accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q0HUY5 | CMOA_SHESR | Carboxy-S-adenosyl-L-methionine synthase | Shewanella | MNASQDTIYAQASEHISDFQFDNRVAGVFSDMIRRSVPGYTQIINTIGDFADRFVKPNTQVYDLGCSLGAATLSIRRQIQGRDCRIIAVDNSESMVTRCQENLSAYVSDTEVELICGDIRDIHIENASLVVLNFTLQFLPPEDREALIAKIYYGLNPGGLLVLSEKIRFDDAPIQSVLEELHLDFKRANGYSELEISQKRSALENVMKPDTLSIHQQRLTGQGFSHFSLWFQCFNFSSMVAIK | Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). | Q0HUY5 |
B8I385 | COAD_RUMCH | Pantetheine-phosphate adenylyltransferase | Ruminiclostridium | MNKFIYPGSFDPVTNGHLDIIERASKICDKLTVAVLINQSKNPLFSIEERVSLLKKVVKGSTNIEIECFSGLLVDFVKEKNANVIIKGLRAVSDFEYELQMALLNKNQAPDIETLFMMSSINYSFLSSSMVKELARHGGNISGLVPECIEKEIIDKFKLK | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | B8I385 |
B3PS18 | LEUD_RHIE6 | Isopropylmalate isomerase | Rhizobium | MDKFVKLTGVAAPLPVVNIDTDMIIPKDYLKTIKRTGLGKGLFAEARYNEDGSENPDFVLNKPAYRDAKILVAGDNFGCGSSREHAPWALLDFGIRCVISTSFADIFYNNCFKNGILPIKVSQEDLDKLMDDASRGSNAILTVDLENLEITGPDGGSIKFDLDAFKRHCLLNGLDDIGLTMEKGKAIDEFEKKNAASHPWAA | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | B3PS18 |
B2JK28 | AROC_PARP8 | 5-enolpyruvylshikimate-3-phosphate phospholyase | Paraburkholderia | MSGNTLGTLFTVTTFGESHGPAIGCVIDGCPPGMSLAEADIQLELDRRKPGTSRHVTQRQEEDKVEILSGVFEGKTTGAPIALLIRNTDQRSKDYGNIADTFRPGHADYTYWQKFGIRDYRGGGRSSARLTAPTVAAGAVAKKWLREKFGTEIRGYMAALGEIDVPFIDWQFVRENPFFVPNADVVPQLEAYMDALRKDGDSIGARINVVASGVPVGLGEPLFDRLDADIAHAMMGINAVKGVEIGAGFASVAQRGSVHGDELTPEGFVGNHAGGVLGGISTGQDITVSIAIKPTSSIRTPRRSIDKNGQPAVVETFGRH... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | B2JK28 |
Q46K52 | TRMFO_PROMT | Folate-dependent tRNA(M-5-U54)-methyltransferase | Prochlorococcus | MKEYPSVTVIGAGLAGSEAAWQIASAGIKVTLFEMRPKKKSLAHHTSEFAELVCSNSFGALSSDRAAGLLQEELRTLQSIVINNADKYSVPAGGALAVDRSQFSLSITNEVSSHPLITIIRDECPCLPKAHQITILATGPLTSELLAKDIKEFTGEKECHFFDAASPIITGESIDFLTAFRASRYDKGDADYVNCPMNEDSYIKFHSELIKAEQAELKDFEKESANFFEGCLPIEQLAKRGIETMRYGPLKPIGIWDPRWGDVNDKSIRRLKRAHAVVQLRQEDKAGKLWNLVGFQTNLKWGEQKRIFRMIPGLSKAEFI... | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q46K52 |
A0QKC8 | FBIB_MYCA1 | Dehydro-coenzyme F420-0 reductase | Mycobacterium avium complex (MAC) | MSPAGEHGTAAPIEILPVAGLPEFRPGDDLGAAVAKAAPWLRDGDVVVVTSKAVSKCEGRLVPAPADPEERDRLRRKLVDEEAVRVLARKGRTLITENRHGLVQAAAGVDGSNVGRDELALLPLDPDASAAALRARLRELLGVEVAVLVTDTMGRAWRNGQTDAAVGAAGLAVLHGYSGAVDQHGNELLVTEVAIADEIAAAADLVKGKLTAMPVAVVRGLSVTDDGSTARQLLRPGTEDLFWLGTAEAIELGRRQAQLLRRSVRRFSAEPVPAELVREAVAEALTAPAPHHTRPVRFVWLQTPAVRTRLLDAMKDKWRA... | Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0. | A0QKC8 |
Q9JJK4 | PEX3_RAT | Peroxisomal assembly protein PEX3 | Rattus | MLRSMWNFLKRHKKKCIFLGTVLGGVYILGKYGQKKLREIQEREAAEYIAQARRQYHFESNQRTCNMTVLSMLPTLREALMQQLNSESLTALLKNRPSNKLEIWEDLKIISFTRSIVAVYSTCMLVVLLRVQLNIIGGYIYLDNATVGKNGTSILAPPDVQQQYLSSIQHLLGDGLTELVTVIKQAVQRILGSISLKHSLSLLDLEQKLKEIRTLVEQHRSCWNDKDASKSSLCHYMMPDEETPLAAQAYGLSPRDITTIKLLNETRDMLESPDFSTVLNTCLNRGFSRLLDNMAEFFRPTEQDLQHGNSINSLSSVSLP... | Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes. | Q9JJK4 |
Q2JD52 | MURD_FRACC | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Frankia | MTGDGQGPGDGQGPGNLTTSISWAGLPVLVVGIGVSGLAAARALLARGARVRVVDAGDSPRHQGAAATLRALGAEVNLGGLPAGPGDSALVVTSPGVPPTAPLITGAAGAGIPVWGEVELAWRWRGGSRWLAVTGTNGKTTTTEMLGAMLAAGGRRSTTAGNIGTPIVDAVAAEPPYETLAVELSSFQLHYTHTMAPLAAAVLNVAPDHLDWHGGAAAYAAAKAGIWRRPGTTAIGNADDATSADLLAAAPGRRVLFGLDPAARPRPGLTVVDGHLVDDAFGGGRLVAVRDLVLTSPHMISNALAAAALARAEGVGPAAI... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | Q2JD52 |
P62558 | SOPB_ECOLI | Plasmid partition protein B | Escherichia | MKRAPVIPKHTLNTQPVEDTSLSTPAAPMVDSLIARVGVMARGNAITLPVCGRDVKFTLEVLRGDSVEKTSRVWSGNERDQELLTEDALDDLIPSFLLTGQQTPAFGRRVSGVIEIADGSRRRKAAALTESDYRVLVGELDDEQMAALSRLGNDYRPTSAYERGQRYASRLQNEFAGNISALADAENISRKIITRCINTAKLPKSVVALFSHPGELSARSGDALQKAFTDKEELLKQQASNLHEQKKAGVIFEAEEVITLLTSVLKTSSASRTSLSSRHQFAPGATVLYKGDKMVLNLDRSRVPTECIEKIEAILKELEK... | Control of plasmid partitioning; required to recognize the cis-acting. Binds specifically with the DNA segment containing the sopC region. SopB is trans-acting. | P62558 |
Q3SPL2 | UVRC_NITWN | Excinuclease ABC subunit C | Nitrobacter | MTSDSSDTAKQIGSGQPSGSPADMRRRDGVAPEQEVDPASLETDEDDEARLPDLPDEPVDAVAEAPLAIGRAAIEHAVRHAPTSPGVYRMMNAARDVLYVGKAKNVRKRLSSYARPTGQVMRIARMIAATAAVEIVSTGTETEALLLEANLIKQLRPRFNVQLRDDKSFPYILITGDHWAPQLLKHRGAQSRPGRYFGPFASAGAVGRTITALQRAFLVRSCTDSFFESRTRPCLLYQIKRCAGPCTGEIDFPGYTALVREATDFLSGRSRAVKEDLARAMEQAAADLAFERAALYRDRLAALSAIQSQQGINPRTVEEA... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q3SPL2 |
P61996 | ENCP4_PYRFU | Putative type 4B encapsulin shell protein PF1875 | Pyrococcus | MENNNIMSQVKEIIEAAIKELEDDGFEPDIILAGPIFIRYLPEDVRLKVYEIEELGSDAIIADSKYLGQIKKAAKRISIDPLLQEKEWEKIIEEIPTQE | May be the encapsulin shell protein in a type 4 A-domain encapsulin nanocompartment system. Its cargo may be upstream glyceraldehyde-3-phosphate dehydrogenase (AC P61879). | P61996 |
A4YCC5 | TDH_SHEPC | L-threonine 3-dehydrogenase | Shewanella | MKALSKLKAEKGIWLVDAPKPEMGHNDLLIKIKKTAICGTDMHIYNWDEWSQKTIPVPMVVGHEYVGEVVDIGQEVRGFKIGDRVSGEGHITCGHCRNCRAGRTHLCRNTSGVGVNREGSFAEYLVIPAFNAFKIPDDISDDLASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVCRHVGARHVVITDVNEYRLELARKMGATRAVNVSKENLKDVMKELGMTEGFDVGLEMSGVPSAFHAMLDTMNHGGKVAMLGIPGGEMAIDWSKVIFKGLVIKGIYGREMFETWYKMASLIQSGLDISPIITHHYKIDD... | Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. | A4YCC5 |
Q1CTW0 | DAPF_HELPH | PLP-independent amino acid racemase | Helicobacter | MVFYKYSGSGNDFLIVQSFKKKDFSNLAKQVCHRHEGFGADGLVVVLPSKDYDYEWDFYNSDGSKAGMCGNASRCVGLFAYQHAIAPKEHVFLAGKREISIRIEEPNIIESNLGNYKILDVIPALRCEKFFTNDSVLENIPTFYLIDTGVPHLVGFVKNKEGLNSLNTLELRALRHEFNANINIAFIENKETIFLQTYERGVEDFTLACGTGMAAVFIAARIFYNTPKKAALIPKSNESLELSLKNDGIFYKGAVRYIGMSVLGMRVFENGCF | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | Q1CTW0 |
A5UE83 | COAD_HAEIE | Pantetheine-phosphate adenylyltransferase | Haemophilus | MTSVIYPGTFDPITNGHLDIIERSAVIFPRVLVAVANSPSKKTLFSLEERVELVRQSVAHLSNVEVFGFSDLLANVIKQHNISAIIRGVRTTIDFEYELQLAALNRLLTKGVESLFFPPAEKWVFVSSTIVREIYLHGGDVAELVPVPVFNALKAR | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | A5UE83 |
Q65K84 | DAPEL_BACLD | N-acetyldiaminopimelate deacetylase | Bacillus | MKLDELAAIRRDLHQIPELGFQEYKTQAYLLNHLAKHPEGRIEIEKWRTGLFVKVKGTAPEKILAYRADMDGLSIREDTGYSFSSVHQDRMHACGHDFHMTIALGIIDHFVRHPVKQDLLFLFQPAEEGPGGAEPMLESDLFKKWEPSMITALHIAPELPVGTIGTKSGLLFANTSELVIELEGKGGHAAYPHLAEDMVVAASSLVTQMQSIVARNVDPLDSAVITIGTITGGSAQNIIAQEARLEGTIRTLSPASMEQVKKRIEAMVRGLETAYQCSGKVSYPAAYYQVCNSSDLVEDFMQFVSENGLAEVVRSKEAMT... | Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate. | Q65K84 |
B3GW58 | PSUG_CORA7 | Pseudouridine-5'-phosphate glycosidase | Corynebacterium | MHNVPIEYSDEVQNALSNGLPILGLESNVLSHGLPYPRNLEMFNACDEIIRSNGVVPALTFIRDKRICIGASPKDVELLTDDPKPIKVSARDIALCIAQGKVGATTASASIAICELAGIRIFSTAGLGGVHRDFSETLDVSADLHEISSRKTIVVSAGVKKFLDIPKTSEVLESLGVPVVGFGTSEFPAFYCRKSGAFLESFSQDPIEIATAAATHIETVGPGGFLILVAPSKEIALDDELVEKAVQRSLINASSQGVRGKAITKFVMRAIDSETDNRSQTANFDVMVEVVNAAAQIARSLKPEFFLDSVAKK | Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. | B3GW58 |
A3PEX4 | RPOB_PROM0 | Transcriptase subunit beta | Prochlorococcus | MSSSALQVAKTATYLPDLVEVQRASFKWFLEKGLIEELQNFSPISDYTGKLELHFIGEEYRLKRPRHDVEEAKRRDATFASQMYVTCRLINKETGEIKEQEVFIGELPLMTERGTFIINGAERVIVNQIVRSPGVYFKDELDKNGRRTYNASVIPNRGAWLKFETDKNNLLYVRVDKTRKINAHVLMRAMGLSDNDVVDKLRHPEFYQSSIESANDEGINSEDQALLELYKKLRPGEPPSVSGGQQLLHSRFFDPKRYDLGRVGRYKINKKLRLTVPDNVRTLTHEDVLSTIDYLINLELDIGGASLDDIDHLGNRRVRS... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A3PEX4 |
P45191 | PSTC_HAEIN | Phosphate transport system permease protein PstC | Haemophilus | MLTKSRKYFNQTWIESLFKQTTALFALLVFILLAAILISLVIGSWESIKRFGGSFLLETYWDPVQEQYGAIIPILGTLITAGIALFIAVPISFGIAIFLTELAPNWLKRPISIAIEMLAAIPSIIYGMWGLFVFVPLFQEHIQPVLIDNLGNLPGLELFFSGVPFGVGLFTAGLVLAIMIIPFIASVMRDVFSIVPPMLKEGAYGLGATTWEVVRQVIVPHTRIGLVGSVMLGLGRALGETMAITFIIGNSFQLPNSLFSPSTSIASAIANEFNEAGGLQKSALMELGLLLFVITTMVLILSRLMITKMQQTKGK | Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane. | P45191 |
Q6PCF9 | S38AA_XENLA | Solute carrier family 38 member 10 | Xenopus | MAASNWGLIMNIVNSIVGVSVLTMPFCFQQCGILLGTLLLMLCTWMAHHSCMFLVKSASVSKRRTYAGLAFHAYGKVGKMMVETSMIGLMLGTCIAFYVVIGDLGSSFFARLFGLEVSEGFRVFLLFSVSLCIVLPLSLQRNMMAFIQSFSAMALMFYTVFMFVIVLSSFKHGLFSGQWLKHVSYIRWEGVFRCIPIYGMSFACQSQVLPTYDSLDDPSVKIMSSIFALSLNVVTTFYITVGFFGYVSFPETIAGNVLVNFPSNLVTEMIRVGFMMSVAVGFPMMILPCRQALNTLLFEQQQKDGTFTAGGYMPPLRFKI... | Putative sodium-dependent amino acid/proton antiporter. | Q6PCF9 |
Q38UT7 | RPOA_LATSS | Transcriptase subunit alpha | Latilactobacillus | MIEFEKPNITKVDESTNYGKFVVEPLERGYGTTLGNSLRRILLASLPGTAVTDIQIDGVLHEFSTIDGVLEDVTQIILNIKKLALKLHVEEDKTIEIDVKGPATVTAADIISDDDVEVLNTDQYICTVAEGGNFHVRMTVKKGRGYVAAVQNKSDDMPIGVLPIDSIYTPISRVNYQVESTRVGRRNDFDKLTLDVWTNGSISPREAISLAAKIMTEHLAIFVDLTDEAKNAEIMVEKEETHKEKMLEMTIEELDLSVRSYNCLKRAGINTVQELTDKSEADMMKVRNLGRKSLEEVKNKLFDLGLGLRTEE | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q38UT7 |
Q12396 | EMP46_YEAST | 46 kDa endomembrane protein | Saccharomyces | MTTRKTASSLQLLGKITGTKAGTKQKKMNFINGLIWLYMCVWMVHGKVTQKDELKWNKGYSLPNLLEVTDQQKELSQWTLGDKVKLEEGRFVLTPGKNTKGSLWLKPEYSIKDAMTIEWTFRSFGFRGSTKGGLAFWLKQGNEGDSTELFGGSSKKFNGLMILLRLDDKLGESVTAYLNDGTKDLDIESSPYFASCLFQYQDSMVPSTLRLTYNPLDNHLLKLQMDNRVCFQTRKVKFMGSSPFRIGTSAINDASKESFEILKMKLYDGVIEDSLIPNVNPMGQPRVVTKVINSQTGEESFREKMPFSDKEESITSNELF... | Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing. | Q12396 |
Q46C69 | PELO_METBF | Protein pelota homolog | Methanosarcina | MRVTNRSLKGREGEIAVTAETLDDLWHLKYIIEKGDLVFSVTKRKADSASDKIRPEKVEKVKVRLGIRVDDLEFHKFANRLRLHGMIERGMDVGSYHTLNIEIGTNLSVIKEHWKNDQLQRIKDAEEASKRPKVVMVAIEEGDADIGFVHHYGIEIYSHIRQSSGKRETGLRNEFFREVVEQLRHAVPEEASIVIAGPGFTKEDFIKYFQETEPAMASKALIEDTSMIGMSGFQEVLRRGAVDRIMQESRIARESALMEDLIREISMDGKAAYGLGDVKNALNFGAVETLLVADETLREGREKGEDIDKLLREVEQAQGK... | May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity. | Q46C69 |
Q31D22 | NDHI_PROM9 | NDH-1 subunit I | Prochlorococcus | MKNFLQQINSYIKEAFNAGKYLYNGLSVTFDHLRRRPVTVQYPYEKLIPSERYRGRIHYEFDKCIACEVCVRVCPINLPVVDWVMNKETKKKELRNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELATFDRHNLNFDNVALGRLPTNVTTDPSIKPLRELAYLPKGVMDPHEIPASDIRVGKLPEEVYDWMRPTSNENKDKISNSNN | NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus co... | Q31D22 |
Q30TU7 | RS5_SULDN | 30S ribosomal protein S5 | Sulfurimonas | MEINREDFEESIVNIGRVTKVVKGGRRFRFTALVVVGNKKGTIGFGAGKAKEVPDAIKKAVDNAFKNLSKVSIKGTTIAHDIEHKYNASRILLKPASEGTGVIAGGAVRPVLELAGIKDVLTKSIGSNNPGTLVRATVEALGRLKG | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q30TU7 |
B7NP10 | AROC_ECO7I | 5-enolpyruvylshikimate-3-phosphate phospholyase | Escherichia | MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGIFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLEIKDWSQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGILGGISSGQQIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRH... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | B7NP10 |
C6DC11 | UNG_PECCP | Uracil-DNA glycosylase | Pectobacterium | MATSLTWHDVLAQEKQQPYFINTLEFVGKERAAGKTIYPPQKDVFNAFRFTELHQVKVVILGQDPYHGPNQAHGLSFSVRPGVPAPPSLANIYKELASDIPGFEIPRHGFLQSWAEQGVLLLNTVLTVEAGQAHSHANLGWETFTDRVIAALNEQREGLVFLLWGSHAQKKGNIIDQRRHHILKSPHPSPLSAHRGFLGCKHFSQANQLLEQQGLSPIDWTPRLPEEA | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | C6DC11 |
Q07U75 | OBG_RHOP5 | GTP-binding protein Obg | Rhodopseudomonas | MKFLDEAKVYIRSGDGGNGCVAFRREKYIEFGGPSGGNGGRGGDVVIEVADGLNTLIDYRYQQHFKAQKGTNGMGKDRHGANGKDIVLKVPRGTQIFDEDRETLLHDFTELGERFVLAEGGNGGFGNAHFKSSTNRAPRNANPGQEGEERWIWLRLKLIADAGLVGLPNAGKSTFLSKVSAAKPKIADYPFTTLHPQLGVVNVDGREFVLADIPGLIEGAHEGAGLGDRFLGHVERCRVLLHLIDATCEHAGKAYKTVRGELDAYAETLSDKVEIVALNKIDAVEPEELKKQRDRLKRAAKKTPLLMSGVTGQGVPEALR... | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. | Q07U75 |
Q47037 | AFAF_ECOLX | Dr hemagglutinin AFA-III operon regulatory protein AfaF | Escherichia | MKINKLTLNERKNDILSYFSEINTPFRTSEVAEHLGVSAYQARHYLQCLEKEGKIKRSPVRRGASTLWEISAVTEPSVKTDRIAD | May have a possible regulatory function on the expression of the other AFA-III genes. | Q47037 |
O34926 | CYPX_BACSU | Cytochrome P450 CypX | Bacillus | MSQSIKLFSVLSDQFQNNPYAYFSQLREEDPVHYEESIDSYFISRYHDVRYILQHPDIFTTKSLVERAEPVMRGPVLAQMHGKEHSAKRRIVVRSFIGDALDHLSPLIKQNAENLLAPYLERGKSDLVNDFGKTFAVCVTMDMLGLDKRDHEKISEWHSGVADFITSISQSPEARAHSLWCSEQLSQYLMPVIKERRVNPGSDLISILCTSEYEGMALSDKDILALILNVLLAATEPADKTLALMIYHLLNNPEQMNDVLADRSLVPRAIAETLRYKPPVQLIPRQLSQDTVVGGMEIKKDTIVFCMIGAANRDPEAFEQ... | Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms pulcherrimin via a nonenzymic reaction with Fe(3+). Substrates with small alkyl groups (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrate... | O34926 |
P05102 | MTH1_HAEPH | Modification methylase HhaI | Haemophilus | MIEIKDKQLTGLRFIDLFAGLGGFRLALESCGAECVYSNEWDKYAQEVYEMNFGEKPEGDITQVNEKTIPDHDILCAGFPCQAFSISGKQKGFEDSRGTLFFDIARIVREKKPKVVFMENVKNFASHDNGNTLEVVKNTMNELDYSFHAKVLNALDYGIPQKRERIYMICFRNDLNIQNFQFPKPFELNTFVKDLLLPDSEVEHLVIDRKDLVMTNQEIEQTTPKTVRLGIVGKGGQGERIYSTRGIAITLSAYGGGIFAKTGGYLVNGKTRKLHPRECARVMGYPDSYKVHPSTSQAYKQFGNSVVINVLQYIAYNIGS... | A methylase, recognizes the double-stranded sequence 5'-GCGC-3', methylates C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease. | P05102 |
Q6AWT8 | GG3_ARATH | Heterotrimeric G protein gamma-subunit 3 | Arabidopsis | MSAPSGGGEGGGKESAAGGVSSSSLAPSSLPPPRPKSPPEYPDLYGKRREAARVQMLEREIGFLEGEIKFIEGVQPASRCIKEVSDFVVANSDPLIPAQRKSRRSFRFWKWLCGPCLSLVSFCCCCQSKCSCHLRKPKCCNCTSCSCIGSKCCDGSCCSNICCCPRLSCPSCSCFRGCWCSCPDMSCCIPSCFRSCSCTRPSCLNKKKSSCCSCNCKIRWSSCFSCPKVRLCSCCFCNCKNLCSNPCCLAF | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. | Q6AWT8 |
Q8DCG1 | RAPA_VIBVU | ATP-dependent helicase HepA | Vibrio | MAFALGQRWISDTESDLGLGTVVALDARTVTLMFAASEENRVYASNDAPVTRVVFNVGDVVECQEGWSLKVEQVVEENGLYTYLGTREDTEETGVALREIFLSNQIRFNKPQDKMYAGQIDRMDNFVLRYRALKNQYEQHRSPMRGLCGMRAGLIPHQLYIAHEVGRRHAPRVLLADEVGLGKTIEAGMIIHQQVLLGRAERILIVVPETLQHQWLVEMMRRFNLHFSIFDEERCVEAFAESDNPFDTQQYVLCSLDFLRKSRKRFEQALEAEWDLLVVDEAHHLEWSQDKPSRGYQVVEGLAERTPGVLLLTATPEQLG... | Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on line... | Q8DCG1 |
P79959 | GBB1_XENLA | XGbeta1 | Xenopus | MSELDQLRQEAEQLKNQIRDARKACADATLAQITANIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICPIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDSRCFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMVYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTLKADRAGVLAGHDNRVSCLGV... | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. | P79959 |
Q6DGM8 | JDP2_DANRE | Jun dimerization protein 2 | Danio | MMPGQIPDPLVTAGSLPSVGPLAGFPATTLTEQLKLAELYRLGTVLSPLMLNRHAKRPFDAIKSEDDDDDERKKRRREKNKVAAARCRNRKKERTDFLQKESERLEMLNSDLKSQIEELKSERQQLIVMLNLHRPTCIVRTDSVKSDEHPLEPRED | Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. | Q6DGM8 |
Q8UBS0 | PROB_AGRFC | Gamma-glutamyl kinase | Agrobacterium tumefaciens complex | MSLTRKPLASHHRIVIKIGSALLVDRKSGLKKDWLDAICEDIAALKKNGADVQVVSSGAIALGRTVLGLPSGALKLEESQAAAAVGQIALARAWSESLSRHEIVAGQILLTLSDTEERRRYLNARATINQLLKIGAIPIINENDTVATTEIRYGDNDRLAARVATMTGADLLVLLSDIDGLYTAPPHLDPDAKFLETIADITPEIEAMAGGAASELSRGGMRTKIDAGKIATAAGCGMIIASGKTLNPLKAIENGARSSWFAPSGTPVTARKTWIAGQLQPAGEIHVDAGAEKALYAGKSLLPAGVRQVKGNFGRGDAIA... | Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | Q8UBS0 |
Q2GDE4 | COXX_NEOSM | Heme O synthase | Neorickettsia | MFQVVSKTDWLTVRAYFALLKPRVVSLVTFTAVTGAVLAYFSGYHAPFFSVFTAIFCIAVGSGAAGALNMYYDRDIDAIMSRTSKRPIPQGKISPEAALVFGLVLFALSVLLMELAVNHLSAVLLSVAVFYYSVIYTVYLKRRTPQNIVVGGGAGAFPPMIGWAAVANHIGVESLVLFLIIFLWTPPHFWALALKNSGEYEAAGIPMLPVTSGVKATKMQILCYSVLLFITSILPYLLRFSGGTYMIVAFILGLVFLYYAINVYLDEKKCMKLFYYSVLYLFLLFGVFILDAALSTALGMLI | Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | Q2GDE4 |
Q54BD5 | TRM13_DICDI | tRNA:m(4)X modification enzyme TRM13 homolog | Dictyostelium | MGEINNNKEINEKDDEINNKRLKYEGFIKKEKKKKQKIDHSIPLKEKPTQEDIDSHSECLFWIVNKKKHRAEFCKYKRAKDSILCNHHKPIDQISSEPQPQLTDYNGDDVTENNNNSTTTTTATTQDDNSKPKERKRIHCPLNPTHIIYECKLQKHLKACPNAKVGQKNAHIELSKKEPYYKENINDLNENVKLTLEPIILSQVSTENLINISIKLDQFFEKFFKNEIQSLNQTHKSFDKIFNSDQQLKHIQQESSIINLLENSNLYNSDNVYLEFGAGSGKLSNHIFMSHEKKSGHILIDRMKFRSLKKVDRLIKNEKG... | tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His). | Q54BD5 |
B0RWG2 | DADA_XANCB | D-amino acid dehydrogenase | Xanthomonas | MRVLILGSGVIGTTTAWYLAQSGCEVTVVDRQPASGLETSYANAGQLSFGYTSPWAAPGVPGKAVKWLFEQHAPLSIRPTRDLRQLAWLSQMLRNCTAERYAVNKARMVRLSDYSRDCLNELRASTGLEFEGRQLGTTQLFRTQQQLDAAAQDIEVLAQYGVPYELLSPAQIAQYEPGLAGGGAQMAGALHLPEDQTGDCRLFTQRLADLATQAGVQFRYGQQIERLEHAGGEITGVQIDGRLVTADRYVLALGSYSADLLLSLGLHLPVYPLKGYSLTIPIVDAQRAPTSTVLDESYKIALTRFDERIRVGGMAEVAGF... | Oxidative deamination of D-amino acids. | B0RWG2 |
Q13WE6 | AROC_PARXL | 5-enolpyruvylshikimate-3-phosphate phospholyase | Paraburkholderia | MSGNTLGTLFTVTTFGESHGPAIGCVIDGCPPGLALNEADIQLELDRRKPGTSRHVTQRQEEDKVEILSGVFEGQTTGAPIALLIRNTDQRSKDYGNIADTFRPGHADYTYWQKYGIRDYRGGGRSSARLTAPTVAAGAVAKKWLREKFGTEIRGYMAALGEIDVPFVDWAHVRENPFFVPNQQIVPQLEAYMDALRKEGDSIGARINVVASGVPVGLGEPLFDRLDADIAHAMMGINAVKGVEIGAGFASVAQRGSVHGDELTPEGFVGNHAGGVLGGISTGQDITVSIAIKPTSSIRTPRRSIDKAGQPAVVETFGRH... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | Q13WE6 |
Q13304 | GPR17_HUMAN | R12 | Homo | MSKRSWWAGSRKPPREMLKLSGSDSSQSMNGLEVAPPGLITNFSLATAEQCGQETPLENMLFASFYLLDFILALVGNTLALWLFIRDHKSGTPANVFLMHLAVADLSCVLVLPTRLVYHFSGNHWPFGEIACRLTGFLFYLNMYASIYFLTCISADRFLAIVHPVKSLKLRRPLYAHLACAFLWVVVAVAMAPLLVSPQTVQTNHTVVCLQLYREKASHHALVSLAVAFTFPFITTVTCYLLIIRSLRQGLRVEKRLKTKAVRMIAIVLAIFLVCFVPYHVNRSVYVLHYRSHGASCATQRILALANRITSCLTSLNGAL... | Dual specificity receptor for uracil nucleotides and cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs following ischemia. | Q13304 |
B2TWC5 | RRAA_SHIB3 | Regulator of ribonuclease activity A | Shigella | MKYDTSELCDIYQEDVNVVEPLFSNFGGRASFGGQIITVKCFEDNGLLYDLLEQNGRGRVLVVDGGGSVRRALVDAELARLAVQNEWEGLVIYGAVRQVDDLEELDIGIQAMAAIPVGAAGEGIGESDVRVNFGGVTFFSGDHLYADNTGIILSEDPLDIE | Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. | B2TWC5 |
P03947 | TRPD_BACSU | Anthranilate phosphoribosyltransferase | Bacillus | MNRFLQLCVDGKTLTAGEAETLMNMMMAAEMTPSEMGGILSILAHRGETPEELAGFVKAMRAHALTVDGLPDIVDTCGTGGDGISTFNISTASAIVASAAGAKIAKHGNRSVSSKSGSADVLEELEVSIQTTPEKVKSSIETNNMGFLFAPLYHSSMKHVAGTRKELGFRTVFNLLGPLSNPLQAKRQVIGVYSVEKAGLMASALETFQPKHVMFVSSRDGLDELSITAPTDVIELKDGERREYTVSPEDFGFTNGRLEDLQVQSPKESAYLIQNIFENKSSSSALSITAFNAGAAIYTAGITASLKEGTELALETITSG... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | P03947 |
Q73TE1 | Y3777_MYCPA | Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_3777 | Mycobacterium avium complex (MAC) | MRSEGDTWDITTSVGSTALFVATARALEAQKPDPLAVDPYAEIFCRAVGGTAADVLDGKDPDHQLKTTDFGENFVNFQGARTRYFDNYFARTADAGVRQVVVLAAGLDSRAYRLDWPAATTIFELDQPQVLDFKREVLARAGAQPRAERREIAIDLREDWPQALRDSGFDPAKPSAWIAEGLLIYLPASAQEQLFTGIDGLAGHGSHVAVEDGAPMKPEDFETAVAEERAATAQGDQRVFFQLVYNEQCAPATEWFGNRGWTAVGTPLADYLREVGRPVPGPETEAGPMIARNTLVSAVRA | Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | Q73TE1 |
Q5FFU1 | RL4_EHRRG | 50S ribosomal protein L4 | Ehrlichia | MEVNVINIESQNIGKIDLNPLIFSVNYRPDILKMVVEWQLSKRRVGAHKTKTIGDVSGTTAKPYRQKHTGRARQGSLRSPQFRGGAVIFGPVVRSHAYSLNKKVRNLGLKVALSLKNSCNKLLILDSIDVNFVKTAQVLRFIKNFEHQSFLIIGKDYNKGMMYSCKNLHNVTLLKQIGTNVFDILRHDCVILTVDTVKYLEDRLL | Forms part of the polypeptide exit tunnel. | Q5FFU1 |
P31786 | ACBP_MOUSE | Endozepine | Mus | MSQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI | Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neurope... | P31786 |
Q6F854 | PANB_ACIAD | Ketopantoate hydroxymethyltransferase | Acinetobacter | MISLSDLRKFKTEGRKFSCLTCYDASMAKAMEFAEIDSILIGDSLGMVIQGHDSTLPVTVDDMAYHTAAVRRGNQHSFIMTDLPFMSYATLPDALNNAKKVMQAGAQMIKIEGGAWLSESIRVLTQNGIPVCVHLGLTPQSVHVFGGYKLQAKTREAADQLIADCQAVVDAGAAILLLECVPAQLGQEIAELFPQTPVIGIGAGKETDGQVLVAQDMLGLSFGKVARFVRNFMKEQAGETAIVDAFKAYHAAVQDQSFPAREHTFQVEL | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | Q6F854 |
D3DFP8 | PSPB_HYDTT | O-phosphoserine phosphohydrolase 2 | Hydrogenobacter | MKRLYLVRHAQSEYNEKGIFQGRLDSDLTPLGFVQARLLAREFLKKKVDIIYSSPQRRAYKTALTISDMLGTQLVVDERLREMSFGEYEGKHFWSMLEAHKDVFLNWLSNPVKHPLPTQESMEEFEKRVRSFLEDVKSSHYQNMLIVAHGGTLHAIVCLLTGIGLENLWNIHMDNAGITEIHMEGEKSTLVYLNKLCHTRQLT | Part of a complex that catalyzes the dephosphorylation of L-phosphoserine to serine and inorganic phosphate. Is poorly or not active toward D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, para-nitrophenylphosphate, and fructose-6-phosphate. Does not display phosphoglycerate mutase activity. | D3DFP8 |
Q0CRD8 | MCR1_ASPTN | Mitochondrial cytochrome b reductase | Aspergillus subgen. Circumdati | MFARQTFRYAQPLKQSFRKYSTEAPKGKSLAPVYLTVGLAGLGVGLYRYNSATAEAPAERAKVFTGGDQGWVDLKLSEIEVLNHNTKRFRFEFEDKEAVSGLNVASALLTKFKPEGGKAVLRPYTPVSDESQPGFLDLVVKVYPNGPMSEHLHSMNVDQRLEFKGPLPKYPWEANKHQHICLIAGGTGITPMYQLARHIFKNPEDKTKVTLVYGNVSEQDILLKKELEELENTYPQRFKAFYVLDNPPKEWTGGKGYISKELLKTVLPEPKEENIKIFVCGPPGLYKAISGNKVSPKDQGELTGILKELGYSQEQVFKF | May mediate the reduction of outer membrane cytochrome b5. | Q0CRD8 |
A0QIR4 | MIAB_MYCA1 | tRNA-i(6)A37 methylthiotransferase | Mycobacterium avium complex (MAC) | MTCGFSRADRSPYHGPVTSTVARDVSGVRTYQVRTYGCQMNVHDSERLAGLLEAAGYRRAAEGAEVADVVVFNTCAVRENADNKLYGNLSHLAPRKRSNPQMQIAVGGCLAQKDREAVLRRAPWVDVVFGTHNIGSLPTLLERARHNKAAQVEIAEALQQFPSSLPSARESAYAAWVSISVGCNNSCTFCIVPSLRGKEVDRSPDDILAEVRSLVADGVLEVTLLGQNVNAYGVSFADPALPRDRGAFARLLRACGEIDGLERVRFTSPHPAEFTDDVIEAMAQTPNVCPALHMPLQSGSDRVLRAMRRSYRAERYLGII... | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | A0QIR4 |
B9LJ40 | SECA_CHLSY | Protein translocase subunit SecA | Chloroflexus | MMNFLRRLLGDSNEKELRRLQPIVEEINRLGPEFAALSDAELRAKTDEFRQRLADGETLDDILPEAFATVREAAHRTIGLRHYDVQLIGGIVLHQGKIAEMKTGEGKTLVATLPLYLNALEGKGVHLVTVNDYLAKVGAGWMGPIYHFLGLTVGFIAHDQSALYDPDFIDPDANPEDQRLVHWRPCTRREAYLADITYGTNNEFGFDYLRDNMAYEKSQLVQRELHYAIVDEVDNILIDEARTPLIISGPAQKSSDLYRQMAQLVRQLRRSSVTAKQVKEEGLEPDGDFFVDERTKSIYLSEKGIEKLERLLRIPPGESL... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains acro... | B9LJ40 |
Q1LU93 | ABITM_DANRE | Protein Simiate | Danio | MEDKEEKKAPSVIDRYFTRWYRTDLKGKPCEDHCILQHSNRICVITLAESHPIFQNGRKIKNINYQISDGCSRLKNKVSGKSKRGGQFLTEFAPLCRITCTDEQEFTIFSCIRGRLLEVNEVILNKPDLLMEKPSTEGYIAVILPKFEESKSVTEGLLTREQYEEILTKRNQQEVPC | May regulate actin polymerization, filopodia dynamics and arborization of neurons. | Q1LU93 |
A5CC91 | SYDND_ORITB | Non-discriminating aspartyl-tRNA synthetase | Orientia | MHKYRTHTCGELSLAHVGLQVKLSGWLYRRRDHGGLLFIDLRDHYGIIQLVFNDDCSAVQAEISKIKFETVITVEGAVVARSNETINKNISTGDVEVVVSSYVVESFAEELPLQINGEYEAPEETRLKYRFLDLRGARLHQNIVLRSKVIQELRNQMLSNGFIEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMMSGFDKYFQIAPCFRDEDARADRSPGEFYQLDIEMAFVTQEDVFGLVEPVLYNTFKKFSNYSITNIPFPRITYDESMLRYGSDKPDLRNPIQISDVTDIFQCSEFTTLKDSIN... | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | A5CC91 |
B2K2I3 | TSAD_YERPB | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Yersinia | MRVLGIETSCDETGIAVYDDKAGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEANLSAKDIDAVAYTAGPGLVGALLVGATIGRALAFAWGVPAVPVHHMEGHLLAPMLEENAPEFPFVALLVSGGHTQLISVTGIGEYLLLGESVDDAAGEAFDKTAKLLGLDYPGGPMLSRMAQQGTVGRFTFPRPMTDRPGLDFSFSGLKTFAANTIRANGDDDQTRADIARAFEDAVVDTLAIKSKRALDQTGFKRLVIAGGVSANQTLRLKLADMMQKRGGEVFYARPEFCTDNGAMIAYAGMVRLRSNLNSE... | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct ca... | B2K2I3 |
P40876 | YCBF_ECOLI | Uncharacterized fimbrial chaperone YcbF | Escherichia | MTNTWNRLALLIFAVLSLLVAGELQAGVVVGGTRFIFPADRESISILLTNTSQESWLINSKINRPTRWAGGEASTVPAPLLAAPPLILLKPGTTGTLRLLRTESDILPVDRETLFELSIASVPSGKVENQSVKVAMRSVFKLFWRPEGLPGDPLEAYQQLRWTRNSQGVQLTNPTPYYINLIQVSVNGKALSNVGVVPPKSQRQTSWCQAIAPCHVAWRAINDYGGLSAKKEQNLP | Part of the elfADCG-ycbUVF fimbrial operon, which promotes adhesion of bacteria to different abiotic surfaces. Could be required for the biogenesis of fimbriae. | P40876 |
Q2K853 | HIS3_RHIEC | Phosphoribosyl-AMP cyclohydrolase | Rhizobium | MGQLIFNQPSEDKSALEDAGDFTPRFDDRGLITAVVADAGDGELLMVAHMNAQALALTIQTGTAHYFSRSRGKIWKKGETSGNLQTVKEIRTDCDQDAIWLKVEVAGHDATCHTGRRSCFYRTVTLREGKPMLDIVDDERHFDPQDVYGK | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | Q2K853 |
O61734 | CYCL_DROME | MOP3 | Sophophora | MEVQEFCENMEEIEDENYDEEKSARTSDENRKQNHSEIEKRRRDKMNTYINELSSMIPMCFAMQRKLDKLTVLRMAVQHLRGIRGSGSLHPFNGSDYRPSFLSDQELKMIILQASEGFLFVVGCDRGRILYVSDSVSSVLNSTQADLLGQSWFDVLHPKDIGKVKEQLSSLEQCPRERLIDAKTMLPVKTDVPQSLCRLCPGARRSFFCRMKLRTASNNQIKEESDTSSSSRSSTKRKSRLTTGHKYRVIQCTGYLKSWTPIKDEDQDADSDEQTTNLSCLVAIGRIPPNVRNSTVPASLDNHPNIRHVLFISRHSGEGK... | Putative transcription factor involved in the generation of biological rhythms. Activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters. | O61734 |
P69750 | O16A_CONCN | Delta-conotoxin-like CnVIA | Pionoconus | MKLTCMMIVAVLFLTAWTFVTADDSRNGLENLSPKARHEMKNPEASKSNKRYECYSTGTFCGINGGLCCSNLCLFFVCLTFS | Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. | P69750 |
Q1JIX0 | PURA_STRPD | IMP--aspartate ligase | Streptococcus | MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGIFFPQKISVIGNGVVVNPKSLVKELAYLHDEGVTTDNLRISDRAHVILPYHIQLDQLQEDAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDKDIFAERLRINLAEKNRLFEKMYDSTPLDFDAIFEEYYAYGQEIKQYVTDTSVILNDALDAGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDEVGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRV... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q1JIX0 |
A7ZVR5 | RF3_ECO24 | Peptide chain release factor 3 | Escherichia | MTLSPYLQEVAKRRTFAIISHPDAGKTTITEKVLLFGQAIQTAGTVKGRGSNQHAKSDWMEMEKQRGISITTSVMQFPYHDCLVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKLDRDIRDPMELLDEVENELKIGCAPITWPIGCGKLFKGVYHLYKDETYLYQSGKGHTIQEVRIVKGLNNPDLDAAVGEDLAQQLRDELELVKGASNEFDKELFLAGEITPVFFGTALGNFGVDHMLDGLVEWAPAPMPRQTDTRTVEASEDKFTGFVFKIQANMDPKHRDRVAFMRV... | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. | A7ZVR5 |
A5F5X0 | NQRB_VIBC3 | NQR-1 subunit B | Vibrio | MGLKKFLEDIEHHFEPGGKHEKWFALYEAAATLFYTPGLVTKRSSHVRDSVDLKRIMIMVWLAVFPAMFWGMYNAGGQAIAALNHLYSGDQLAAIVAGNWHYWLTEMLGGTMSSDAGWGSKMLLGATYFLPIYATVFIVGGFWEVLFCMVRKHEVNEGFFVTSILFALIVPPTLPLWQAALGITFGVVVAKEVFGGTGRNFLNPALAGRAFLFFAYPAQISGDLVWTAADGYSGATALSQWAQGGAGALINNATGQTITWMDAFIGNIPGSIGEVSTLALMIGAAFIVYMGIASWRIIGGVMIGMILLSTLFNVIGSDTN... | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. | A5F5X0 |
Q9H4L7 | SMRCD_HUMAN | ATP-dependent helicase 1 | Homo | MNLFNLDRFRFEKRNKIEEAPEATPQPSQPGPSSPISLSAEEENAEGEVSRANTPDSDITEKTEDSSVPETPDNERKASISYFKNQRGIQYIDLSSDSEDVVSPNCSNTVQEKTFNKDTVIIVSEPSEDEESQGLPTMARRNDDISELEDLSELEDLKDAKLQTLKELFPQRSDNDLLKLIESTSTMDGAIAAALLMFGDAGGGPRKRKLSSSSEPYEEDEFNDDQSIKKTRLDHGEESNESAESSSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDMQYVSQSEVPNGKEVSSRSQNYP... | DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Requi... | Q9H4L7 |
Q0VND6 | NDK_ALCBS | Nucleoside-2-P kinase | Alcanivorax | MAVERTLSIIKPDAVAKNVIGEIVTRFEKAGLSVVAMKMVHLSDEKAGGFYAEHKERPFFKDLVGFMTSGPVVVQVLEGEDAVAKNRDLMGATNPKEAEAGTIRADFAETIDANAVHGSDSTESAAREVAYFFSDEEVCPRAS | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | Q0VND6 |
P25573 | MGR1_YEAST | Mitochondrial genome-required protein 1 | Saccharomyces | MAVFTPPSGNSNSTDHTHTQDDHDKDDNDIKKFYIRPSLGLKLWGPLVPAPDNLPGLYTLITIQSAVGFFALWRLRRLYKLPPPRRIATGTHSDLSFGELPSEMIVNGKTKIKKDIADFPTLNRFSTTHGDIVLAPPPIIPRQSRFVSVRKLLWGLFGSLLLSQSLLELTRLNFLKYDPWCDEMKSVRDKKFFNNIVKYYHEGIDPTKIKVKDAMNGTPLSTNIPEVKQSVALARAQVEAQNPIIKWFGPLEYKPMSFNEYLNRMEFHLDMFEFFQNKRNIRENSIELINSISHNPQSSSTGLEGLSESKKLHLQNVEKR... | Component of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. Together with MGR3, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Required for growth of cells lacking the mitochondrial genome. | P25573 |
A1V8B2 | RPOB_BURMS | Transcriptase subunit beta | pseudomallei group | MQYSFTEKKRIRKSFAKRSIVHQVPFLLATQLESFSTFLQADVPTAQRKSEGLQAAFTSVFPIVSHNGFARLEFVSYALSSPAFNIKECQQRGLTYCSALRAKVRLVLLDKESPSKSVVKEVKEQEVYMGEIPLMTPTGSFVINGTERVIVSQLHRSPGVFFEHDKGKTHSSGKLLFSARIIPYRGSWLDFEFDPKDVLYFRVDRRRKMPVTILLKAIGLTPEQILANFFVFDNFTLMDEGAQMEFVPERLRGEVARFDITDREGKVIVQKDKRINAKHIRDLEAAKTKYISVPEDYLLGRVLAKNVVDGDTGEVIANAN... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A1V8B2 |
C3K6G9 | LPXB_PSEFS | Lipid-A-disaccharide synthase | Pseudomonas | MANLRIALVAGEASGDILGAGLMRALKAQHPAVQFIGVGGPLMQAEGLTSYFPMERLSVMGLVEVLGRLRELLARRKLLIQTLIEEKPDVFIGIDAPDFTLTLELKLRQAGIKTVHYVSPSVWAWRQKRVLKIREGCDLMLTLLPFEARFYEEKGVPVRFVGHTLADTIPLQADRTAARAELGLPDGPLVALMPGSRGGEVGRLASVFFDAAERLQALKPGVRFVLPCASPQRRVQIETLLEGRNLPLTLLDGQSHLALAACDAVLIASGTATLEALLYKRPMVVAYRLAPLTFWILKRMVKSPYISLPNLLAQRLLVPE... | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | C3K6G9 |
Q7VG29 | PTH_HELHP | Peptidyl-tRNA hydrolase | Helicobacter | MPCLLVAGLGNPSAKYQNTRHNIGFMVLDFLSKELDFDFSFDKKFNAEVGAINIGPHKVFFLKPQTFMNLSGEAINPFVRYFDITHTFVIHDDIDIGFGDMRFKYGGSSGGHNGLKSIDSFMGDTYFRLRFGVGRSANKNVVEYVLSDFNAQEREQLEGLIAHAKEAVMSFCNMAQYPKEHILTHLQQYFTLKIPKLTPSQTQNNESFATQFSQMQYTRFTQG | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q7VG29 |
Q47MU1 | TIG_THEFY | PPIase | Thermobifida | MKTAVEELSPTRVKLTIEVPFEELDHAFDVTYKSLAKQVRIKGFRPGKAPAKLIDRYVGRGAVLTQAVNHAVPELYSEAVSKEEVPVLGPPEVEITRLEDGKELAFTAEVDVRPKFEVTDYEGIEVTVDDAEVTEEQVNERLEALRQRFATLIGVDRPAEQGDHVSIDLSASVDGKKLEDAQASGVSYEIGAGTLLQGLDEAIIGLSAGESATFTTTLVGGEHKGREADVTVTVHSVKLKELPELDDEFARLASEFDTIEELRASEAERLGELLRAQQLRQARDRVLEKLVDSIDIPLPESVIKQEADRRRELLDRQLSQ... | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | Q47MU1 |
A9M8Q9 | ODO1_BRUC2 | Alpha-ketoglutarate dehydrogenase | Brucella | MAKQEQAPDRANDVFALTSFLYGGNADYIEELYAKYEDDPNSVDPQWRDFFAKLGDNADDVKKNAEGPSWTRKNWPIAANGELVSALDGNWAEVEKHVADKLKGKAAKGEAKGAAGTPLTAEEITQAARDSVRAIMMIRAYRMRGHLHANLDPLGLAEKPNDYNELEPENYGFTPADYNRKIFIDNVLGLEYATVPEMLDILKRTYCGAIGVEFMHISDPAEKAWIQERIEGPDKKVAFTPEGKKAILSKLIEAEGFEQFIDVKYKGTKRFGLDGGESLIPALEQIVKRGGQMGLKEVVLGMAHRGRLNVLSQVMGKPHR... | E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). | A9M8Q9 |
Q8BG54 | SPTC3_MOUSE | Serine-palmityl-CoA transferase 3 | Mus | MANLNDSAVTNGTLHNPKTQQGKRQSTGCVKNGISKEAQQNRKAYAEDKPVFEPYQEAPLYVYVLTYMGYGIGILFGYLRDFMRNWGIEKCNAAVEREEQKDFVPLYQDFENFYKRNLYMRIRDSWSHTVCSAPEPYMNVMEKVTDDYNWTFRHTGKVIENIINMASYNYLGLAGKYDDSMVRVKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIIRGQPGTGRAWKKILIVVEGVYSMEGSIVNLA... | Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. SPT complexes containing SPTLC3 generate shorter chain sphingoid bases compared to complexes containing SPTLC2.... | Q8BG54 |
Q73YQ8 | MURG_MYCPA | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Mycobacterium avium complex (MAC) | MNDTVKKPTGGRGDDPLPAGAALSAVAPHEPVSVVLAGGGTAGHVEPAMAVADALKALDPHVRITALGTARGLETRLVPERGYDLELITPVPLPRKPTGDLARLPSRVWRAVRETRAVLHAVDADVVIGFGGYVALPAYLAARGVSPRKPRVPVVIHEANASAGLANRVGARTAQRVLSAVPDCGLPGAEVVGVPVREAITSLDRAALRAEARRHFGFADDARVLLVFGGSQGAASLNRAVSGAAAQLAAAGVSVLHAHGPKNTLDLREPQPGDPPYVAVPYLDRMDLAYAAADLVICRSGAMTVAEVSAVGLPAIYVPL... | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | Q73YQ8 |
P46005 | AGGC_ECOLX | Outer membrane usher protein AggC | Escherichia | MKTSSFIIVILLCFRIENVIAHTFSFDASLLNHGSGGIDLTLLEKGGQLPGIYPVDIILNGSRIDSRDIFFYTKKNRHGEYYLKPCLTRDILINYGVKTEEYPNLFRQNSEKNRDSSDCADLSVIPQATEDYHFIKQQLILGIPQVAIRPPLTGIAHETMWDDGISAFLLNWQVEGSHWEYRSNTRNSSDNFWASLEPGINLGSWRIRNLTTWNKSSGQSGKWESSYIRVERGLNNIKSRLTFGDDYTPSDIFDSVPFRGGMLGSDENMVPYNQREFAPVVRGIARTQARIEVRQNGYLIQSRIVSPGAFALTDLPVTGN... | Involved in the export and assembly of the AAF/I fimbriae subunits across the outer membrane. | P46005 |
A5VPI6 | SSRP_BRUO2 | Small protein B | Brucella | MNKPKNSPARKMIAENRKARFNFEILDTLEAGLVLTGTEVKSLRANQANIAESYASFEDGEFWLINSYIPEYTQGNRFNHEPRRLRKLLVSRWEMSRLFNSVSREGMTVVPLKLYFNDRGRAKLELALARGKKTHDKRETEKKRDWNREKARLLRDRG | 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 resemb... | A5VPI6 |
P42453 | RUBR_ACIAD | Rubredoxin | Acinetobacter | MKKYQCIVCGWIYDEAEGWPQDGIAPGTKWEDIPDDWTCPDCGVSKVDFEMIEV | Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. | P42453 |
A4VL90 | PQQB_PSEU5 | Pyrroloquinoline quinone biosynthesis protein B | Pseudomonas | MFIRILGSAAGGGFPQWNCNCANCAGLRAGTLNAKARTQSSIAISDNGVDWILCNASPDIRAQLESFPALQPARAPRDTAIGAIVLLDSQIDHTTGLLTLREGCPHEVWCTEMVHQDLTTGFPLFNMLEHWNGGLKWNPIALSGNFSIPCCPNLHITPIPLRSSAPPYSPHRNDPHPGDNIGLLIEDRNTGGTLFYAPGLGQVSEELLATMRRADCLLVDGTLWRDDEMLVREVGTKLGSEMGHLQQSGPGGMIEVLDGMPAVRKILIHINNTNPILDEDSVEREILGEHGIEVAYDGMNIEL | May be involved in the transport of PQQ or its precursor to the periplasm. | A4VL90 |
Q2SZ88 | PROA_BURTA | Glutamyl-gamma-semialdehyde dehydrogenase | pseudomallei group | MDIDQYMTDVGRRARRASRSIARASTAAKNAALEAVARAIERDAGALKAANARDVARAKDKGLDAAFVDRLTLSDKALKTMVEGLRQVATLPDPIGEMSNLKYRPSGIQVGQMRVPLGVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEALESNTALAKLIGEGLAEAGLPQDTVQVVETADRAAVGRLITMTEYVDVIVPRGGKSLIERLINEARVPMIKHLDGICHVYVDDRASVTKALTVCDNAKTHRYGTCNTMETLLVARGIAPAVLSPLGRLYREKGVELRVDADARAVLEAAGVGPLVDATDEDWRTEYL... | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. | Q2SZ88 |
Q5M2B2 | RS10_STRT2 | 30S ribosomal protein S10 | Streptococcus | MANKKIRIRLKAYEHRTLDTAAEKIVETATRTGATVAGPVPLPTERSLYTIIRATHKYKDSREQFEMRTHKRLIDIINPTQKTVDALMKLDLPSGVNVEIKL | Involved in the binding of tRNA to the ribosomes. | Q5M2B2 |
A5VM67 | HEM3_LIMRD | Pre-uroporphyrinogen synthase | Limosilactobacillus | MTNKVIVGSRKSKLAMAQTELVIASLEKIFPDIKFEIKNVITEGDRNRHVSLAKIGGKGVFVKEIEDELKDGTIDFAVHSLKDVMPILPEELVLGAFPKRVSPYDCLVSRKNLSSLNDLPKGARIGTNSLRRQGQLLSIRPDLKIIPIRGNIDTRLRKIDTEALDGIILAEAGLTRLNIDLSSYHVLDLQNYIMPAVGQGCLAIECRKNDTRIRKMLDQINDEESAYCVQVEREFMRELGGSCNFPIGGHAYAKNGQILFDGLIASPNGEHVIKETKIPANNSGVGKKVADQLLAKDKFGIIEGE | Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | A5VM67 |
P37915 | TSAK_ORITS | TSK56 | Orientia | MKKIMLIASAMSALSLPFSASAIELGEEGLECGPYAKVGVVGGMITGVESARLDPADAEGKKHLSLTNGLPFGGTLAAGMTIAPGFRAEIGVMYLTNITAQVEEGKVKADSVGETKADSVGGKDAPIRKRFKLTPPQPTIMPISIAVRDFGIDIPNQTSAASTSRSLRLNDEQRAAARIAWLKNCAGIDYRVKNPNDPNGPMVINPILLNIPQGNPNPVGNPPQRANPPAGFAIHNHEQWRHLVVGLAALSNANKPSASPVKVLSDKITQIYSDIKHLADIAGIDVPDTSLPNSASVEQIQNKMQELNDLLEELRESFDG... | May be an adherent factor for rickettsial adsorption to the host-cell surface and a determinant of virulence of individual rickettsial strain. It is the major outer membrane protein. | P37915 |
Q57962 | PPSA_METJA | Mja pepA intein | Methanocaldococcus | MLIIQNTKGDSMKFIAWLDELSNKDVDIAGGKGASLGEMWNAGLPVPPAFVVTADAYRHFIKETGLMDKIREILSGLDVNDTDALTNASKKIRKLIEEAEMPEDLRLAIIEAYNKLCEMCGEDEVTVAVRSSATAEDLPEASFAGQQDTYLNIKGAENVVKYVQKCFSSLFTPRAIFYREQQGFDHFKVALAAVVQKLVNAEKAGVMFTVNPISENYDELVIEAAWGLGEGVVSGSVSPDTYIVNKKTLEIVDKHIARKETMFVKDEKGETKVVEVPDDMKEKQVLSDDEIKELAKIGLNIEKHYGKPMDVEWAYEKGKF... | Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. | Q57962 |
Q83IX6 | WZYE_SHIFL | Probable ECA polymerase | Shigella | MSLLQFSGLFVVWLLCTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQVLLSAGCFYAVYYVTYKTRLRKRVADVPRRPLFTMNRVETNLTWVILMGIALVSVGIFFMHNGFLLFRLNSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGMNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYDNIDFQGLAPIVRDFYVFIPSWLWPGRPSMVLNSANYF... | Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. | Q83IX6 |
A7ME80 | NFUA_CROS8 | Fe/S biogenesis protein NfuA | Cronobacter | MIRISDAAQAHFAKLLASQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFVTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVTLMEITDEGYAILQFGGGCNGCSMVDVTLKEGIEKQLLNEFPELKGVRDLTEHQRGEHSYY | Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | A7ME80 |
P61911 | DUT_RHOPA | dUTP pyrophosphatase | Rhodopseudomonas | MTQKITVSIRHLPHGEGLPLPEYQTAHAAGLDLIAAVPQDAPLTLQPGRYVLVPTGLTIALPENYEAQVRPRSGLAAKHGVTVLNAPGTIDADYRGEIGVLLINHGTEPFAIRRGERIAQMVIAPVSRAQFVAVEALPESGRGAGGFGSTGR | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | P61911 |
B1KRP8 | DEOC_SHEWM | Phosphodeoxyriboaldolase | Shewanella | MSDLKKAAQKAIELMDLTTLNDDDTDQKVIELCHKAKTPAGNTAAICIYPRFIPIARKTLNELGCEDIKIATVTNFPHGNDDIAIAVLETRAAVAYGADEVDVVFPYRSLMEGNETLGFELVKACKEACGDDAILKVIIESGVLEDPALIRKASELCIDAGADFIKTSTGKVPVNATIEAAEIMMTVISEKNTKVGFKPAGGVRDAAAAGEFLGLAARLLGDDWATPATFRFGASSLLVNLLHTLELGEEAKGPQGY | Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. | B1KRP8 |
Q21HN0 | ILVC_SACD2 | Ketol-acid reductoisomerase type I | Saccharophagus | MQVYYDKDCDLSIIQGKKVAIIGYGSQGHAHACNLKDSGVDVTVGLRTGSSSVAKAEAHGLKVADVATAVAAADVVMILTPDEFQSVLYKEEIEPNIKQGATLAFAHGFAIHYNQVVPRADLDVIMVAPKAPGHTVRSEFVKGGGIPDLIAIFQDASGTAKEVALSYASGVGGGRSGIIETTFKDETETDLFGEQAVLCGGAVELVKMGFETLTEAGYAPEMAYFECLHELKLIVDLMYEGGIANMNYSISNNAEYGEYVTGPKVINEESRKAMRQALKDIQQGEYAKNFILEGQSNYPSMTAWRRNNAAHPIEQVGGKL... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q21HN0 |
Q82X69 | RPOA_NITEU | Transcriptase subunit alpha | Nitrosomonas | MSSNSFLTPRIVEVHNISPLHAKVVMEPFEHGFGYTLGNALRRVLLSSIPGCAPTKVSISGVVHEYSTIDGLQEDVVDLILNLKGVVLKLHNNKTQSVLTLKKSSEGIVTAGDIEATHDVEIVNPDHVIAHITSGGKIEAQITVEKGRGYWPSANRSKEDKSSSSIGDILLDASFSPIRRVSYAVESARVEQRTDLDKLIIDIETNGSVDPEEAIRYAAKVLVEQFSFFADLESTPLPTEQPKAPVIDPILLRPVDDLELTVRSANCLKVENIFYIGDLIQRTEAELLRTPNLGRKSLNEIKEVLASRDLSLGMKLENWP... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q82X69 |
Q891J8 | CLPX_CLOTE | ATP-dependent Clp protease ATP-binding subunit ClpX | Clostridium | MDMAKNDDKKQLKCSFCGKKQDQVKRLVAGPGVYICDECIELCSEIITDELEEDINTDMSSLPKPSEIKSYLDDYVIGQDDAKKALSVAVYNHYKRINLNNVNDDVELQKSNILLLGPTGSGKTLLAQTMAKFLNVPFAIADATTLTEAGYVGEDVENILLKLIQNADYDIEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQSLLKILEGTIASVPPQGGRKHPHQEFIQLNTTNILFICGGAFDGVDKLIERRTRNSSLGFGADIKSKRDENVGELLKKIMPEDLLKFGLIPEFIGRLPITVTLSALDRDALVE... | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Q891J8 |
Q07UI9 | UGPC_RHOP5 | sn-glycerol-3-phosphate import ATP-binding protein UgpC | Rhodopseudomonas | MASVTLRNVRKTYPGGFEAIKGIDFAVGDGQFCVLVGPSGCGKSTLLRMVAGLETITAGEIDIGGRVVNTIEPADRDIAMVFQNYALYPHMSVYNNMAYGLRNRGMKKPDIDARVREAARILEIEPLLQRKPKQLSGGQRQRVAMGRAIVRQPKVFLFDEPLSNLDAKLRIAMRVEIRKLQRRLATTAIYVTHDQLEAMTLADQLVVMNGGVVEQIGSPLEVYRKPATTFVASFIGAPPMNLMQLDGDALRGQLAGGAGAGVLGIRPEDLTLLTDGSAPEGGVAIELRIEAVERVGPESFVYGSRSNGGAAVSPHPGERP... | Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system. | Q07UI9 |
Q0T0L8 | ZUPT_SHIF8 | Zinc transporter ZupT | Shigella | MSVPLILTILAGAATFIGAFLGVLGQKPSNRLLAFSLGFAAGIMLLISLMEMLPAALAAEGMSPVLGYGMFIFGLLGYFGLDRMLPHAHPQDLMQKSVQLLPKSIKRTAILLTLGISLHNFPEGIATFVTASSNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLAEILGGVLAWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCGMSVMGFSLVLLQTAGIG | Mediates zinc uptake. May also transport other divalent cations. | Q0T0L8 |
Q58909 | Y1514_METJA | Putative gamma-glutamylcyclotransferase MJ1514 | Methanocaldococcus | MEYVFVYGSLRKGFWNHEPYLKNSKFIGKGKTKEKYAMYVNIIPYVVENEKISHIVGEVYEVDEKTLKRIDCLEGHPDYYRRKKVSIILDSGKEIEAWLYFYPESCGILVESGDYKDYRG | Putative gamma-glutamylcyclotransferase. | Q58909 |
Q8DWG1 | PYRG_STRMU | UTP--ammonia ligase | Streptococcus | MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITDALKEKIKRAATTTDSDVIITEVGGTVGDIESLPFLEALRQMKADVGADNVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEQPAGQGIKNKLAQFCDVAPEAVIESLDVDHLYQIPLNLQAQNMDQIVCDHLKLDVPVADMTEWSAMVDKVMNLKKKTKIALVGKYVELPDAYLSVVEALKHSGYVN... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | Q8DWG1 |
Q1CRF2 | PLSY_HELPH | Lysophosphatidic acid synthase | Helicobacter | MEGVLNFLTNINVIFTLLGYLIGGIPFGYALMKIFYGMDITKIGSGGIGATNVLRALQSKGVSNAKQMALLVLILDLFKGMFAVFLSKLFGLDYSLQWMVAIASILGHCYSPFLNFNGGKGVSTIMGSVVLLIPIESLIGLTVWFFVGKVLKISSLASILGVGTATVLIFFVPYMHIPDSVNILKEVDTQTPMVLIFIFTLIKHAGNIFNLLAGKEKKVL | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | Q1CRF2 |
Q9BYZ8 | REG4_HUMAN | Regenerating islet-derived protein IV | Homo | MASRSMRLLLLLSCLAKTGVLGDIIMRPSCAPGWFYHKSNCYGYFRKLRNWSDAELECQSYGNGAHLASILSLKEASTIAEYISGYQRSQPIWIGLHDPQKRQQWQWIDGAMYLYRSWSGKSMGGNKHCAEMSSNNNFLTWSSNECNKRQHFLCKYRP | Calcium-independent lectin displaying mannose-binding specificity and able to maintain carbohydrate recognition activity in an acidic environment. May be involved in inflammatory and metaplastic responses of the gastrointestinal epithelium. | Q9BYZ8 |
P21616 | AVP_VIGRR | Vacuolar H(+)-pyrophosphatase | Vigna | MGAAILPDLGTEILIPVCAVIGIAFALFQWLLVSKVKLSAVRDASPNAAAKNGYNDYLIEEEEGINDHNVVVKCAEIQNAISEGATSFLFTEYKYVGIFMVAFAILIFLFLGSVEGFSTSPQACSYDKTKTCKPALATAIFSTVSFLLGGVTSLVSGFLGMKIATYANARTTLEARKGVGKAFITAFRSGAVMGFLLAANGLLVLYIAINLFKIYYGDDWGGLFEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGLNHE... | Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane. | P21616 |
B0UBI3 | UREG_METS4 | Urease accessory protein UreG | Methylobacterium | MTTPHHGPLRVGIGGPVGSGKTALMEGLCKALRGRFDLCAITNDIYTKEDARLLTVAGALPEERIMGVETGGCPHTAIREDASINLAAVAEMRRRFPSLDLILIESGGDNLAATFSPELADLTLYVIDVAGGEKIPRKGGPGITRSDLLVINKTDLAPLVGADLAVMEADTQRMRGGRPYVFTSLRRGDGVEAVARFVIEAGGL | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | B0UBI3 |
A1RRK0 | RSMA_PYRIL | S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase | Pyrobaculum | MGKRRWSQHFLRDTSVAQFITELVPSGLDIIEVGPGRGALTLPLAEKSKTIYAIEIDPTLAEFLKRQAPPNVVVIVGDALEIEWPRADFFVSNIPYSITSPLLLKLAKYRLPAVVTIQKEVAERLVAAPGTENYGRLTVAIRCHYDVEVLRILPPHVFSPPPKVYSAVVRLTPRRPCVEDFENFQRFTARLFSTRRKTLRRLKLGETEKRVYQLTLEEIVELYKKHFDTTETCRS | Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | A1RRK0 |
P83642 | DRS5_PHYDS | Dermadistinctin-Q2 | Phyllomedusa | GLWSKIKEAAKTAGLMAMGFVNDMV | Antibacterial peptide with activity against Gram-positive bacteria S.aureus and E.faecalis, and Gram-negative bacteria P.aeruginosa and E.coli. | P83642 |
Q8FL76 | LEU3_ECOL6 | Beta-IPM dehydrogenase | Escherichia | MSKNYHIAVLPGDGIGPEVMTQALKVLDAVRNRFAMRITTSHYDVGGAAIDNHGQPLPPATVEGCEQADAVLFGSVGGPKWEHLPPDQQPERGALLPLRKHFKLFSNLRPAKLYQGLEAFCPLRADIAANGFDILCVRELTGGIYFGQPKGREGSGQYEKAFDTEVYHRFEIERIARIAFESARKRRHKVTSIDKANVLQSSILWREIVNEIATEYPDVELTHMYIDNATMQLIKDPSQFDVLLCSNLFGDILSDECAMITGSMGMLPSASLNEQGFGLYEPAGGSAPDIAGKNIANPIAQILSLALLLRYSLDADDAAS... | 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. | Q8FL76 |
A4XNB2 | FMT_PSEMY | Methionyl-tRNA formyltransferase | Pseudomonas | MPDSLRIVFAGTPEFAAEHLKALLASQHEVIAVYTQPDRPAGRGQKLMPSPVKQLAVEHGIPVHQPASLRNEEAQAELAALKPDLMVVVAYGLILPQVVLDTPRLGCINSHASLLPRWRGAAPIQRAVQAGDLESGVTVMQMEAGLDTGPMLLKVSTPISAEDTGGSLHDRLARLGPQAVLQAIDGLAAGTLIGELQDDAQANYAHKLNKDEARLDFSRPAVELERLIRAFHPWPICHTTLNGDALKVHAAELGEGSGAPGTILAADKNGLTVACGEGALRLTRLQLPGGKPLAFSDLYNSRREQFAPGLVLGQ | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. | A4XNB2 |
Q60B95 | SELO_METCA | Protein adenylyltransferase SelO | Methylococcus | MSTAMPGAFSPPRGLADLPLCPVYSRLGRPFHQPVAATSLPEPRMVHFNAALAGELGFGPEAGPQLLEILAGNRPWPGYASSASVYAGHQFGAWVPQLGDGRALLIAEVRTPARERVELQLKGAGPTPYSRGLDGRAVLRSSIREYLASEAMHALGVPTTRCLSLVASPQPVARETVESAAVVCRAAASFVRFGQFEYFAGRGQTEPMARLADHVIAEHFPHLQGHPERHAAWLGEVIERTARLIAQWQLLGFCHGVMNTDNFSVLGLTLDYGPFGFMDRFRWYHVCNHSDYEGRYAYRAQPEVGRWNCERLLQAVSPLL... | Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation). | Q60B95 |
B0KRC0 | MNME_PSEPG | tRNA modification GTPase MnmE | Pseudomonas | MNTVRETIAAIATAQGRGGVGIVRLSGPLAGKAGQLITGRTLTPRHAHYGPFRDDDGLVLDEGIALFFPGPNSFTGEDVLELQGHGGPVVLDMLLQRCVQVGCRLARPGEFSERAFLNDKLDLAQAEAIADLIEASSSQAARNALRSLQGEFSKRVHSLTEALIALRIYVEAAIDFPEEEIDFLADGHVLSMLDAVRGELSTVQREAGQGALLRDGMTVVIAGRPNAGKSSLLNQLAGREAAIVTDIAGTTRDILREHIHIDGMPLHVVDTAGLRDTDDHVEKIGVERALKAIGEADRVLLVVDSTAPEASDPFALWPEF... | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | B0KRC0 |
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