPQLEKPTMAVIGLVQSLGATIPITDLQARWAAQVIKGTCTLPSVNDMMDDIDEKMGEKFKWYGNSTTIQTDYIVYMDELASFIGAKPNLLWLFLKDPRLAVEVFFGPCSPYQFRLVGPGKWSGARNAILTQWDRSLKPMKTRVVSKVQKSCSHFYSRLLRLLAVPVLLIALFLVLI | Essential hepatic enzyme that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds. Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite. TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thrombus formation. | P97501 |
Q3ECH9 | CLE18_ARATH | CLE18 C-terminus | Arabidopsis | MHLLKGGVVLIITLILFLITSSIVAIREDPSLIGVDRQIPTGPDPLHNPPQPSPKHHHWIGVEENNIDRSWNYVDYESHHAHSPIHNSPEPAPLYRHLIGV | Extracellular signal peptide that regulates cell fate . Represses root apical meristem maintenance . Root growth factor that regulates the pattern of root growth and lateral root development . Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2 . | Q3ECH9 |
Q058B2 | DAPE_BUCCC | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Buchnera | MHTNVLNLSKKLINISSISPRDLGCQEILIKRLQLLGFFIERINLKDTKNFWAYRGKGKTVTFLGHTDVVPAGSTRKWKTSPFVATIKDGKLFGRGSADMKGSIAAMLIAVENFIKKFPNHKGRISFLITSDEETSGKNGIRKVVSILKEKKEVIDFCLVGEPTSEKILGDCVKNGRRGSLSADLMIYGTQGHIAYPKLFLNPIHNSIPFLLDLSNLIFDKGNLFFEPTSIQISKIFSEKNCTLNMIPGELRVFFNIRFNTLVNKKKIIRIVENLLNKYLIKYSIFWTYHAKPFLSSSNFLLNLLTKCIYKHTNIIPKIKNNGGTSDARFIFNLTDKIIEFGLPNLTIHKVNEYVYINDLLKLQNIYYSFLEKLLL | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | Q058B2 |
Q28487 | VACHT_MACFU | Solute carrier family 18 member 3 | Macaca | GMGLANLLYAPVLLLLRNVGLLTRSRSERDVLLDEPPQGLYDAVRLRERPVSGQDGEPRSPPGPFD | Involved in acetylcholine transport into synaptic vesicles. | Q28487 |
Q59XP0 | SEC9_CANAL | Protein transport protein SEC9 | Candida | MGIKKMFQKKEPTEQEIREELSRVGISTRSNNTRQEKFGAFKNYAQERANMKPQLGPVGGNPYANINPGTNNNNNNPYANDNGNNSTGNPNNNSNSNNGGNPYGGGVTNNNPYGGSGGNGRGSSPSPYAPTTSTTTRSSNPYGNNNGSRSSQNTSSPYAKSTNNSSYSNSPYSGSTVNNGNRGGHSNNSNSSAGGNPYAAGGRSSQSQNSRDNVYTAPATRTSTRQTQGYGGGDTDSTLDLNAIPSHQMFDNKKPIKRNQQSSQQPANDYNLDLNDEYGEEEDLNLDISEVPEEQQQINSEDEEVEAIKQDIKFVKQESVQSTRNTLRMAQEADASGTNTLGMLGSQSERLYNAEQNLLLAETQTQIADEKVKELKRLNRSIFIPANGNPFNKKSRLRQQEEKIKNQKLQEKYIRENNRQEMFASEQRIKQGITNNSTNNDVYNKYQDEKNLSAAKRYQFENDSEDDDMEKEIASNLNQIDQYAKKLKGLANTMGTEVDNQNTRLKKIEESADKLDINVHMNTTRLNNIR | Late secretory t-SNARE protein required for secretion and proper cytokinesis. Plays an important role in the secretion of virulence-associated extracellular enzymes and vesicle-mediated polarized hyphal growth. | Q59XP0 |
D4ADY9 | ELOV7_RAT | Very long chain 3-oxoacyl-CoA synthase 7 | Rattus | MAFSDLTSRTVRFYDNWIKDADPRVENWLLMSSPLPQTIILGLYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGTGYSFRCDIVDYSQSPRAMRMVHTCWLYYFSKFIELFDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYFYYGLCAMGPAYQKYLWWKKHLTSLQLVQFVLVTVHIGQIFFMEDCNYQYPVFLYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTMENGNCKSKHH | Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. | D4ADY9 |
Q3Z8G2 | SYT_DEHM1 | Threonyl-tRNA synthetase | Dehalococcoides | MANQIDEAKPISDLEIMRHSAAHIMAEAVLSMFPEAKLGIGPAIDTGFYYDFDLPRTLTPEDLPEIETRMNQLVKANLPFRREEMSKDEARKLFADQPYKLELLDDIPDEIVSVYRQGNLCDLCRGPHVNYTSKVKAFKLLSIAGAYWRGDEKRPMLQRIYGAAFLDKASLAEYLNMLEESAKRDHRKLGKELELFSLHQEIGGGLVNWLPNGAIVRHLIEEFWKKEHLKRGYSLVYTPHIAKVDLWKTSGHWGFYRENMYSPMDIDGEEYVLKPMNCVYHILMFKNRTRSYKELPIRMAELGTVYRYERSGVLHGLSRVRGFTQDDAHIFCLYEQLEKEVVKVLDLAKFMIDTFGFTRYKVMLSTRPEKYVGELDKWEYATDILAKALESNQIAYQVDPGEGVFYGPKIDIKFEDALGRAWQGPTIQVDFQLPERFDVSVVGEDGKDQPVAMVHRTVLGSMERFMSCLTEQYGGAFPVWLSPKQVMLIPIADRHSEFAEKLACELREEEVRVEVDNRSETMNQKIRQAQLAKIPYMLVVGDKEIETQSVSIRTRSGSQCVMPFAEFKSMLIDKIKTKSTEI | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | Q3Z8G2 |
B6EMV8 | METK_ALISL | Methionine adenosyltransferase | Aliivibrio | MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVMVGGEVTTSAWVDIEEITRETVREIGYVHSDMGFDANSCAVLNTIGKQSPDINQGVDKEDPKEQGAGDQGIMFGYATNETPILMPAPITYAHLLVKQQAEVRKSGKLDFLRPDAKSQVTFQYDQGKIVGIDAVVLSTQHSDSVTTADLREAVMEEIIKPVLPAEWLSKETKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGAARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGMADRCEIQLSYAIGVADPTSIMIETFGTEKVSHDIIIESVRQHFDLRPYGLQEMLNLLQPIYKKTAAYGHFGREEFPWEATDKAEILRDFAGIK | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | B6EMV8 |
Q24XT2 | LEU3_DESHY | Beta-IPM dehydrogenase | Desulfitobacterium | MPKIAVLPGDGIGQEIIPQAVRVLKAVLAETDAEFEFQDYPIGGAAIELVGKALPDETLQGCREADAVLLGAVGGHQWDHLPASERPETAALLGLRKGLNFYANIRPVRMIPSLLATSTLKENVLDGVDMVVIRELTGGVYFGEKGRSDNPRSAYDKMTYSEEEIRRILIQGFETAMLRSKKLCSVDKANVLETSRLWREIANELAKEYPEVELTHMYVDNAAMQLVRNPKQFDVIVTENMFGDILTDLASMLGGSIGMLSSASLSGTQGMYEPAHGSAPDIAGKNLANPLATILSAALMLRYSFGMEAEALRIESAVEKVLEQGYRTGDLAQAGDKVVGTIEMGDAVLAAL | Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | Q24XT2 |
F8JX40 | FLUDE_STREN | Fluoroacetaldehyde dehydrogenase | Streptomyces | MTVHQAPGTPGSVISLRPRYDNWIGGDWKAPAEGRYFANPTPVTGEEYTEIARSTAADIDLALDAAHAAAPAWGRTAPAERAAVLGRIADRIEQHLTELAVAEVWDNGKPIREALAADLPLAVDHFRYFAGVLRAQEGSISQLDEDTVAYHFHEPLGVVGQIIPWNFPLLMAVWKLAPALAAGNAVVLKPAEQTPVSILVLMELIADILPPGVINVVNGFGIEAGKPLAINPRIAKVAFTGETTTGRLIMQYASQNLIPVTLELGGKSPNLFFEDVAAARDDFYDKALEGFTMFALNQGEVCTCPSRALIAGGIYDGFLGDALERTRAVKQGNPLDTETMIGAQASNDQLEKILSYIDIGTAEGAKVLTGGERVDLGGSLSGGYYVAPTIFEGDNRMRIFQEEIFGPVVSVTRFDGYDDAISIANDTLYGLGAGVWTRDLSTAYRAGRAIQAGRVWTNCYHAYPAHAAFGGYKNSGIGRETHKMMLDHYQQTKNLLISYSAKGPGLF | Catalyzes the oxidation of fluoroacetaldehyde to fluoroacetate. Has high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde. | F8JX40 |
Q0RRW1 | NUOH_FRAAA | NDH-1 subunit H | Frankia | MSVTASTLVLAAPVDPDLSGFGDDPFWLILLKGVAVFAFLLLMTLFSIVFERKVVAKMQQRVGPNRHGPKGWLQSLADGAKLMLKEDLIPALADKPIFILAPILSAVPAFLAFAVIPFGPEVSIFGERTTLQLADLPVSVLYMLAAASLGVYGLILSGWSSGSTYPLLGSLRSAAQIISYEVAMGLSFVAVFIYAGTLSTSGIVESQSGRWYIALVPSFVLYCISMVGETNRTPFDLPEAEGELVGGFHTEYSSIKFAFFFLAEYINMVTVSAIATTLFLGGWQPPPIPGLSGLDHGWVPLIWFVLKLLLFLFFFIWLRGTLPRLRYDQFMAFGWKVLIPVGLLWVLVIATFRVYQKDVDDRTPWLIGAGVVIGIMLIVALLDPGGAKHQRELEEAERRKLAEAPSLESIPWPPPPPGGAHHRPAVPAGTSANGSSTVIPADPPPRQES | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Q0RRW1 |
O76002 | OR2J2_HUMAN | Olfactory receptor OR6-19 | Homo | MMIKKNASSEDFFILLGFSNWPQLEVVLFVVILIFYLMTLTGNLFIIILSYVDSHLHTPMYFFLSNLSFLDLCHTTSSIPQLLVNLRGPEKTISYAGCMVQLYFVLALGIAECVLLVVMSYDRYVAVCRPLHYTVLMHPRFCHLLAAASWVIGFTISALHSSFTFWVPLCGHRLVDHFFCEVPALLRLSCVDTHANELTLMVMSSIFVLIPLILILTAYGAIARAVLSMQSTTGLQKVFRTCGAHLMVVSLFFIPVMCMYLQPPSENSPDQGKFIALFYTVVTPSLNPLIYTLRNKHVKGAAKRLLGWEWGK | Odorant receptor. | O76002 |
B9DMM3 | CH10_STACT | Chaperonin-10 | Staphylococcus | MLKPLGNRVIIKRVESEQTTKSGIVLTEKAKEKSNEGKVIAVGPGRLLDNGERVTPEVKEGDTVVFEQYAGSEVQVGEDKYLVISEEEVLAIVQ | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. | B9DMM3 |
Q45390 | PTLA_BORPE | Pertussis toxin liberation protein A | Bordetella | MNPLKDLRASLPRLAFMAACTLLSATLPDLAQAGGGLQRVNHFMASIVVVLRGASVATVTIAIIWAGYKLLFRHADVLDVVRVVLAGLLIGASAEIARYLLT | Component of the type IV secretion system ptl required for secretion of assembled pertussis toxin (PTX) through the outer membrane. | Q45390 |
O95988 | TCL1B_HUMAN | TCL1/MTCP1-like protein 1 | Homo | MASEASVRLGVPPGRLWIQRPGIYEDEEGRTWVTVVVRFNPSRREWARASQGSRYEPSITVHLWQMAVHTRELLSSGQMPFSQLPAVWQLYPGRKYRAADSSFWEIADHGQIDSMEQLVLTYQPERKD | Enhances the phosphorylation and activation of AKT1 and AKT2. | O95988 |
Q1LTC4 | RS8_BAUCH | 30S ribosomal protein S8 | Candidatus Baumannia | MSMQDPIADMLTRIRNGQTAHKTILFMPSSKLKVAIARLLQEEGFIKDYKVEGNIKKKPVLKIFLKYFQGKPVIENIQRISRPSLRIYRKKTALPNIMGGMGIAIISTSKGIMTDYTARQAGLGGEIICHVA | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | Q1LTC4 |
A4SF45 | NUOD_CHLPM | NDH-1 subunit D | Chlorobium | MQELEMAGQGSLRLSRKSDTIVVLEKDLSTEQMVLSMGPQHPSTHGVLRLECLTDGEVVTEAEPYLGYLHRCFEKHCEHVDYPAIVPYTDRMDYLAGINSEMAYCVAVEKLLDLEIPRRVEFIRVIVSELNRIASHLVAIGTYAIDLGAFTPFLFCFRDREHILNMLEWATGARMLYNYIWVGGLAYDVPAGFNERVLEFVNYFRPKALELQQLLTENEIFVKRTKGIGIMPADVAINYGWSGPMLRGSGVQWDIRRNDPYSIYPELDFAVPVPDGKLSVVGDCLSRHLVRALEIEESLKIIEQCIDKMPGTQGFDPRSAVPKRVRPKAGEVYGRAENPRGELGFYIQSDGKSTSPLRCKARSSCFVNLSAMKDLSRGQLIPDLVAIIGSLDIVLGEVDR | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | A4SF45 |
G5EDE9 | NFKI1_CAEEL | ANK repeat-containing protein nipk-1 | Caenorhabditis | MATVAPKGNCLVARAIPSDSHADQLTDLLCKLSVNGDANQKSVNKFESQHGVTPSDFRDIQNIRSSALAKKTKTSKFQLDGVTLFADLTPNSKSKKKTENQETKEKDEEAEEKKDGPPKDDKELKMKKEKEQEDENAELDEQKKDGDLLGRGPVHNVRVATGGSHPYHRAQIPYGCAAQTPITDISAYTGYGSGYECGSTWSLSPDTTIGSISASTTPDTVLSSDGYGSASPPQHSPKESLQSPFSDISSADTSRVLTPENNELPESLQDFILQYSNQYTKEESIRGRPPSADSGVSSPMSARSAPYASPHVPQGTCSGPTTPSFNQTRLSPRTSENGITAKQRLNAIIPESDLATGFHWACTTWKNVLTNRDADGDTPLHIVAAHNDLGKIYALCETLRKTMNENDDNVFNVSNNFGETPLYVAVLQRSIEVVEYLLELGASPNSRSSRAVGDSPLHFATARGMNNMVEALLSKREIRVNETNDDGQTSLLCAVKMHGMMDEQTQHKIDNKSIIEMLIKAGADPTIAETSTGKTIVHHAVDKMDVELLDFLKTVVNEDTFTELANLSDFHGDTAVDLLCSSTQNEDTNNVRENLYIRLLTSGAVPNKSRA | Acts downstream of the receptor complex composed of ilcr-1 and ilcr-2, which is a signaling complex that modulates neuronal activity and animal behavior in response to sensory neuron input. Mediates signaling of the complex. | G5EDE9 |
Q8S8S2 | LPCT2_ARATH | Lysophosphatidylethanolamine acyltransferase 2 | Arabidopsis | MADPDLSSPLIHHQSSDQPEVVISIADDDDDESGLNLLPAVVDPRVSRGFEFDHLNPYGFLSESEPPVLGPTTVDPFRNNTPGVSGLYEAIKLVICLPIALIRLVLFAASLAVGYLATKLALAGWKDKENPMPLWRCRIMWITRICTRCILFSFGYQWIRRKGKPARREIAPIVVSNHVSYIEPIFYFYELSPTIVASESHDSLPFVGTIIRAMQVIYVNRFSQTSRKNAVHEIKRKASCDRFPRLLLFPEGTTTNGKVLISFQLGAFIPGYPIQPVVVRYPHVHFDQSWGNISLLTLMFRMFTQFHNFMEVEYLPVIYPSEKQKQNAVRLSQKTSHAIATSLNVVQTSHSFADLMLLNKATELKLENPSNYMVEMARVESLFHVSSLEATRFLDTFVSMIPDSSGRVRLHDFLRGLKLKPCPLSKRIFEFIDVEKVGSITFKQFLFASGHVLTQPLFKQTCELAFSHCDADGDGYITIQELGEALKNTIPNLNKDEIRGMYHLLDDDQDQRISQNDLLSCLRRNPLLIAIFAPDLAPT | Possesses acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates . Exhibits strong acylation activity on lysophosphatidylethanolamine (LPE), and lower activity on lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS) . Exhibits acylation activity on both LPE and LPC . Has a preference for 18:1-LPE over 16:0-LPE as acceptor . Palmitoyl-CoA (16:0-CoA) is a better acyl donor than oleoyl-CoA (18:1-CoA) . Among several different acyl-CoA species the best acyl donor is eicosanoyl-CoA (20:0-CoA) . Activity is calcium-independent . Its activity is essential for maintaining adequate levels of phosphatidylethanolamine (PE), LPE and LPC in the cells, which is crucial for plant growth regulation . | Q8S8S2 |
Q6FSZ8 | OCA1_CANGA | Putative tyrosine-protein phosphatase OCA1 | Nakaseomyces/Candida clade | MDSPTLEDRENSIEDCDDDDDNIYINEETEEGHEKVLVTHAPQERIVPPLNFCPVERYLYRSGQPSPVNFPFLLNLNLKTIVWLANEEPQDSLLEFCDTHKINLQFAAINPDAGEDDNPWDGLTEHSIINVLQTIVTKENYPLLVCCGMGRHRTGTVIGCLRRIMGWNLASVSEEYRRFTGSRGGRILVELLIEAFDTALVEIDKKNAPDWLLTSLE | Putative tyrosine-protein phosphatase required for protection against superoxide stress. | Q6FSZ8 |
Q8NR40 | GLGB_CORGL | Glycogen branching enzyme | Corynebacterium | MTVDPASHITIPEADLARLRHCNHHDPHGFYGWHETEAGSVIRTRQVGATQVNLLIDDTSHVMTPIGDDIFAIDLGHRERADYRLEVTWPDQEPQVKADPYYFLPTVGEMDIYLFSEGRHERLWEILGANIKTYQTALGTVRGTAFTVWAPNAIGCAVVGGFNGWNASQHPMRSMGGSGLWELFIPGIEEGEVYKFAVQTREGQRRDKADPMARRAELAPATGSIVASSEYQWQDSEWLRERSQTDLASKPMSVYEVHLGSWRWGKNYEDLATELVDYVADLGYTHVEFLPVAEHPFGGSWGYQVTGYYAPTSRWGTPDQFRALVDAFHARGIGVIMDWVPAHFPKDDWALARFDGEALYEHPDWRRGEQKDWGTLVFDFGRNEVRNFLVANALYWIEEFHIDGLRVDAVASMLYLDYSREHGEWEPNIYGGRENLEAVQFLQEMNATVLRLHPGALTIAEESTSWPGVTAPTWDGGLGFSLKWNMGWMHDTLEYFSKNPVHRAFHHSELTFSLVYAFSERFVLPISHDEVVHGKGSLWDRMPGDTWNKAAGLRTFLAYMWSHPGKKLLFMGQEFGQREEWAEGQGLPWDIVDGWQGEYHEAIRTLTRSLNGVYSDSPALHTQDFTGEGFTWNKGDDATNNILAFTRFGSDGSQMLCVFNLSGTSQPEYQLGVAAGGEWKLVLNTDDAEFLGAENDIATSVQAAATPRDNFAYSLSLHVPAMSAQFYSLQK | Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. | Q8NR40 |
Q6FU50 | LHS1_CANGA | Heat shock protein 70 homolog LHS1 | Nakaseomyces/Candida clade | MKLSILFLFAIAVQAAFLGIDYGQQSIKAMVVSPKAMMEIVLTPEAKRKDTSGICIRNVNGVLERHYGNSIGSLVTRFPQNTAMHLRSLLGKSMNDKDTIESYLRENPGANLTSTTRNTIAITIDGVEYPVEQLVAMNLQEIIDRANQHIKETDTTGIDFVEQVGIAIPEQFNQAQRQALLDALALTSVKDEAVLVSDGLSVAIDYALKRPDLEINVPQYYIVFDVGTSAAKATLFSLTQPEDLSSPIKIEIGAFDSEATVGGSKFIAAIADIVEDKFLEKNTKITRKSLVENPRARAKIIQAAEKAKLVLSANNEAIISIESLVDDIDFRTTIARSEFQDIFEDNKHTVVKAIKGAIGNQLWDDNISLEDISGVILSGGSSRVPMVQEEIAKLVGEEKILKNVNADETVINGATLKGLKYFGSFKTKPLDITERSLFDYSVEMSGESSSKTVFEKGTKFPNESSILYKAPKKFGKELKFDLFESDTRILSNIVDTTVSSKNWTSACKKGQLYLNVTFDLDSNRVFKIKDITVLCDSDGNAKEEEFEFIDVINDVTKATDVMPLSNAEIRQLSNAITSWNRKDRERKRVQESLNVLEAELYDCRSFIEEFEEKLGEEEFETLKSFTAFVKEKLEYLEDNSADMSKKDIEKLVRETRSQRDTLSRFYNSLDAALGSKDFQKLVDTASKSIKKYKEIESKNLADLENKAEKFNVIGLNVTEKYNSILSKMSFSSIRRSSEENIKTLAGLIDEVNESIKSKAIDDESLENLIKTKLAFEELINTLDLENRQWTYQHQLVMKELKKMYNKKMKAIKKQEKQNENEENGDDEGDDEDETKTKKYLKEATSSGDSSTIKEEDSTGSNEAGNKGDEEDEEEEEDDSSAGNVFDDEL | Chaperone required for protein translocation and folding in the endoplasmic reticulum. | Q6FU50 |
Q6LX65 | LADH_METMP | Lactaldehyde dehydrogenase | Methanococcus | MFIDGKWIIREDIDVFDPYTLENIEKITALDREETKNAIEVTEKHKEIMKNLSPSKRYKILMKVAEHLSSKKDFFAKTISIDVGKPIKQSKIEVDRTLTALKLSAFYAKELRGETINSENGLIFTKKEPLGVIGAITPFNFPLNLATHKIGPAIATGNSVVLHPSSKAPIVAIYLTKIIEHVLKQMDIPRGVFNLATGNGEIVGDEISKNDNVNMVSFTGSVEVGESISKNAKMKKVTLELGGNNPMIVLKDSDIKLAAKSAVKSKFLNAGQVCISVGQVLVEEEVVETFTKYVIEETKKLILGNPLDKNTDIGPLISPESALRIENLIKQSVSEGGELLIGGNRQNSLISPAVINIDEENILSKIETFGPILPILTVKDSEEAVNIANNSKYGLQAGLFTNNINNAMKIADELEYGGIMINSSPTFRKDNMPFGGVKKSGLGREGIKYTVEEMSETKTVVIHNI | Involved in F420 biosynthesis through the oxidation of lactaldehyde to lactate. | Q6LX65 |
Q9FL59 | FTIP1_ARATH | FT-interacting protein 1 | Arabidopsis | MAAKDGAKSQEDYKLKDMKPELGERWPHGGQRGGTGWIGSERAASTYDLVEQMFYLYVRVVKAKDLPPNPVTSNCDPYVEVKIGNYKGKTKHFEKRTNPEWNQVFAFSKDKVQSSTVEVFVRDKEMVTRDEYIGKVVFDMREVPTRVPPDSPLAPQWYRLEDRRGESKKRGEVMVAVWLGTQADEAFPDAWHSDASSVQGEGVQSVRSKVYVSPKLWYLRVNVIEAQDVEPSDRSQPPQAFVKVQVGNQILKTKLCPNKTTNPMWNEDLVFVAAEPFEEQFFLTVENKVTPAKDEVMGRLISPLSVFEKRLDHRAVHSKWYNLEKFGFGALEGDKRHELKFSSRIHLRVCLEGGYHVMDESTLYISDVKPTARQLWKSPIGILEVGILSAQGLSPMKTKDGKATTDPYCVAKYGQKWVRTRTIIDSSSPKWNEQYTWEVYDPCTVITLGVFDNCHLGGSEKSNSGAKVDSRIGKVRIRLSTLEADRIYTHSYPLLVLQTKGLKKMGEVQLAVRFTCLSLAHMIYLYGHPLLPKMHYLHPFTVNQLDSLRYQAMSIVAARLSRAEPPLRKENVEYMLDVDSHMWSMRRSKANFFRIVSVFAGLIAMSKWLGDVCYWKNPLTTILFHVLFFILICYPELILPTTFLYMFLIGLWNFRFRPRHPAHMDTKVSWAEAASPDELDEEFDTFPTSKGQDVVKMRYDRLRSVAGRIQMVVGDIATQGERFQALLSWRDPRATCLFVIFCLVAAMILYVTPFKIIALAGGMFWMRHPKFRSKMPSAPSNFFRKLPSKADCML | Involved in the export of FT from the phloem companion cells to the sieve elements through the plasmodesmata. Regulates flowering time under long days. | Q9FL59 |
P15970 | TOG1B_AGEAP | Omega-agatoxin-1B | Agelenopsis | ERGLPEGAECDGNESDCKCAGAWIKCRCPPMWHING | Omega-agatoxin are antagonist of voltage-gated calcium channels. They block insect neuromuscular transmission presynaptically. This toxin is a blocker of L-type calcium channels (Cav/CACNA1). | P15970 |
P39573 | RS12_SACS2 | 30S ribosomal protein S12 | Saccharolobus | MVKSKSPKGIYAARKLRLKRLKFRRSQRKYKTKILKLKEKYDPLGGAPMARGIVLEKVGIESRQPNSAVRKCVRVQLVRNGRVVTAFVPGDGGVNFIDEHDEVIITGIGGTLGRSMGDLPGVRYKVIMVNGVSLDALYKGKKQKPVR | With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits. | P39573 |
B1YLN6 | GCST_EXIS2 | Glycine cleavage system T protein | Exiguobacterium | MSQTTLKRTPLFDIIAPTGKMVDFAGFEMPVLFSSIKEEHTAVRERVGMFDVSHMGELFVSGSDALAFLQQTLSNDISKIAIGQAQYNVLCQEDGGTVDDLLVYRLDEQDYLLVVNASNIEKDEAHLRQYLTGDVLLENQSDAYGQIAVQGPKAVEVLQELTALKLEDIKFFRFAQGELAGVEMLVSRSGYTGEDGFELYMPSADASAVWNALLEADVVPCGLGARDTLRFEACLPLYGHELSATISPIEAGMGFAVKPQVKSFVGSEVLVKQKEDGPRRQLIGLELTDKGIARQDAPVLVNGETIGFVTTGTLPPTIGKAIALALVPTEYATEETFEIEVRGKKLAAKRIDTPFYRRSK | The glycine cleavage system catalyzes the degradation of glycine. | B1YLN6 |
Q4QKJ8 | RS15_HAEI8 | 30S ribosomal protein S15 | Haemophilus | MSLSTEKKAAIVAEFGRDAKDTGSSEVQIALLTAQINHLQAHFAEHKKDHHGRRGLLRMVSRRRKLLDYLKRTDLALYQSTIARLGLRR | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | Q4QKJ8 |
Q7TUT0 | SYY_PROMM | Tyrosyl-tRNA synthetase | Prochlorococcus | MPETPITMPAWLQRGMVDLFPSGQWGDADQQLATRLDEAREQNRPLRVKLGIDPTGRDIHLGHSILFRKLRAFQDAGHTAVLIIGDFTARIGDPTGKSSTRVQLTSEQIEANATTYLAQLGQGQSAEKALLDFTTPGRLEVRRNTEWLADLDLPEVIGLLGTATVGQMLAKEDFGNRYGSGVPIALHEFLYPLLQGYDSVAVQADVELGGTDQKFNVAMGRDLQRHFDQRPQFGLLLPILAGLDGVQKMSKSLSNTVGLNEDPLSMYSKLEKVPDALVSSYVVLLTDLDPEALPVNPRERQKAMAIAVTASRHGIAAAEAAQNDAARLVSGSQDDAASVPEAFLSDVNFPAKAFYLLSAIGLCASSSEARRQIKGGAVRLDGEKITDPNLEFTDSSLLMGKVLQVGKKTFRRLTR | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | Q7TUT0 |
Q80TS7 | DEND_MOUSE | Dendrin | Mus | MLDGPLFSEGPDSPRELQDEESGSCLWVQKSKLLVIEVKTISCHYSRRAPSRQSMDIQASYWARGPQSRTCRLRPGSPEPPPRRPWASRVLQEATNWRAGPPAEVRAREQEKRKAASQEREAKETERKRRKAGGARRSPLGQPRPEPRNALRAAQPTGFPVFSRPERFGQVGRAPRPSVLPQGDPGVAWAGPWGGRRPGPPSYEAHLLLRGSAGTAPRRRWDRPPPYVAPPSYEGPHRTLGTKRGPELSRAPTSSAPVPATTRTEGGRTKKRLDPRIYRDVLGAWGLRQGRGLLGGAPGCTAARARPESCKGAIEKSSGLVAAGLNSAGDSHSQGKTTGGPGTDAALSRSAISSPPRPVPRSRQHLRGSRKGKEGSEQIWLPTCWLASPKKPPVRHSQTLPRPWAPGGTGWKESLGQREGAEHETLEVWKVTRRAHTLPRISRGPAGREGIFVIDATCVVIKSQYVPTPRTQQGQLVPSGESCSVSDSLSQPKPCHEEEGEGAAANPSVCQKRLLSSRVLNQPSEGRECEAEVGQQGDSSLEERSSSGLGFPVGEVNPRDAPTQPGSQEHPTLGPAAPVCAGSLKGSEAAGVPRRAGGGWARTPGPYAGALREAVSRIRRHTAPDSDSDEAEDLSVHSGSSDGSDTDAPGASWRNERTLPALGNTRPREGGKTAGLSDSIREIVDVISQTEEGFIREDTRKTPQGNRERE | Promotes apoptosis of kidney glomerular podocytes. Podocytes are highly specialized cells essential to the ultrafiltration of blood, resulting in the extraction of urine and the retention of protein. | Q80TS7 |
Q87S81 | MURQ1_VIBPA | N-acetylmuramic acid 6-phosphate lyase 1 | Vibrio | MTNDALIAALSHLVSEGRNPDTMDIDLLPSLDIVQRINQQDKLVPLAVEKVLPEIAQAVDKITDAFKVGGRLIYMGAGTSGRLGVLDASECPPTFGVSDKMVIGLIAGGPEAILKAKEGAEDSPQLGEQDLKAIDFSSNDVLVGIAASGRTPYVIGGLEYANTIGATTVALSCNPDSPIADIADIAISPVVGPEALTGSTRLKSGTAQKLVLNMLTTASMIRLGKSYQNLMVDVKATNNKLVARAARIVMQATECTKEEATEVLKQTNYEVKLAILMILTDLDIESARQHLHHQDGFLRKAVESHKSN | Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. | Q87S81 |
P0DO31 | ILIB_NEOS2 | Ilicicolin H biosynthesis cluster protein B | unclassified Neonectria | MALATPLPATQAAVKVTGPSTVDVSAATTLPVLEAFEVLVRVACVSINHVDGKSADMSPTPGATSGVDFSGLIVALGSKVDSDEFRANNNMRALSIGDRVFGGVFGNNPLRHDNGAFAEYVAVPARLIWHMPAAMDFSTAATIGATLATVGLALFQYLQVPMPSTQTISDSKTIPDPQQKTRMALVYGGGTATGAMAIQVLKLAGFRPITTCSPGSAARAMHLGAAATFDYRSPTCGADLREHTANGLELALDCITDTASMSICYEALGSAGGRYVALDAFPLRGHTRRSVAAEWVCTYTQFGHAVAWVPPYNLDARPRDREIAEAWYVVAQQLVDEGLIEPYPKEDRTGGLAAVGEGMRAVWKGEISGRKLAYPIAEECY | Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . IliB collaborates with the hybrid PKS-NRPS synthetase iliA to assemble the backbone of ilicicolin H . The PKS portion of iliA and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain of iliA during the chain assembly . The nascent chain is then condensed with tyrosine, catalyzed by the iliA C domain, and the resulting PKS-NRPS hybrid is offloaded by the iliA RED domain to form an advanced tetramic acid intermediate . The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable). | P0DO31 |
Q95YM9 | FGFR_HALRO | Fibroblast growth factor receptor | Halocynthia | MKEFEVKVASTAFVLVLFSLTINQILASETSTKFRSPVPAPTVPDWNHLPNEGNEENVVSAPKQDGASGGQKPYWTKREKMMKRLHAEPAGNTVRFRCAVDGNPKPQVLWYKNDLIVQKNDRVGGYKYRNQVLILESVVLSDKGNYMCVARNEYGSINHTYQLDVQERSASKPILAEGLPQNKSAYIGDDVTFKCKVYSDAHPHIQWLKSINNHNNAAPNYTVLKAAGVNTTDLDMEVLILKNVSFEEAGEYTCLAGNSIGISHQSAWLSVLPVPPPTTDTITKGIPNETNIIIYVMCGVLVILFGLAVVLVLYYHCYNGKDPPMLVRIENPDNIPPMTKIEHPTMLFGNTQAWQRMCMPMQEPFEFNIQLDLQWELQREDITLVERLDEGFFGQVFKADLVTCNNTRKEKMVCAVKMLKGNRNEKDVLDLLTEMDQMKRVGKHKNIINLLGVCTQNGPLWLVIEYAAQGNLRDYLRRNRPQNTLCNLVLPSEGRNPDDELPVPHGDTLTQKDIVSFAFQVARGLEFLAQKKCIHRDLAARNVLVTEELVMKIADFGLARDIRSCDYYRKHTRGHLPYKWMALEAMSDNIFTHATDVWSFGVLLWEIFSLAGSPYPGIKTHELVKFLRSGERLDKPQYASQEMYRLMRDCWEEDPSKRPNFRTLVEDLDRMLAESSTEVYIDFAAGCEAEYSESSEDESESQNSDEEDDDSVFERMRQIDSLSNGNIPFNEEDSSNSDPYVAPLLQNEENVLQNEHARLRSEA | Receptor for basic fibroblast growth factor. | Q95YM9 |
O27970 | OGT_ARCFU | O-6-methylguanine-DNA-alkyltransferase | Archaeoglobus | MFSVKWGELYFNVVMEGGKAVKSYFSTYPSFSSSDSEYARQLERYFSGERVEVRIPYRLKASSFTRRVLEEVSRIPYGMVRMYSDIAKALNTSPRAVGQAVKRNPLPVIIPCHRVVGKKEIGGYTVSCSDIDGKSLKKRLLRLEGVF | Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | O27970 |
P46925 | PLM2_PLAFX | Plasmepsin 2 | Plasmodium (Laverania) | MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL | During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation . May cleave preferentially denatured hemoglobin that has been cleaved by PMI . Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). | P46925 |
O67908 | PGSA_AQUAE | Phosphatidylglycerophosphate synthase | Aquifex | MNVPNLLSLSRLILSPLILYFVLEENYLSSLVLVLFLALMDFLDGFFARKLNQSTRMGKILDPLADKVFTFFSLLSYTFFSKERLNPLIFFLLLGRDITLIIGGIFLIKRKFTPEPSIYGKFTTLFVSLSLLSVGILNVYDVNFLRILTNVLEIVSLILILVSWVDYTLKGFKMIFKE | This protein catalyzes the committed step to the synthesis of the acidic phospholipids. | O67908 |
Q1MLL4 | GDH_RHIL3 | RlGDH | Rhizobium | MSYQQKFRLDGERAVVTGGGRAIGLCCTEALAEAGAAVVVIERSEADAEQALALRNRGYDVEVRVGDVTDAARMDAIATELADGGRPATILVNNAGIGQSGIPAQDLTDADWLRMMDVNLNGVFWCSRAFGRSMISMKRGAIVNLGSMSGTICNRPQPQTAYNVSKAAVHHLTRSLAAEWAHHGIRVNAVAPTYIETPMVVAVEANRERIPLWLADTPMARMGTPEEVASAVLFLASGAASLMTGAIVNVDAGFTCW | Catalyzes the oxidation of galactitol to D-tagatose. Also catalyzes the oxidation of a wide range of substrates, including polyvalent aliphatic alcohols and polyols, to the corresponding ketones and ketoses. Galactitol is the preferred substrate. | Q1MLL4 |
Q601K7 | RL16_MESH2 | 50S ribosomal protein L16 | Mesomycoplasma | MLQPKKTKHRKTFRLYHDKRDAHSGNFVAFGDYGLQATGSAWVSAAQIEAARIAITRRMGREGQVIIRVFPHLALTSKPIGVRMGSGKGSVDRWVAVVKRNTILFEVRGVKDEIARDALRLGGHKLPLKWKIVATV | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q601K7 |
Q0MQF7 | NDUC2_PONPY | NADH-ubiquinone oxidoreductase subunit B14.5b | Pongo | MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYLGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFFAGYYLVKRENYLYAVRDREMFGYMKLHPEEFPEEEKKTYGEIFEKFHPVH | Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. | Q0MQF7 |
Q76LB1 | ALMT1_WHEAT | Aluminum-activated malate transporter 1 | Triticum | MDIDHGRESDGEMVGTIASCGLLLHSLLAGLGRRAAGFARKVGGAAREDPRRVAHSLKVGLALALVSVVYFVTPLFNGLGVSAIWAVLTVVVVMEYTVGATLSKGLNRALATLVAGCIAVGAHQLAELAERCGDQGEPIVLTVLVFFVASAATFLRFIPEIKAKYDYGVTIFILTFGLVAVSSYRVEELIQLAHQRFYTIAVGVFICLCTTVFLFPVWAGEDVHKLASGNLDKLAQFIEGMEFNCFGENSVANNFGGKDSPQMHKSVLNSKATEDSLCTFAKWEPRHGQFRFRHPWSQYQKLGTLCRQCASSMEALASYVITTSKTQCPAAANPELSCKVRKTCGEMSLHSSKVLRDLAMATRTMTVPSPVNITMATAVKAAESLRSELAENTALLQVMHVAVTATLLADLVDRVKEIAECVDVLARLAHFKNPEDTKNVVVSTVSRGIDEPLPDVVIL | Malate transporter critical for aluminum tolerance. Permeable to chloride, nitrate, sulfate and malate. | Q76LB1 |
Q927W9 | FABZ_LISIN | Beta-hydroxyacyl-ACP dehydratase | Listeria | MLDIKKIKEILPHRYPFLLVDRVISVEEGKKVTAIKNVTANEEFFNGHFPEYPVMPGVLIVEALAQTSGIAMMQSEANKGKIGLFAGIDGCRFKRQVVPGDQLLLEAEITRMRGAIAKAKVKATVEGDLVCEAEIMFALSDLPQ | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | Q927W9 |
Q134R4 | RL1_RHOPS | 50S ribosomal protein L1 | Rhodopseudomonas | MAIGKRLKKAREGVDRTKLYPLDEAVKMVKERATSKFDETIEVALNLGVDPRHADQMVRGVVMLPNGTGRTLRVGVFARGAKADEAKAAGADVVGAEDLVEQVQGGNINFDRCIATPDMMPLVGRLGKVLGPRGMMPNPKIGTVTMDVAGAVKGAKGGSVEFRVEKAGIVQAGVGKASFTEEKLVENIKALADAVTKAKPTGAKGTYIQRVAVSSSMGPGVKVEPGSIH | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | Q134R4 |
C5BHJ4 | DEOB_EDWI9 | Phosphodeoxyribomutase | Edwardsiella | MKRAFIMVLDSFGIGEAKDAKSFGDEGADTLGHIARACARGEADIGRQGPLHLPNLSRLGLGKAALESTGRFPEGLDENAEVIGAYGYANELSSGKDTPSGHWEIAGVPVLFDWGYFHEHQNSFPQALLDTLVERANLPGYLGNCHSSGTVILDQLGEEHMKSGKPIFYTSADSVFQIACHEETFGLERLYELCEIARDELNKGGYNIGRVIARPFVGDKAGHFQRTGNRHDLAVEPPAPTMLKKLVDEKQGDVVSIGKIADIYANVGITKKVKATGIDALFDATLQEMRQAGNDTIVFTNFVDFDSSYGHRRDVAGYAAALELFDRRLPEMLALVKEDDILILTADHGCDPTWHGSDHTREHIPVLVYGPKVKPGSLGERDTFADIGQTVARYFGLSPMAYGKPMF | Phosphotransfer between the C1 and C5 carbon atoms of pentose. | C5BHJ4 |
Q5V3T2 | MEND_HALMA | Menaquinone biosynthesis protein MenD | Haloarcula | MTAPNVNTLWAETLVGELVAGGVDAVCLSPGSRSTPLTVAFAEHPDIEVFSHLDERSAAFFALGRARRTGEPTPLVCTSGTAAANYHPAVIEANQSGVPLLLLTADRPPELIDSGANQTVDQEKLYGDAVRWYRDMPEPEAEPRKVRMLRTTAARALAESTGSDPGPVHLNCRFRKPLEPTPMPEDDPAGVPADWAGGDNGAKIGRDGPFVTTSEGVETPDEQTVRRVQDALEAAERGLIVAGPADQGLSADSLERLAAATGFPVLADPLSDLRFGPHVDRLDVPVCGGYDGYLGSDSVDQWDDPDVVVRFGASPTSKPLRHYLRDADCQQFLVDPAGGWSEAEFTATNLLVANPDATADALAGETLGGVAASWREQFIRAEQTHWDAVTETASETYWEGGVLSDVTALAPDPATLFISNSMPIRDMDRFGGPRDADLTVLGNRGASGIDGITSTALGAGSATSDPLVLVTGDLAYYHDMNGLLALGRCAVDATVVLLNNDGGGIFHMLPIEDHPTFEDQFRTPHGLDFEPTEALYSLQFERVADRRQFRERFAESVQTDGTQVIEVRFDAGDSHAVRDQLTEQVAETLAGD | Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). | Q5V3T2 |
Q8LWS1 | NU4LM_ODORR | NADH dehydrogenase subunit 4L | Odobenus | MSMVYANIFMAFVVSLMGMLVYRSHLMSSLLCLEGMMLSLFVMMSVTILNNHFTLANMAPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. | Q8LWS1 |
A6T3I9 | RL6_JANMA | 50S ribosomal protein L6 | Janthinobacterium | MSRVGKMPIALPSGAEATITAAQITVKGPLGSLTQSLNGLVNIENDNGTLNFKVANDSREANAMSGTLRALVNNMVNGVTKGFEKKLTLVGVGYRAAAQGDKLNLSLGFSHPVVHQMPQGVKVETPTQTEILIKGIDRQKVGQVAAEVRAYREPEPYKGKGVRYSDEVVVIKETKKK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | A6T3I9 |
Q9HGE0 | FUM6_GIBM7 | NADPH--cytochrome P450 reductase | Fusarium fujikuroi species complex | MSATALFTRRSVSTSNPELRPIPGPKPLPLLGNLFDFDFDNLTKSLGELGKIHGPIYSITFGASTEIMVTSREIAQELCDETRFCKLPGGALDVMKAVVGDGLFTAETSNPKWAIAHRIITPLFGAMRIRGMFDDMKDICEQMCLRWARFGPDEPLNVCDNMTKLTLDTIALCTIDYRFNSFYRENGAAHPFAEAVVDVMTESFDQSNLPDFVNNYVRFRAMAKFKRQAAELRRQTEELIAARRQNPVDRDDLLNAMLSAKDPKTGEGLSPESIVDNLLTFLIAGHETTSSLLSFCFYYLLENPHVLRRVQQEVDTVVGSDTITVDHLSSMPYLEAVLRETLRLRDPGPGFYVKPLKDEVVAGKYAVNKDQPLFIVFDSVHRDQSTYGADADEFRPERMLKDGFDKLPPCAWKPFGNGVRACVGRPFAMQQAILAVAMVLHKFDLVKDESYTLKYHVTMTVRPVGFTMKVRLRQGQRATDLAMGLHRGHSQEASAAASPSRASLKRLSSDVNGDDTDHKSQIAVLYASNSGSCEALAYRLAAEATERGFGIRAVDVVNNAIDRIPVGSPVILITASYNGEPADDAQEFVPWLKSLESGRLNGVKFAVFGNGHRDWANTLFAVPRLIDSELARCGAERVSLMGVSDTCDSSDPFSDFERWIDEKLFPELETPHGPGGVKNGDRAVPRQELQVSLGQPPRITMRKGYVRAIVTEARSLSSPGVPEKRHLELLLPKDFNYKAGDHVYILPRNSPRDVVRALSYFGLGEDTLITIRNTARKLSLGLPLDTPITATDLLGAYVELGRTASLKNLWTLVDAAGHGSRAALLSLTEPERFRAEVQDRHVSILDLLERFPDIDLSLSCFLPMLAQIRPRAYSFSSAPDWKPGHATLTYTVVDFATPATQGINGSSKSKAVGDGTAVVQRQGLASSYLSSLGPGTSLYVSLHRASPYFCLQKSTSLPVIMVGAGTGLAPFRAFLQERRMAAEGAKQRFGPALLFFGCRGPRLDSLYSVELEAYETIGLVQVRRAYSRDPSAQDAQGCKYVTDRLGKCRDEVARLWMDGAQVLVCGGKKMANDVLEVLGPMLLEIDQKRGETTAKTVVEWRARLDKSRYVEEVYV | Bifunctional cytochrome P450/NADPH--P450 reductase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins . On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls . The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine . The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain . This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 . The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 . Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins . The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis . The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis . Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 . The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria . If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone . Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond . In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification . | Q9HGE0 |
P0C2S8 | TX90D_PHONI | Neurotoxin Pn3-6B | Phoneutria | MKYRIFKMKYTLLFLSVIALVHIFAVEAKDEPESDALVPQERGCLDIGKTCKDDCECCGCGNVCYCPFDWFGGKWQPFGCSCAYGLKYVCAHKQKKCPNV | Probable neurotoxin. | P0C2S8 |
P18858 | DNLI1_HUMAN | Polydeoxyribonucleotide synthase [ATP] 1 | Homo | MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIEEVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSASTAKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPLKPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSAVWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQSQIQNQQGEDSGSDPEDTY | DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. | P18858 |
Q02SH1 | RLMH_PSEAB | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Pseudomonas | MRLRLIAVGSRMPRWVEEGWQEYVKRLPAELSLELVEIPLNTRGKNADVARLIRQEGEAMLARVQPGERVVTLEVEGRLWSTEQLARELDRWRLDARTVNLMVGGPEGLAPEVCARSEQRWSLSPLTLPHPLVRILVGEQIYRAWTVLSGHPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | Q02SH1 |
A6MM86 | CCSA_BUXMI | Cytochrome c biogenesis protein CcsA | Buxus | MIFLTLEHILTHISFSIVSIVITIHLITLLVDEIVGLYDSLEKGMISTFLCITGLLVTRWIYSGHLPLSNLYESLIFLSWSFSIIHMIPYFKNHKNHLSLVTAPSAIFTQGFATSGLLTEMHQSAILVPALQSQWLMMHVSMMVLSYGALLCGSLLSVALLVITFRKNIDIFGKRNHLLIGSFSFGEIQYTNERSNVLRNVSFLSLRNYRRYQLIRQLDNWSYRVISLGFIFLTIGILSGAVWANEAWGSYWNWDPKETWAFITWTIFAIYLHTRTNKNFQGADSAIVASIGFIIIWICYFGVNLLGIGLHSYGSFILTSN | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. | A6MM86 |
B1WSL8 | HIS1_CROS5 | ATP phosphoribosyltransferase | Crocosphaera subtropica | MITIALPKGALLSDSIELFKRIGLDFSSFLDSKNRQLQIIDPTNTAQGLLVRATDVPVYVEYGQAQLGIVGYDLLLEKSPDVAHLADLNFGGCRMSVAVPKTSPYQTPAELPPNGKVASKFVNCAKTYFQQLDLPVEIIPLYGSVELGPITGMSEAIVDLVSTGRTLKENGLVEVETLFHSTARLIAHPLSYRLNLDNLNDLSEQIKNSVSKS | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. | B1WSL8 |
B8JEX6 | PLSX_ANAD2 | Phosphate-acyl-ACP acyltransferase | Anaeromyxobacter | MVGKIAPIAVDAMGGDHAPGAIVQGAVNAARKGLPVVLVGPEARVREELARHRAASSLPLEVHPATEVVEMHDHPGQAMRRKKDNSIRVCFDLVASGRAAGMVSAGNSGAVMAGAILVLGRPEGVERPAIVSVLPALKGAPLMLDMGAVVDCRPIHLVQFALMGEVYSRRVHGVTRPRVAILSNGEEDTKGTDLTRAAAAALRRAPIDFVGYCEGRDLLTGEVDVIVTDGFTGNVALKTMEGTAKVVGEYLKRALRSTTVSKIGGLLSRAALEGMKKRIDWREVGGAPLVGVNGVGFISHGRSDALAIENAIRRAGDAARTHFIDEIARAVAPSHALLEVPADGAATEQGPTPRRIAPPRT | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | B8JEX6 |
A3MYF1 | GLPE_ACTP2 | Thiosulfate sulfurtransferase GlpE | Actinobacillus | MSETFTEISPHQAWELIENEGATLADIRDGRRYAYSHPQDAFHLTNESYGRFLDEVDYEEPVIVMCYHGVSSRNTAQFLVEQGFDRVYSVKGGFDGWERSGLPIETAY | Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. | A3MYF1 |
Q5KQI6 | SNAT1_ORYSJ | Nuclear shuttle protein-interacting protein homolog | Oryza sativa | MAPAASASASAVVTPSSFRCVPTASCGLGARGKAPAPRRLLHDHAQGKKRAAATWSLKAGLWDSLRSGFLKSNNSTETVEPPSAPIEEEEPLPEELVLLERTLADGSTEQIIFSSAGDVNVYDLQALCDKVGWPRRPLTKIAASLRNSYLVATLHSVTMPSKAEGEERKQLIGMARATSDHAFNATIWDVLVDPSYQGQGLGKALMEKVIRTLLQRDISNITLFADNKVVDFYKNLGFEADPQGIKGMFWYPRF | Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin . Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine . | Q5KQI6 |
A5W985 | TRUB_PSEP1 | tRNA-uridine isomerase | Pseudomonas | MAQVKRIRRNISGIILLDKPLGFTSNAALQKVRWLLNAEKAGHTGSLDPLATGVLPLCFGEATKFSQYLLDSDKGYETVMQMGQTTNTGDAEGEVLQTRDVTVGRADIEALLPRFRGPISQIPPMYSALKRDGQPLYKLARAGEVVEREARSVTINRLELLECEGTRARLSVGCSKGTYIRTLVEDIGEALGCGAYVAELRRTQAGPFALAQTVTLEELEQAHAEGGNEALDRFLMPSDSGLQDWPLVSLSEHSAFYWLHGQAVRAPDAPQFGMVRVQDHNARFIGIGEVSEDGRIAPRRLIRSE | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A5W985 |
C6DCE7 | TOLB_PECCP | Tol-Pal system protein TolB | Pectobacterium | MKHVLKVAVSFLMLWAAVLHAEVRIEITQGVDSARPIGVVPFKWAGPGAAPEDVGGIVGADLRNSGKFNPIDANRMPQQPATASEVTPAAWTALGIDAVVVGQVQPSADGSYLVSYQLVDTSGNPGNVLAQNQFKVTKQWLRYAAHTASDEVFEKLSGIKGAFRTRIAYVVQTNGGQFPYELRVADYDGYNQFVVHRSPQPLMSPAWSADGSKLAYVTFESGRSALVIQTLANGAIRQVASFPRHNGAPSFSPDGSKLAFALSKSGSLNLYVMNLASGQISQVTDGRSNNTEPTWFPDSQTLAYTSDQAGRPQVYKVNANGGAPQRLTWEGAQNQDADVSADGKFLVTVGSNGGAQHISKLDLVTGAVQVLTDTFLDETPSIAPNGTMVIYSSKQGLGSVLQLVSTDGRFKARLPATDGQVKFPAWSPYL | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. | C6DCE7 |
C1D5X9 | FOLD_LARHH | Methenyltetrahydrofolate cyclohydrolase | Laribacter | MTAQLIDGKTISAALLDRVAAGVKARTEAGKRAPALAVILVGNNPASEVYVRNKKKGCEKAGIQSLAYDLPESTSEADLLALVDELNARSDVDGILVQLPLPRHINPETVIERINPKKDVDGFHPYNMGRLAVKMPLLRPCTPRGVMIMLEHAGISVEGKHAVVIGQSNIVGRPMALELLMERATVTICHSRTRDLPEEVKRADIIVAAVGIPRFVKGDWVKPGAVVIDVGINRLEDGKLCGDVDFDAAKEHASWITPVPGGVGLMTVATLLANTLDAANLHA | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | C1D5X9 |
Q13VF6 | RSGA_PARXL | Small ribosomal subunit biogenesis GTPase RsgA | Paraburkholderia | MSGRSPKAPRAPSSTRAGGLVVAAHGRHYLVAPDDGGAMLQCFPRGKRSEVAVGDHVIYELASADQGVIVEIGERRNLLYRSDQYKSKLFAANLDQLLIVLATEPHFSEDLLGRALVAAEANGLKPLIVLNKTDVTDELEGARKRLEPYRALGYTVVEVSIRTQPEAARAALIERLHGHSTLLLGQSGMGKSTLVNLLIPDAEVATREISTALNSGRHTTTFTRLYPLPDSADGTGGSLIDSPGFQEFGLHHLTEGRLERAFPEFRPLLPNCRFYNCHHLHEPGCAILEAVADGRIRRERHALYAQLVHEASQIVR | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit. | Q13VF6 |
A2QA27 | XYND_ASPNC | Xylobiase xlnD | Aspergillus subgen. Circumdati | MAHSMSRPVAATAAALLALALPQALAQANTSYVDYNIEANPDLYPLCIETIPLSFPDCQNGPLRSHLICDETATPYDRAASLISLFTLDELIANTGNTGLGVSRLGLPAYQVWSEALHGLDRANFSDSGAYNWATSFPQPILTTAALNRTLIHQIASIISTQGRAFNNAGRYGLDVYAPNINTFRHPVWGRGQETPGEDVSLAAVYAYEYITGIQGPDPESNLKLAATAKHYAGYDIENWHNHSRLGNDMNITQQDLSEYYTPQFHVAARDAKVQSVMCAYNAVNGVPACADSYFLQTLLRDTFGFVDHGYVSSDCDAAYNIYNPHGYASSQAAAAAEAILAGTDIDCGTTYQWHLNESIAAGDLSRDDIEQGVIRLYTTLVQAGYFDSNTTKANNPYRDLSWSDVLETDAWNISYQAATQGIVLLKNSNNVLPLTEKAYPPSNTTVALIGPWANATTQLLGNYYGNAPYMISPRAAFEEAGYKVNFAEGTGISSTSTSGFAAALSAAQSADVIIYAGGIDNTLEAEALDRESIAWPGNQLDLIQKLASAAGKKPLIVLQMGGGQVDSSSLKNNTNVSALLWGGYPGQSGGFALRDIITGKKNPAGRLVTTQYPASYAEEFPATDMNLRPEGDNPGQTYKWYTGEAVYEFGHGLFYTTFAESSSNTTTKEVKLNIQDILSQTHEDLASITQLPVLNFTANIRNTGKLESDYTAMVFANTSDAGPAPYPKKWLVGWDRLGEVKVGETRELRVPVEVGSFARVNEDGDWVVFPGTFELALNLERKVRVKVVLEGEEEVVLKWPGKE | Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. | A2QA27 |
Q8KA03 | RL25_BUCAP | 50S ribosomal protein L25 | Buchnera | MFIVKAEIRDKKGKSFSRKLRIEDKFPGVLYGFNNTPISITMDHNLVFNLQKKEDFYKETLCLLIKEKKYTVKVHAIQRHAFKMKILHIDFIYAKI | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. | Q8KA03 |
Q2YVU6 | GLMU_STAAB | Glucosamine-1-phosphate N-acetyltransferase | Staphylococcus | MRRHAIILAAGKGTRMKSKKYKVLHEVAGKPMVEHVLESVKGSGVDQVVTIVGHGAESVKGHLGERSLYSFQEEQLGTAHAVQMAKSHLEDKKGTTIVVCGDTPLITKETLETLIAHHEDANAQATVLSASIQQPYGYGRIVRNASGRLDRIVEEKDATQAEKDINEISSGIFAFNNKTLFEKLTQVKNDNAQGEYYLPDVLSLILNDGGIVEVYRTNDVEEIMGVNDRVMLSQAEKAMQRRTNHYHMLNGVTIIDPDSTFIGPDVIIGSDTVIEPGVRINGRTEIGEDVVIGQYSEINNSTIENGACIQQSVVNDASVGANTKVGPFAQLRPGAQLGADVKVGNFVEIKKADLKDGAKVSHLSYIGDAVIGERTNIGCGTITVNYDGENKFITIVGKDSFVGCNVNLVAPVTIGDDVLVAAGSTITDDVPNDSLAVARARQTTKEGYRK | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. | Q2YVU6 |
B2A2U8 | PYRR_NATTJ | Uracil phosphoribosyltransferase | Natranaerobius | MVQEKAEIMDQEKFNRTLTRISHEIIEKNKGIDDLVLIGIRTRGVPLAERLAHKIEEIEGESIATGLLDITLYRDDLSTLSEKPILNKTEVPFSIKNKKVVLVDDVLYTGRTARAALDAVIDLGRPKYIQLAVIVDRGHRELPIRADYVGKNVPTSKKELISVRLSEIDGEDRVMIEETVKE | Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. | B2A2U8 |
A4WGE6 | MNMG_ENT38 | Glucose-inhibited division protein A | Enterobacter | MFYQDPFDVIIIGGGHAGTEAAMAAARMGQQTLLLTHNIDTLGQMSCNPAIGGIGKGHLVKEVDALGGLMAKAIDHAGIQFRILNASKGPAVRATRAQADRVLYRQAVRTALENQPNLMIFQQAVEDLIVENDRVVGAVTQMGLKFRAKAVVLTVGTFLDGKIHIGLDNYSGGRAGDPPSISLSRRLRELPLRVNRLKTGTPPRIDARTIDFSVLAQQHGDTPIPVFSFMGNAAQHPQQVPCYITHTNEKTHDVIRNNLDRSPMYAGVIEGIGPRYCPSIEDKVMRFADRNQHQIFLEPEGLTSNEIYPNGISTSLPFDVQIQIVRSMQGMENAKIVRPGYAIEYDFFDPRDLKPTLESKFIQGLFFAGQINGTTGYEEAAAQGLLAGLNAARFSAEKEGWAPRRDQAYLGVLVDDLSTMGTKEPYRMFTSRAEYRLMLREDNADLRLTEMGRELGLVDDERWARFNEKLERIETERQRLKSTWVNPLADSVAEVNAHLAAPLSREASGEDLLRRPGMTYEQLVQMTPFAPGLDDAEAAEQVEIQIKYEGYIARQQDEIEKQQRNENTLLPEMLDYRQVTGLSNEVIAKLNDHKPVSIGQASRISGVTPAAISILLVWLKKQGMLRRSA | NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | A4WGE6 |
Q0HYN8 | MODC_SHESR | Molybdenum import ATP-binding protein ModC | Shewanella | MLNINIEKQLGQLQLKVNTQLPLQGVTAVFGRSGAGKTSLVNLLGGLTTPDKGEISLGDTLLFKHKTVNLPPEKRRIGYVFQEARLFPHYSVNGNLTYGMRHKTPELFDKVVSLLGIEKLLSRYPSTLSGGEKQRVAIGRALLTSPQMLLMDEPLASLDLPRKRELLPYLQTLAQELKLPIVYVSHSLDEILQLADHMLVLHQGKMIAQGPLTQVWNSEQMRPWVPLQELSSLLSARIADRHPDYPMTRLLMDDGNQLWVSGQLPPTHKQLKVRIQANHVSVCTEEPKGSSVRNLLRGKIKELYPSDNGEQIQLKIALGKDELWANITPWARDELQLIPGKAIYAQIKGVTMTQMDIAESH | Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. | Q0HYN8 |
B6JGH2 | BPT_AFIC5 | Aspartate/glutamate leucyltransferase | Afipia | MTQHSRNTPQFYLTAPTPCPYLEGFQERKVFTHLVGDKAGELNDLLTHGGFRRSQSIAYRPACDLCRACVSVRVIAGEFEPSRNLRKVLHRNADLVGEMRNAVPTSEQYSIFRAYLDARHHDGGMADMTVLDYAMMVEDTHVTTRIVEYRRRTDSGKQGGELVAAALTDVLGDGLSMVYSFFDPDVDDRSLGTFMILDHIARARSMGLPYVYLGYWIEGSSKMSYKARFLPQQRLSPNGWLRVDATGIATQD | Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate. | B6JGH2 |
A0L4K5 | PIMT_MAGMM | Protein-beta-aspartate methyltransferase | Magnetococcus | MVAVSLKMSQPAAPPPPMGERARTRMLLALQSRGIHDPRVLEVMGALPRHDFVDEALAGHAYGDATLPIGEGQTLSQPYTVARMSQALELGYGMHVLEIGTGSGYQTAVLAALCRRVYTVERIPSLALLARERLERMGITNVRYRVGDGTLGWPEPRPFERIIVTAGAPATPERLKRQLEIGGRMIIPEGGKLNQQLICIQRTGPESWQRDVLEACRFVPLVGQQGWE | Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. | A0L4K5 |
A0LGB7 | SSRP_SYNFM | Small protein B | Syntrophobacter | MTKNKPSTAEKTRLICQNKKAYHDYDILEKFEAGIVLLGTEVKSLREGRANLKDSYARVRKGEVFLQGLHISPYTHASYNNHEPERVRKLLLHAHEIKRLTGKTQERGLALIPLKLYFSKGKVKVELALAQGKKLYDKRESIKRKEENRELDRLRKRRRQE | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. | A0LGB7 |
Q3AGP0 | NDK_SYNSC | Nucleoside-2-P kinase | unclassified Synechococcus | MAERTFIAIKPDGVQRGLVGEILGRFERKGFKLVGLKQITPSRALAEQHYGVHKERPFFAGLVDFITSGPVVAMVWEGDGVIASARKLIGATKPLEAEPGTIRGDLAVNIGRNVIHGSDAAETAQFEIGLWFQASELNDWSPSDQGWRVEG | (Microbial infection) Catalyzes the phosphorylation of dZDP to dZTP, when the bacterium is infected by a phage that produces the substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'-triphosphate), which is then used by the phage as a DNA polymerase substrate. | Q3AGP0 |
A2Q908 | EIF3B_ASPNC | Translation initiation factor eIF3 p90 subunit homolog | Aspergillus subgen. Circumdati | MAPSFDTLTEQDLHEEEEEEIDFSDLKEQYEVKLEEGLDTFVVIDGLPVVPEESRQKLIKFLLRKLNTVGHTSEDAVFMPLNDKNMSEGFAFVEYETPEQAIAAVKQLHGVPLDKKHTLAVNKLMDIDRYGREGRIDEEYKPPTIEPFKEKEHLRSWLGDANARDQFALYRGDKVGVFWNNKSNPPENVVDRAHWTQLFVQWSPKGTYLASVHPQGVQLWGGPAFSKQKQFPHPFVQLVEFSPGESYLTTWSARPIQVEEGHPVLTYEEDGKNIIIWDIVTGKPLRSFVSHDLTAGPGGDGEPKKKVQWPAFKWSADEKYVARMQQHQSISIYELPRMNLLGKTSVKIDGVMDFEWSPATVVREGVKQYEQLLCFWTPEIGSNPARVALMSVPSKEIVRTRNLFNVSDVKLHWQSQGTYVCVKVDRHSKSKKSMATNLEIFRVREKGVPVEVVDSLKDTVINFAWEPNGGRFVAITTGEAPSGAAVLPKTSVSFFAPEKKGVSAGNFKVVRTIEKKTSNAIYWSPKGRFVVVATVHSQTNFDIDFWDMDFEGEKPEGEKDLAANLQLMKTVEHYGVTDIDWDPTGRYVVSSASVWTHSMENGYNIHTFAGQTLAEHPTDKFKQFIWRPRPPTLLSKEEQKQVRKNLREYSKEFDEEDKYAVDIANTAVVETRKRVLNEWAAWIRREKEMLAEEKDAYGVPEDVDSSKQAKDAPAVSEDQGETVVEEIVEEIIEENEEVIG | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. | A2Q908 |
Q71NV7 | PSBN_LEUSC | Protein PsbN | Leucodon | METATLVAIFISCSLVSFTGYALYTAFGQPSKELRDPFEEHED | May play a role in photosystem I and II biogenesis. | Q71NV7 |
P60666 | HIS6_MYCPA | ImGP synthase subunit HisF | Mycobacterium avium complex (MAC) | MSPNSTGLAVRVIPCLDVDDGRVVKGVNFENLRDAGDPVELAAVYDAEGADELTFLDVTASSSGRATMLDVVRRTAEQVFIPLTVGGGVRTVADVDVLLRAGADKVSVNTAAIARPELLEEMARQFGSQCIVLSVDARTVPPGAVPTPSGWEVTTHGGRRGTGIDAVEWASRGADLGVGEILLNSMDADGTKAGFDLEMLQAVRSAVTVPVIASGGAGAAEHFAPAIEAGADAVLAASVFHFRELTIGQVKAAMAEAGIPVRMVR | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | P60666 |
Q325X3 | GLND_SHIBS | [Protein-PII]-UMP uridylyl-removing enzyme | Shigella | MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG | Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | Q325X3 |
A5UFI6 | RSMC_HAEIG | rRNA (guanine-N(2)-)-methyltransferase RsmC | Haemophilus | MISLESQVLERHLSFFDGKSVLFAGGISDNFPQTLASKCSSIQIWSCYFDYARTQSAVNFSVEFQGQADLIVYYWTKNKQEVNFQLLQLLAQASIGQEILIIGENRCGVRSVEKTLAPYGEIAKIDSARRCGLYHFSLQNKPHFELKNFWRTYQHSTLENLTIYSLPGVFSAAELDTGTELLLSTIDNKIKGKVLDLGCGAGVIGSMIKKRAPNAQITMTDIHAMALESARKTLSENQLQGEVYASDVFSDIEGKFDLIISNPPFHDGIDTAYRTVKELITQAKWHLNQGGELRIVANAFLPYPELLRQYFNDYQVLAQTGKFKVYSVKN | Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle. | A5UFI6 |
A3Q0T7 | ARGB_MYCSJ | NAG kinase | unclassified Mycobacterium | MTAATHTKAQVLAAALPWLKQLHGKIVVVKYGGNAMTDDTLKAAFAADMVFLRNCGVHPVVVHGGGPQISAMLKRLGIPGDFRGGFRVTTPEVLDVARMVLFGQVGRELVGLINAHGPYAVGITGEDAHLFTAVRRDVMVDGVATDIGLVGDVEHVNTEAVRDLIAAGRIPVVSTIAPDANGVVHNINADTAAAALAAALSAEKLLMLTDIEGLYTDWPDRNSLVSQINTADLTELLPTLEAGMVPKIEACLRAVTEGVPSAHVIDGRVEHCVLVELFTDEGTGTKVVNP | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | A3Q0T7 |
F4HX80 | ALT4_ARATH | Acyl-lipid thioesterase 4 | Arabidopsis | MIRVTGTAAPAMSVVFPTSWRQPVMLPLRSAKTFKPHTFLDLKGGKEMSEFHEVELKVRDYELDQFGVVNNAVYANYCQHGMHEFLESIGINCDEVARSGEALAISELTMNFLAPLRSGDKFVVKVNISRTSAARIYFDHSILKLPNQEVILEAKATVVWLDNKHRPVRIPSSIRSKFVHFLRQNDTV | Acyl-ACP thioesterase involved in the production of fatty acids and beta-keto fatty acids. Can produce fatty acids of medium to long chain (6:0, 8:0, 10:0 and 16:1) and small amounts of medium to long chain beta-keto fatty acids (8:0, 14:0 and 16:1) when expressed in a heterologous organism (E.coli). Possesses thioesterase activity for lauroyl-ACP (12:0-ACP) in vitro. May play a role in the development of floral organs by generating short chain fatty acids. | F4HX80 |
Q8H1U5 | APC2_ARATH | Cyclosome subunit 2 | Arabidopsis | MEALGSSDCNLEILETLSDDAIQEITESYDGFFTTVESLIAGTGDSLVEDEFVSHVYCLCKYGLDSLVRDHFLRSLEQAFEKGGASSFWQHFDAYSEKKHHNYGEEIQIVLCKALEEISIEKQYHEKCLSIVVHALQSFKEQSSDDRQNSDTERVHLFSRFQSMLSSTLMTTLPQHFPEILHWYFKERLEELSAIMDGDGIEEQEDDCMDLDEKLRYKNGEMDVDEGCSQGKRLGHDKLVKNIGKVVRDLRSIGFTSMAENAYASAIFLLLKAKVHDLAGDDYRTSVLESIKEWIQTVPLQFLNALLSYLGDSVSYGTTSSGLTSPLACCPSPSFSRVVTPSEGIVRWKLRLEYFAYETLQDLRIAKLFEIIVDYPESSPAIEDLKQCLEYTGQHSKLVESFISSLKYRLLTAGASTNDILHQYVSTIKALRAIDPAGVFLEAVGEPIRDYLRGRKDTIKCIVTMLTDGSGGNANGSGNPGDSLLEELMRDEESQENVGFDDDFHTDDKQAWINASRWEPDPVEADPLKGSLSQRKVDILGMLVDIIGSKEQLVNEYRVMLAEKLLNKTDYDIDTEIRTVELLKIHFGEASMQRCEIMLNDLIDSKRVNTNIKKASQTGAELRENELSVDTLTSTILSTNFWPPIQDEPLELPGPVDKLLSDYANRYHEIKTPRKLLWKKNLGTVKLELQFEDRAMQFTVSPTHAAIIMQFQEKKSWTYKDLAEVIGIPIDALNRRVNFWISKGVLRESTGANSNSSVLTLVESITDSGKNEGEELLTGEEEGETSIASVEDQLRKEMTIYEKFIMGMLTNFGSMALERIHNTLKMFCVADPSYDKSLQQLQSFLSGLVSEEKLEFRDGMYLLKK | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication. | Q8H1U5 |
Q8Z861 | RIMO_SALTI | Ribosome maturation factor RimO | Salmonella | MSNVTHQPKIGFVSLGCPKNLVDSERILTELRTEGYDVVPHYDDADMVIVNTCGFIDSAVQESLEAIGEALNENGKVIVTGCLGAKEDQIREVHPKVLEITGPHSYEQVLQHVHHYVPKPKHNPFLSLVPEQGVKLTPRHYAYLKISEGCNHRCTFCIIPSMRGDLVSRPIGDVLSEAKRLVDAGVKEILVISQDTSAYGVDVKHRTGFHNGEPMKTSMVSLCEQLSKLGVWTRLHYVYPYPHVDDVIPLMAEGKILPYLDIPLQHASPRILKLMKRPGSVDRQLARIKQWREICPELTLRSTFIVGFPGETEEDFQMLLDFLKEARLDRVGCFKYSPVEGAGANELPDQVPEEVKEERWNRFMQLQQQISAERLQEKVGREILVIVDEVDEEGAIGRSMADAPEIDGAVYLNGETNVKPGDIVRVKVENADEYDLWGSRV | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | Q8Z861 |
O75807 | PR15A_HUMAN | Myeloid differentiation primary response protein MyD116 homolog | Homo | MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG | (Microbial infection) Promotes enterovirus 71 replication by mediating the internal ribosome entry site (IRES) activity of viral 5'-UTR. | O75807 |
Q9SXJ8 | NHX1_ORYSJ | Na(+)/H(+) exchanger 1 | Oryza sativa | MGMEVAAARLGALYTTSDYASVVSINLFVALLCACIVLGHLLEENRWVNESITALIIGLCTGVVILLMTKGKSSHLFVFSEDLFFIYLLPPIIFNAGFQVKKKQFFRNFMTITLFGAVGTMISFFTISIAAIAIFSRMNIGTLDVGDFLAIGAIFSATDSVCTLQVLNQDETPFLYSLVFGEGVVNDATSIVLFNALQNFDLVHIDAAVVLKFLGNFFYLFLSSTFLGVFAGLLSAYIIKKLYIGRHSTDREVALMMLMAYLSYMLAELLDLSGILTVFFCGIVMSHYTWHNVTESSRVTTKHAFATLSFIAETFLFLYVGMDALDIEKWEFASDRPGKSIGISSILLGLVLIGRAAFVFPLSFLSNLTKKAPNEKITWRQQVVIWWAGLMRGAVSIALAYNKFTRSGHTQLHGNAIMITSTITVVLFSTMVFGMMTKPLIRLLLPASGHPVTSEPSSPKSLHSPLLTSMQGSDLESTTNIVRPSSLRMLLTKPTHTVHYYWRKFDDALMRPMFGGRGFVPFSPGSPTEQSHGGR | Vacuolar antiporter that acts in low affinity electroneutral exchange of protons H(+) for cations such as Na(+) or K(+) across membranes . Plays important roles in the transport of Na(+) and K(+) accumulated in the cytoplasm into vacuoles, and is involved in salt stress tolerance . | Q9SXJ8 |
B6EMN5 | ARGE_ALISL | N-acetylornithinase | Aliivibrio | MKIPEFKEYYQQLISTSSISSTDSSWDEGNAKVIHKLAQWCEDLGCEVEIEEIEKGKLNLLAKLGSGEGGLLLAGHTDTVPYDQGRWNYDPHTLTEANDRFYGLGTADMKGFFAFILEAIKNINWKDQSKPLYILATCDEETTMLGARHFASNTSIQPDYCIIGEPTNLMPIRGHKGHVANAVRVTGKSGHSSNPAYGVNALEIMNEIMFALMNLKNKLVKEYHNPGFSIPYPTLNLGHIHGGDSPNRICGCCELHYDVRPLPGISLDGLDNMLRDALKDVEEKWPGRIEITPLHEPIPGYECSADSPIVTSVAEICGQEVETVNYCTEAPFLQDLCPTLVLGPGSIEQAHQPDEFLAFSFIDPTINILSKLMYKHCF | Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines. | B6EMN5 |
A6ZPY9 | MTNB_YEAS7 | Methylthioribulose-1-phosphate dehydratase | Saccharomyces | MSSQDVLIHSDDPCHPANLICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMTPEDLFVMDAQTLEYLRSPKLYKPSACTPLFLACYQKKDAGAIIHTHSQNAVICSLVFGDEFRIANIEQIKAIPSGKVDPVTKKPMTLSFFDTLKIPIIENMAHEDELIDDLHKTFKDYPDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQMGIPPDCGIGEEKKHLKMASP | Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). | A6ZPY9 |
A7GJS8 | PDXS_BACCN | Pdx1 | Bacillus cereus group | MTNVTGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMGAVSIPVMAKCRIGHLVEARVLESLGVDYIDESEVLTPADEVNHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRQVNAEIRQVANLREDELMTYAKNTGAPYEVLLEIKRLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVEATTHYEDYELIANLSKGLGDAMKGVEISTLLPEQRMQERGW | Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. | A7GJS8 |
Q6TPG9 | SLOB_PROMU | Snaclec mucrocetin subunit beta | Protobothrops | MGRFIFVSFGLLVVFLSLSGTEAGFCCPLGWSSYDEHCYQVFQQKINWEDAEKFCTQQHRGSHLVSFHSSEEVDFVVSKTSPILKHDFVWMGLSNVWNECAKEWSDGTKLDYKAWSGQSDCITSKTTDNQWLSMDCSSKRYVVCKFQA | Platelet-agglutinating factor that acts in a vWF-independent manner. Binds specifically to platelet GPIbalpha (GP1BA) to a distinct binding site from that of flavocetin-A. | Q6TPG9 |
A7GYU6 | SYP_CAMC5 | Prolyl-tRNA synthetase | Campylobacter | MRFSKFYAPTTKEAPKDASLPSHIFLVRGGFVEQIGSGLYNFLPLGKMMLDKITKVVKEEMDAAGVLEVSFSVVTSGELWKQSGRFNVFGKELLRFKDRKENDFVLSPTNEEAAVALVRGKVTSYKQLPLNIYQINTKFRDEARPRFGLLRGREFTMKDAYSFHANEADMKREFDLMEATYSKIFTRLGLNFRAVEADSGAIGGSGSKEFMVLAKNGEDDILCCDSCKYAANVEAAKRAKKTSDAPAPQADATKFYTPDAKTIKAVAEFFKVDEFYTIKAVIKKAIYEDTQKIVAFFVRGNDELQETKAQNACGALELVDASEDEVAAAGLVAGFCGPVGLSGVDFYIDNELKGQTQMICGANEKDYHFVGVSVSSFNDERFKDLVSVQAGDICPKCGGKLELSKGIEVGHIFQLGYKYSSAMGATFLDENGKARPFLMGCYGIGVSRLIAVMVEASHDDRGCVWKKECTPFECEIVISNLKDEAGVKFATKLYENLRNLGLCVLLDDRNERFGVKMNDFELLGFPYAIIVGKGLENGEVELITRDGLVKEVVKKDEILSVLKEKLC | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. | A7GYU6 |