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
|
|---|---|---|---|---|---|---|
Q980Q7
|
NDK_SACS2
|
Nucleoside-2-P kinase
|
Saccharolobus
|
MVAQRTFVMIKPDGVKRGLIGEIISRFEKRGLKIVSLKMVKMSRDTAEKLYEEHKGKSFFEELVNYVTSGPVVCMVIEGDDVVQVIRRMIGNTDPKEAPPGTIRGDYALSKSENVIHASDSIEKAQREMSLFFDKSDL
|
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.
|
Q980Q7
|
Q9PL20
|
SYI_CHLMU
|
Isoleucyl-tRNA synthetase
|
Chlamydia
|
MDNEDKVSFPAKEEKVLTFWKEQNIFQKTLENRDGSPTFSFYDGPPFATGLPHYGHLLAGTIKDVVCRYATMDGHYVPRRFGWDCHGVPVEYEVEKSLGLTEPGAIDRFGIANFNEECRKIVFRYVDEWKYFVDRIGRWVDFSATWKTMDLSFMESVWWVFHSLYKQGLVYEGTKVVPFSTKLGTPLSNFEAGQNYKEVDDPSVVAKFALQDDQGILLAWTTTPWTLVSNMALAVHPGLTYVRIQDKESGEEYILGQESLARWFPDRESYKWIGQLSGESLVGRRYCPLFPYFQDQQDRGAFRVIPADFIEESEGTGVVHMAPAFGEADFFACQEHNVPLVCPVDNQGCFTSEVTDFVGEYIKFADKGIARRLKNENKLFYQGTIRHRYPFCWRTDSPLIYKAVNSWFVSVEKVKHKMLKANESIHWTPGHIKHGRFGKWLEGARDWAISRNRYWGTPIPIWRSEDGELLVIRSIQELEELSGQKIVDLHRHFIDEIVIHKNGKSFHRIPYVFDCWFDSGAMPYAQNHYPFERAEETEARFPADFIAEGLDQTRGWFYTLTVIAAALFDQPAFKNVIVNGIVLAEDGNKMSKRLNNYPSPKKIMDTYGADALRLYLLNSVVVKAEDLRFSDKGVEAVLKQVLLPLSNALAFYKTYAELYGFSPNETTDLELAEIDRWILSSLYSLVGKTRENMAQYDLHAAVSPFIDFIEDLTNWYIRRSRRRFWESEDSPDRRAAFATLYEVLMVFSKIIAPFIPFTAEDMYQQLRVETDPESVHLCDFPHVVLEKILPDLEKKMQDIREIVALGHSLRKEHKLKVRQPLQHMYIVGAKERMAALAQVDSLIGEELNVKEVHFCSETPEYVTTLVKPNFRSLGKRVGNRLPEIQKALAGLSQEQIQAFMHNGFMVLSLGEETISLNEEDITVSWEAAPGFVARSSASFVAILDCQLTSPLIMEGIAREIVNKINTMRRNGKLHVSDRIAIRLHAPKIVQEAFSQYEEYICEETLTTSVSFIDDKEGEEWDVNGHAVSLSLEVIGH
|
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
|
Q9PL20
|
O13928
|
RHO3_SCHPO
|
GTP-binding protein rho3
|
Schizosaccharomyces
|
MSSCFGSKKKPIYRKIVILGDGAAGKTSLLNVFTKGYFPQVYEPTIFENYIHDIFVDGNSIELSLWDTAGQEEYDQLRSLSYSDTHVIMICFAVDSRDSLENVITKWLPEVSSNCPGVKLVLVALKCDLRGADEEQVDHSKIIDYEEGLAAAKKINAVRYLECSAKLNRGVNEAFTEAARVALAAQPRGTKDGADESHGTGCIIA
|
Involved in controlling cell shape and septation . Regulates cell separation by modulating the function of the exocyst complex . Involved in post-Golgi vesicle transport . Involved in driving sexual development in a palmitoylation-dependent manner .
|
O13928
|
Q3AFE5
|
UVRC_CARHZ
|
Excinuclease ABC subunit C
|
Carboxydothermus
|
MTLWEKVKNLPDSPGVYLYKDEKGEVIYVGKAKNLKNRVRSYFQPPEKLLPKTRVMMEKARDIEVIITSTEVEALILEQNLIKRYRPRYNILLKDDKSYPYLKITGEEFPRLLITRRVVNDGGRYFGPYPDAGALNETYKLLRSIFKFRTCTPTIFAQKKRPCLNFHIKKCSAPCAGEISREEYFKEIEMVVDFLEGRGENLIKKLKKEMAIASDNLEFERAAKLRDQILALEKILAKQKISRGQRNADVVVVANRENLGVGLIFVIRQGNLLGQKVYTFTGEMETGELLNQVLVTHYGEAKEVPVEIILSTRENLDEEFLNSWFELKFGKKPKFTVPKRGEKFELLKMALENVNFTLDEKIKLNEKKQLLNEKALMDLKEALNLPVVPRRIEGYDISHLAGTGTVASMVVFIDGEPVKGKYRRFAIRSAANDDYTAMFEAVLRRFKKYLALQEEGGADGSFEELPDLVLIDGGKGQLNAAMDALKETNLLGKFTVIALAKEQEEIFLPGKKDSLLLTQDREGLKLLQRVRDEAHRFARGYQEKKRVKTLASLLEQVEGIGPKRRKQLLNKFGSIKNLREATVEEITAVPGITREIAERLKELLEME
|
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.
|
Q3AFE5
|
O95758
|
PTBP3_HUMAN
|
Regulator of differentiation 1
|
Homo
|
MDGVVTDLITVGLKRGSDELLSSGIINGPFTMNSSTPSTANGNDSKKFKRDRPPCSPSRVLHLRKIPCDVTEAEIISLGLPFGKVTNLLMLKGKSQAFLEMASEEAAVTMVNYYTPITPHLRSQPVYIQYSNHRELKTDNLPNQARAQAALQAVSAVQSGSLALSGGPSNEGTVLPGQSPVLRIIIENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVNAHYAKMALDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDFTRLDLPTGDGQPSLEPPMAAAFGAPGIISSPYAGAAGFAPAIGFPQATGLSVPAVPGALGPLTITSSAVTGRMAIPGASGIPGNSVLLVTNLNPDLITPHGLFILFGVYGDVHRVKIMFNKKENALVQMADANQAQLAMNHLSGQRLYGKVLRATLSKHQAVQLPREGQEDQGLTKDFSNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVTVDDLKNLFIEAGCSVKAFKFFQKDRKMALIQLGSVEEAIQALIELHNHDLGENHHLRVSFSKSTI
|
RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U).
|
O95758
|
Q839V7
|
SYE_ENTFA
|
Glutamyl-tRNA synthetase
|
Enterococcus
|
MTKVRVRYAPSPTGHLHIGNARTALFNYLFARHNDGEFIIRIEDTDQKRNIEDGEKSQLENLAWLGMEWDESPAHPGEYGPYRQSERKEIYQPLIDQLLSSNRAYKCYCTPEELEAEREAQQARGEMPHYAGTCANLTPSEQAAKEAAGLEPVIRFRVPRNTEYKFDDIVKGEITFESDNIGGDFVIQKRDGMPTYNFAVAVDDHLMKISHVLRGDDHIANTPKQLMIYEAFEWTPPVFGHMTLIINSETGKKLSKRDETILQFIEQYRELGYLPEAMFNFIALLGWSPVGEEEIFSQEDLIKLFDEQRLSKSPAAFDAKKLEWINNQYMKQMDLSELTDMCIPYLVADGRVEENPSPEKIEWLKQLVSLYQPQMSYAAEIVELSNLFFNEHPVLDDAAKEFLQGETVPTVLHAFKEQLEALDVFDVPSIKAAIKAVQKETGVKGKNLFMPIRIAVSGQMHGPELGETIELLGKEKALDHLNKVL
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
Q839V7
|
Q8HQQ8
|
MATK_PINHA
|
Intron maturase
|
Pinus subgen. Pinus
|
MDEFHRCGKEDSFWQQCFLYPLFFQEDLYAISHDHYLDVSSSSRPMEHLSSNDQLSFLTVKRLIGQIRQQNHSIVLFVNCDPNALADRKKSFYSESVLEALTLVLEVPFSIRSKYSVEGMNECKSFRSIHSIFPFLEDKFPHSNSILDARIPYSIHPEILVRTFRRWIRDAPSLHPLRSVLYDYRNSPENLQRSIIVVPRVNTRFFLFLLNYYVCECESILFSRLKRSSHSRSLSHGSFPQRTHFHRKIKHIIIFSRRNSLKSIWSLKDPKINYVRYGERPIIAIKGAHLLVKKCRYYLLIFRQFYFHLWSEPYRVCSHQLSKNCSSSPGYFLRVRMNPIFVRTKMLDELFIADLITNEMDPIVPIVPIIGLLAAEKFCDISGRPISKLSWTSLTDDDILDRFDQIWRNLFHYYSGSFDRDGLYRIKYILSLSCAKTLACKHKSTIRVVRKELGPELLKKSFSKEREFDSLPFSSKAAARSQRERIWHSDILQINPLANSWQKIQDLKIENLFDQ
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q8HQQ8
|
Q39GX4
|
BPT_BURL3
|
Aspartate/glutamate leucyltransferase
|
Burkholderia cepacia complex
|
MTHPTELPLSPLSALQFYATAPYPCSYLDGRVARSQVATPSHLINSDIYTELVKAGFRRSGVFTYRPYCDGCRACVPVRVPVDAFAPSRTQRRMWKRHRTLVATVSPLHYDEEHYALYMRYQSARHAGGGMDRDSRDQYEQFLLQSRINSRLVEFRDLDAPGGEPGKLRMVSMIDILGDGLSSVYTFFEPDDQHTSYGTYNILWQIEQAKSLGLPYVYLGYWIRESPKMAYKANFHPLEGLIDGRWKILDPERIDLPPVDAALARAPLPGGHSGSG
|
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.
|
Q39GX4
|
Q8W4B1
|
RCF3_ARATH
|
Protein SHINY 1
|
Arabidopsis
|
MERSRSKRNYHYDQDYDGDSMPRSKPRYNNNYHFGGGGGGNNRYRGGGGGGGGNGRPSKSHPETMATTTYRILCHDAKAGGVIGKSGTIIKSIRQHTGAWINVHELVPGDAERIIEISDNRRRDPDGRMPSFSPAQEALFSVHDRILESEAQFGYGGPPPEEEEDYGGVRPGGGRVVTRLVVSRMHVGCLLGKGGKIIEQMRIETKTHIRILPRESNLPRCVSLSEEIVQIVGELNAVKNALAIVSSRLRESQHRDRSNFQGRSHSPERSFAAAGDDYMPQLRRQSSDRFPRGNFRNNNFSSRQSNYAEEAPAVPVGENVYSEELVFQILCPADKIVRVVGESQGIIDLLQNEIGVDVRVSDPVAGSDEQIITISSEEAPDDPFFPAQEALLHIQTQIIDLIPDKDNLITTRLLVPSRDSICLEGKAGSVSEISRLTGTSVQILAREEIPRCASINDVVIQITGEIRAAREALVELTLLLRSHMFKELSQKETPPASTSTTGPLEGVAGVMEVASSNNTIQSREGPTSSNLNLQQVSTILPQFKEGFGSVAKAGESEHREEVPVTTSRMAVPLVTRSTLEVVLPEAVVPKLVTKSRNKLAQISEWSGASVTIVEDRPEETQNIIRISGTPEQAERAQSLLQGFILSIQEDGP
|
Acts as negative regulator of osmotic stress-induced gene expression . Involved in the regulation of thermotolerance responses under heat stress. Functions as an upstream regulator of heat stress transcription factor (HSF) genes. Negatively regulates HSFA1A, HSFA1B and HSFA1D, but positively controls the expression of HSFA1E, HSFA3, HSFA9, HSFB3, and DREB2C . Forms a complex with CPL1 that modulates co-transcriptional processes such as mRNA capping and polyadenylation, and functions to repress stress-inducible gene expression . Regulates pre-mRNA processing under salt stress . Involved in primary miRNA processing and pri-miRNA biogenesis . Binds both intronless and intron-containing pri-miRNAs . Acts as a regulator of biotic stress response gene expression and basal JA-mediated responses involved in defense. Acts as negative regulator of resistance to the fungal pathogen Fusarium oxysporum .
|
Q8W4B1
|
A5UBC5
|
RSMC_HAEIE
|
rRNA (guanine-N(2)-)-methyltransferase RsmC
|
Haemophilus
|
MISLESQVLERHLSFFDGKSVLFAGGISDNFPQTLASKCPSIQIWSCHFDYARTQSAVNFSVEFQGQADLIVYYWTKNKQEVNFQLLQLLAQAPIGQEILIIGENRCGVRSVEKTLAPYGEIAKIDSARRCGLYHFSLQNKPHFELKNFWKTYQHSTLENLTIYSLPGVFSAAELDTGTELLLSTIDNKIKGKVLDLGCGAGVIGSMIKKRVPNAQITMTDIHAMALESARKTLSENQLQGKVYASDVFSDIEGKFDLIISNPPFHDGIDTAYRAVTELITQAKWHLNQYGELRIVANAFLPYPELLRQHFNDYQVLAQTGKFKVYSVKN
|
Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
|
A5UBC5
|
Q5JJF9
|
RL24_THEKO
|
50S ribosomal protein L24
|
Thermococcus
|
MKLDMKQPRKQRKFLYNAPLHLRGKIMSAPLSKELREKYGVRNLPIRVGDKVKVMRGDFKGVEGKVVEVDLRRYRIHVEGVTHKKTDGTEVFYPLHPSNVMIVELNLEDEKREKIIERRAA
|
Located at the polypeptide exit tunnel on the outside of the subunit.
|
Q5JJF9
|
Q8XXQ3
|
NUOC_RALSO
|
NDH-1 subunit C
|
Ralstonia
|
MTDKLATLQSALEKALGNRIQSLTEAVGEITLVVKAADYLETMRTLRDDATLKFEQLIDLCGVDYSAYGDGAWNGPRFAAVSHLLSVTHNWRVRVRVFAPDDDLPVVASVVDVWNAADWFEREAFDLYGLVFEGHPDLRRILTDYGFIGHPFRKDFPVSGYVEMRYDPVQRRVIYQPVTIEPREITPRVIREDQYGGLKH
|
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.
|
Q8XXQ3
|
Q889X9
|
RL7_PSESM
|
50S ribosomal protein L7/L12
|
Pseudomonas
|
MSISQDDILNAVAEMSVIQVVELIKAFEEKFGVTAAAGSAGPAAAAAVVEEQTEFNVMLLEAGEKKVNVIKAVRELTGLGLKEAKAVVDGAPGIVLEAVAKDAADKAKATLEEAGAKVELK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
Q889X9
|
Q553B1
|
DDX46_DICDI
|
DEAD box protein 46
|
Dictyostelium
|
MDEYDKKRRLEHGGSDRSRSSNDNRNSHGSSGNNYRDDRKDDRYYRDDRSHYNNNNNNNNNNNNNNNNNNGNGYRDDRNYSSQNKYQNHHQQSPPQQQQQQQNSSYVPSQPPQQQTQTQQQPHIQAPPPAKPRKSRFDQAPETIPIQAPQQPPMISNQPIFKQQPMYQQPMYQQKQQQPQPPIFQQQQKQQQPPIFQHHQPPPIYQQPPVYQQQQQQQQPVFQQQQQQRVATEAIQFQQTPQQLAIEQERLKQERENEKKIEQANLEEEMKKRREKVEQWRKQKLEQELKASGSSNSGSTSSPPTTTTTTTKTTAATTTATTSPLTIPSQQQQTATTSPIKKKWSLEEEEETAQPLVNTNIEQKEIKLPPTANIPAAAATTTSATINTTTIKQSIEEDDDIDPLDAYMENLNKEANLNLKKSKTSQMIDDDEKLEEESEGEDDGKDKTIKKGKKEMLHTDHTSIKYAEFQKNFYIEVPVLANMTETEVLDFRSELGVKITGKDCPKPIQSWAQAGLTEKVHLLLKKFQYEKPTSIQAQTIPAIMNGRDLIGIARTGSGKTLAFLLPMFRHILAQPKSAPGEGMIALIMSPTRELALQIHVECKKFSKVLGLRTACVYGGASISEQIAELKRGADIVVCTPGRMIDILCANNRRITNLRRVTFLVLDEADRMFDMGFGPQINCIVDSIRPDRQTIMFSATFPPKVENVAKKILNKPLEIIAGGRSIVSSDIEQFVEVRPTETRFRRLIELLSIWYHKGQILIFTNRQETTDNLYRQLSNSQYQCLSLHGSKDQTDRDETISDFKNKVKTILIATPLASRGLDIKDLNLVVNFDCPDHLEDYVHRVGRTGRAGNRGTAYTFITPDEERFSSSIIKALEQSGSKVPDELRKLNDTYEKKRKEGKDVLLAPTGFTGRGHKFDAAEEDKKNIERKQQRKAYGIEEEEEEEDEDKEKAEKEKLAAASAEKEKQLLSEKEKLDPATTNTIVIPGVDGTIITPSSLLQTDPSVPVGQQAINQIFGISQVTSSEEAIKKLQLAAQLGMKGNIQKLNNQITPLNQTHFIEELEINDYSQQARWKVTHKDALLEITNFTNTTITTKGTFFPPNKIPAPGERKLYLYIEGPSDASVKNAKSDIKKILDEVQSTHQSTGKYSVF
|
ATP-dependent RNA helicase which may be involved spliceosome assembly and in nuclear splicing.
|
Q553B1
|
O68309
|
CH60_AERSA
|
Chaperonin-60
|
Aeromonas
|
MAAKEVKFGNEARIKMLEGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFQNMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVAELQVLSQPCADNNAIAQVGTISANSDEKVGRLIAEAMDKVGRDGVITVEDGQGLDDELAVVEGMQFDRGYLSPYFVNKPETGAVELDDPFILLVDKKVSNIREMLPVLEGVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIAMLTSGGTVIEEVGMELEKATLEDLGRAKRIVITKENTTIIDGVGDAALIESRVAQIRQQIEETSSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALHATRAAVEEGVVAGGGVALVRVAAKLAGLRGDNEDQNVGIKVALRAMEAPLRQIVINAGEEASVIANAVKNGEGNFGYNAYTEQYGDMLAMGILDPTKVTRSALQFASSIAGLMITTECMITELPKKDTPAMPDMGGMGGMGMM
|
Together with its co-chaperonin GroES, 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.
|
O68309
|
A9WW49
|
LEPA_BRUSI
|
Ribosomal back-translocase LepA
|
Brucella
|
MSTPLDHIRNFSIVAHIDHGKSTLADRLIQLTGGLDTREMKDQVLDSMDIERERGITIKAQTVRLSYKAKNGEDYVLNLIDTPGHVDFAYEVSRSLAACEGSLLVVDASQGVEAQTLANVYQAIDNNHEIVVVLNKIDLPAAEPERVKQQIEEVIGIDASDAVEISAKTGLGIEDVLEAIVNKLPAPKEGDRNAPLKAMLVDSWYDSYLGVIVLVRVIDGVLKKGQTIRMMGTGAKYPVERTGVFTPKMVQVDDLGPGELGFITASIKEVADTRVGDTITEDRRPTENMLSGFKPAQPVVFCGLFPVDAADFEDLRGAMGKLRLNDASFSFEMETSAALGFGFRCGFLGLLHLEIIQERLEREFNLDLITTAPSVVYRLNMTDGTHKELHNPADMPDVVKIASIEEPWIKATIMTPDDYLGAIMKLCQERRGIQIDLTYVGPRAMITYDLPLNEVVFDFYDRLKSISKGYASFDYNLSDYREGDLVKMSILVNEEPVDALSMLVHRSAAEKRGRALCEKLKELIPQHMFKIPIQAAIGGRIVARETISALRKDVTAKCYGGDVTRKRKLLEKQKEGKKRMRQFGKVEIPQEAFIQALKMGDD
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
A9WW49
|
B8EBG3
|
ARGC_SHEB2
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Shewanella
|
MKNIAIIGASGYTGAQLTALIHAEADLTIQGLYVSENSLDKGKPLADLYPSYSHIALTLSPLSDDAKAKIVAEADAVVLATEHSVSLHLAAWFYSQGLAVFDLSGAYRFSDVAQYPKWYGFEHEYPEVLAKAVYGLAEWNAKEIAATKMIAVPGCYPTASLTALKPLASLLTSAYPVINAVSGVTGAGRKAQLHTSFCEVSLTPYGVLGHRHQPEIVTQLGQEVIFTPHLGNFKRGILATITVQLKPGTTTADVAAAYSVYDQAPLVTVKHNQFPKVDDVVLTPNCHLGWKFDENSGYLVVASAIDNLMKGAASQALQCIKIHFNL
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
B8EBG3
|
Q6ABV4
|
YIDD_LEIXX
|
Putative membrane protein insertion efficiency factor
|
Leifsonia
|
MLRGYRAVFSPFYGDVCRYYPSCSAYTLQAVQEHGVIFGGYLGVCRILRCHPWAAGGVDDVPLRGKRRYRMTAFGFVVATSQGKA
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q6ABV4
|
A1WR02
|
MDH_VEREI
|
Malate dehydrogenase
|
Verminephrobacter
|
MNKKPVRVAVTGAAGQIGYALLFRIASGEMLGKDQPVILQLLEVPAEGPQKALNGVMMELDDCAFPLLAGMTAHSDPMAAFKDADYALLVGSRPRGPGMERAELLAVNGAIFIAQGKALNAVASRQVKVLVVGNPANTNAFIAMQSAPDLPRKNFTAMLRLDHNRAVSQIAAKTGQAVADIEKLTVWGNHSPTMYADYRFATAGGQSVAAMINDQAWNANVFLPTVGKRGAAIIEARGLSSAASAANAAIDHMRDWALGSNGRWVTMGIASDGQYGIPKDIVFGFPVTCANGEYQLVQGLALDAFSQQRIQATLAELQAEQDGVRHLL
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
A1WR02
|
Q3B5D7
|
MURA_CHLL3
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Pelodictyon
|
MDKLVITGGKRIEGEITASGSKNSSLPIIAATLLSGSGTFTLHRIPDLQDITTFRQLFDHLGAETAFSHNTLTITTANVQSVLAPYELVKKMRASIYVLGPLLARFGHARVSLPGGCAFGPRPIDLHLMAMEKLGARITIETGFIDAVAEGGRLKGATIDFPVSSVGATGNALMAAVLAEGTTIIRNAAAEPEIEALCHFLQAMGADIRGTGTTELIIHGCDSLRHVEFSNIFDRIEAGTILAAAAITGGSVTIRGVIPSHMESVLQKFSDAGCRIETTDDTVILKSTGRLKATDITAEPFPAFPTDMQAQWMALMTQAEGTSEITDHVYHERFNHIPELNRLGAHIDIEGNRAVVHGPQALSGTKVMSTDLRASASLVLAGLVAEGTTEVLRVYHLDRGYERIETRLQNLGAEIKREKYSEFG
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q3B5D7
|
A7NBQ8
|
YBEY_FRATF
|
Endoribonuclease YbeY
|
Francisella
|
MDNLNINFINDDEHPIPSQDLLLKCLQLVADKHHISHAEVNLNIVSNDEIQQINKQFRNKDKPTNIISFEFEKPQGLPDDIANDFLGDIVIAPAVLENEAKEQNKEINDHWQHIFIHGLLHLLGYDHQDDQEAEVMENLEIQLLAQLGIANPYIEQENQNGR
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A7NBQ8
|
Q1C3Y6
|
ENO_YERPA
|
2-phosphoglycerate dehydratase
|
Yersinia
|
MSKIVKVIGREIIDSRGNPTVEAEVHLEGGFVGLAAAPSGASTGSREALELRDGDKSRFLGKGVLKAVAAVNGPIAQAVIGKDAKDQANIDKIMIDLDGTENKSQFGANAILAVSLAAAKAAAASKGMPLYEHIAELNGTPGKFSMPLPMMNIINGGEHADNNVDIQEFMIQPVGAKTLKEAVRIGSEVFHHLAKVLKAKGLNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEDLTKQYPIVSIEDGLDESDWAGFKYQTEVLGDKIQLVGDDLFVTNTKILKEGIEKGVANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGDRAPFNGLKEVKGQ
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
Q1C3Y6
|
O84222
|
UBIX_CHLTR
|
Flavin prenyltransferase UbiX
|
Chlamydia
|
MKRYVVGISGASGIVLAVTLVSELARLGHHIDVIISPSAQKTLYYELDTKSFLSTIPQNFHNQIVLHHISSIESSVSSGSNTIDATIIVPCSVATVAAISCGLADNLLRRVADVALKEKRPLILVPREAPLSAIHLENLLKLAQNGAVILPPMPIWYFKPQTAEDIANDIVGKILAILQLDSPLIKRWENPR
|
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
|
O84222
|
P04189
|
SUBT_BACSU
|
Subtilisin E
|
Bacillus
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MRSKKLWISLLFALTLIFTMAFSNMSAQAAGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELKKDPSVAYVEEDHIAHEYAQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSSNQRASFSSAGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGNSFYYGKGLINVQAAAQ
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Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
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P04189
|
Q492Q4
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FABH_BLOPB
|
3-oxoacyl-[acyl-carrier-protein] synthase III
|
Candidatus Blochmannia
|
MFTRILGTGSYLPKNIRSNIVLEKMVDTSHEWIVARTGIQERRISTSDETVAKMGYFAAKRALDMSCVHSDKVGIIIVATTSSSHAFPSSACQIQRDLHIRDTIAFDLSAACSGFVYALGVADQYVKNGSVDYALVVGSDTLSHALNPRDRGTLILFGDGAGAVVLGRSKTPGIISIHLHADGDHGDLLTLPNCNRKSPAISNYLTMSGNKVFKIAVSVLARVIDETLNVNNLHRDELDWLVPHQANLRIISATAKRLDMDMRKVVITLDRHGNTSAASVPLALDEAVRDGRIKSGQLVLLEAFGAGFTWGSALLRF
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Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
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Q492Q4
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B9E684
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CLPX_CLOK1
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ATP-dependent Clp protease ATP-binding subunit ClpX
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Clostridium
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MKMAKNDDKKQLKCSFCGKTQDQVRRLIAGPGVYICDECIELCSEIISDEFEEDIQIDMTSIPKPVEIKNYLDQYVIGQEDSKKSLSVAVYNHYKRINSNNNSNDDVELQKSNILLLGPTGSGKTLLAQTLARFLNVPFAIADATTLTEAGYVGEDVENILLKLIQNADYDIERAEHGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQINTTNILFICGGAFDGIDSIIERRTRVSTLGFGAEIQSKKDKDIGKLLKQIMPGDLLKFGLIPEFVGRIPIIVTLEALDRAALISILKEPKNALVKQYKKLFELDDVELEFKDEALEAIADEALKRNTGARGLRAIIEETMKDVMFDIPSKEEIAKVIINKDAVSTKMPELIEAENGKRTPIKLKKSRTRKGPETA
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ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
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B9E684
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A7NGH6
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DCD_ROSCS
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Deoxycytidine triphosphate deaminase
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Roseiflexus
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MTIKSDRWIQVMAREYGMIEPFVAEQVRGGIISYGLSSYGYDMRVADEFKVFTNVFNTLVDPKHFDPRSFVDIRGDYCDIPPNSFALARSVEYFRIPRNVLCIVLGKSTIARCGIIVNVTPLEPEWCGYVTIEISNTTPLPARIYANEGIAQVLFLESDEPPLVSYADKAGKYQNQTGVVPPRL
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Catalyzes the deamination of dCTP to dUTP.
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A7NGH6
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O13853
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ITS3_SCHPO
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PtdIns(4)P-5-kinase
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Schizosaccharomyces
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MKIDSNGIVNPHSITNEIPSYDEKQAVDLNGNAFAPNGTFQKKDLISHKNDFERTMRHDVLHTNPKIEVRSETHIYEPNDSLFKENQDFPSNPTAHSPSSSSNDSVITATGVPDGILRDSPIVSALEPPSSNSSSSPQLQNLKHQLSSPQPSRAPIDRSSSNPVTSSQQPPNDRSTLSSSQKAKRPLKRSYSEKNSSNAEPSGSRSGDRGTNVSTSGSLLDGIPPDIGSASWAEAVKQKRVNMRRRREELDDECVLVGTRVSEGHENYVTAYNMLTGIRVGVSRCQAKMDRELTPADFTARHKFTFDITGNELTPSAKYDFKFKDYAPWVFRHLRQLFHLDAADYLVSLTSKYILSELDSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLREILYDYYEHVKNNPNTLISQFYGLHRVKLPFGRKIHFVVMNNLFPPHRDIHQTFDLKGSTLGRELDENQPCQSPMCTMKDTNWIRRNMHLQFGPLKRQIFLTQVKADIDMLSSLGIMDYSLLVGIHDLSRGNRDKIRNSILSVYDPNVSQHRVPSINGNESHSNVHVIRQVVNSTGPVSLDQSCNLLPTDQFVERRNFMFYSDDGGFQATDENNEPGNFIFYIGIIDLLTKYSYVKRVEHLWKGINHSDSVISAVPPAEYASRFYKFVESSIKPTLLVLKPFPLKPQDGQRVNKQQSVNAGNVRTNNKHGSLNNNTAPSSRNAKSTSAHKSPKTEHRFPFPCRNVTTNTSSS
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Involved, together with the calcineurin ppb1, in cytokinesis.
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O13853
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Q1D8I9
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TPIS_MYXXD
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Triose-phosphate isomerase
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Myxococcus
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MATARRRKIVAGNWKMNKSVPEALALVRDLRGQVASLGDTVEVVVAPPFVALQPLHVALEGAPLALAAQNCHWESSGAFTGEISAPMLAELGCAYVIVGHSERRQLFGDTDEQVNKRAKAVRAAGMTPIICVGETLAEREANQTLAVVERQVRGALEGFGAKEVAGFVLAYEPVWAIGTGRNATAAQAQEVHAAIRGLVERLYDGETAGRVRIQYGGSVKPDNAAELLGQPDVDGALVGGASLKAGDFAAIVKAAT
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Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
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Q1D8I9
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C1KVC1
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GRPE_LISMC
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HSP-70 cofactor
|
Listeria
|
MSEKKNKKERLADEIEQEELNILDETEETVEEEAAADTLTEEQAKILELENKLDEVENRYLRMQADFENVKKRHIADRDASQKYRSQSLAQDLLPALDSFEKALATTSDQEEVKQILKGMEMVYNQILVAFEKEGIEVIPAVGEQFDPNFHQAVMQDSDENAGSNEITAELQKGYKLKDRVIRPSMVKVNQ
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Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
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C1KVC1
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A1RMG0
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ANMK_SHESW
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AnhMurNAc kinase
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Shewanella
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MKNAYYIGLMSGTSMDGVDAVLVDFSGPQPQLICSHTEAIPSHLLKGLQRLCLPGADEINRLGRLDRNVGQLFALAVNNLLAKCNIAKEDIIAIGSHGQTVRHMPNLEVGFTLQIGDPNTIATETGIDVIADFRRKDIALGGQGAPLVPAFHQQTFAEIGKKRIILNIGGIANVTYLPGTSEHVLGFDTGPGNTLIDAWIQHVKSEPFDKNGEWAASGKTNPDLLAQLLSHPYFSLAYPKSTGRELFNQAWLEQQLSPFNHLDEEDIQSTLLDMTCHSIARDVIKLSPEGELFVCGGGAFNTQLMQRLAALLPGYKLDTTSALGVDPKWAEGIAFAWLAMRNHLGLPANLPAVTGASREAVLGGRFSAK
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Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
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A1RMG0
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Q5I2B2
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AMP_AMARE
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Antimicrobial peptide Ar-AMP
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Amaranthus
|
MVNMKSVALIVIVMMAFMMVDPSMGAGECVQGRCPSGMCCSQFGYCGRGPKYCGRASTTVDHQADAAAAAATKTANNPTDAKLAGAGSP
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Chitin-binding protein that inhibits the growth of the fungal pathogens B.cinerea, F.culmorum, H.sativum and A.consortiale, but not that of R.solani. Induces morphological changes in the fungal pathogens F.culmorum, H.sativum and R.solani, but not in A.consortiale and B.cinerea. Has antibacterial activity against the Gram-positive bacterium B.subtilis, but lacks antibacterial activity against the Gram-negative bacterium E.coli.
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Q5I2B2
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Q1AYW0
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RLMN_RUBXD
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tRNA m2A37 methyltransferase
|
Rubrobacter
|
MGLAGAQERAGRPLAAEFLPEVEEVLAERGEPPYRLRQVYAALAGSLASGWDEVASLPKGLREELAGRVPASVLELRRISRARDGTRKYLFFTRDGHAIETVMIPERSRRTVCISTQVGCPMACTFCATGLLGIKRNLKAREIAEQVFAVARDIAPERVTNVVVMGMGEPFLNYRETLRALRVLNDRRGFNLAARHIAVSTSGLVDKIRRFADEPEQFHLAISLHTPFEEERRRLMPVAARHPIPELMNAARYYVERTRRKLFFEYTLLAGVNDRMRHAEALAELLDHPLYHLNLLRFNWTDTGFSATSARRAKEFLRRARELGLSATLRPSRGQDIEAACGQLAARDARSPTAR
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Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
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Q1AYW0
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O79229
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CYB_THAIM
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Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
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Thalassarche
|
MAPNLRKSHPLLKMINNSLIDLPTPSNISAWWNFGSLLGICLMTQILTGLLLAMHYTADTTLAFSSIAHTCRNVQYGWLIRNLHANGASFFFICIYLHIGRGFYYGSYLNKETWNTGILLLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFMIAGLTLIHLTFLHESGSNNPLGILSNCDKIPFHPYFTLKDILGFTLMFLPLTALALFSPTLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLSPLLHKSKQRTLTFRPLSQLLFWLLVTNLFILTWIGSQPVEHPFIIIGQLASITYFTILLVLFPTIAALENKMLNY
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Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
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O79229
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Q31ZV3
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TRPA_SHIBS
|
Tryptophan synthase alpha chain
|
Shigella
|
MERYESLFAQLKERKEGAFVPFVTLRDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS
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The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
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Q31ZV3
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Q84VG1
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CHMP1_ORYSJ
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Protein CHROMATIN MODIFYING PROTEIN 1
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Oryza sativa
|
MGNPEKLMTQIFDLKFTSKSLQRQARKCEKEEKEQKLKVKKAIEKGNMDGARIYAENAIRKRTEHMNYLRLASRLDAVVARLDTQAKMQVIGKSMANIVKSLDSALATGNLQKMSETMDNFERQFVNMEVQAEFMEGAMAGSTSLSTPETEVNSLMQQVADDYGLEVSVGLPQAAAHAIPAAKEKEKAVDEDDLSRRLAELKARG
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Involved in ESCRT-dependent multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
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Q84VG1
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B4SP54
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HUTI_STRM5
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Imidazolone-5-propionate hydrolase
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Stenotrophomonas maltophilia group
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MHVDTLWSNVHLITLDGEGLGVIRDGVLACADGRIVHVGPAGSDANLRPTTRIDGEGRWMSPGLIDCHTHLVYAGNRANEFEQRLQGISYAEIARAGGGIVSTVRATRAATPEQLASESRPRLLAMRAEGVTTLEIKSGYGLTLPDERKQLQVARALGEGCRVNVVTTFLGAHAIPPGREAQEYTDEVCNVMIPAIAAEGLAEAVDVFCENIAFSPAQARQVFEAARAHGLAIKIHAEQLSNQHGAELAASFGALSADHIEHLDDAGIAAMAAAGTVAVLLPGAFYFTRDTTLPPIAALRAAGVPLALATDSNPGTSPLTSPLLAMNMGATLFRLTVDECIAGFTREAARALGRGDRIGRLAIGMDCDLAIWDIDAPADLVYRIGFNPLHARVVRGQPDLPASWSNT
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Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
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B4SP54
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P09020
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HXC5_XENLA
|
XlHbox-5
|
Xenopus
|
EFRQIYPWMTKLHMSHETDGKRSRTSYTRYQTLELEKEFHFNRYLTRRRRIEIANNLCLNERQIKIWFQNRRMKWKKDTKVKSKDSM
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
P09020
|
Q8QZV2
|
SHSA2_MOUSE
|
Transmembrane protein 46
|
Mus
|
MWGGRCSPSTSSRHRASLLQLLLAALLAAGARASGEYCHGWLDAQGVWRIGFQCPERFDGGDATICCGSCALRYCCSSAEARLDQGGCDNDRQQGVGEPGRTDREGPDSSAVPIYVPFLIVGSVFVAFIILGSLVAACCCRCLRPKQDPQQSRAPGANRLMETIPMIPSASTSRGSSSRQSSTAASSSSSANSGARAPPTRSQTNCCLPEGTMNNVYVNMPTNFSVLNCQQATQIVPHQGQYLHTPYVGYAVQHDSVPMTPVPPFMDGLQPGYRPVQPPFAHTNSEQKMFPAVTV
|
Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling.
|
Q8QZV2
|
A1JII9
|
RSD_YERE8
|
Regulator of sigma D
|
Yersinia
|
MLNRLESLTQRVGGSNELIDQWLHARKELLVSYCTVIGIKPQKGKHTPLNEKALENFCHNLVDYLSSGHFHIYDRIIKQVEGASSPKMALTTKVYPALKNNTQTIMAFHDRYTNIEIDDDSCTEFQQALSDIGEALDARFRLEDQLIQWAAESWQAAKPVIQAGQVK
|
Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.
|
A1JII9
|
A0A075TRB3
|
PATN_PENEN
|
Patulin biosynthesis cluster protein N
|
Penicillium
|
MVLTTGLKGAHVLITGGTRGMGEAMVHKFLQEEANVSYCARTVTNTEYDDFYSTLAEGNTARAVGTAFDVASKDSLVKWVESSAERLGRIDVIIANASPMHMEGETEHWESSFAIDVMGFVELVKAATPYLEKSPQASIIVQSSFMGREFYRSPPAAYGPCKAAQLQHVQELSHFLGPKGIRVNAISPGPVLCKGGPWELYSKINPEWVEEQRLKIPLKRLGGPTEVANVAVFLASPLASFVSGTNMLVDGGIHVGTQF
|
Isoepoxydon dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria . PatN catalyzes the conversion of isoepoxydon into phyllostine . The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
|
A0A075TRB3
|
Q34179
|
CYB_CEPNE
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Cepaea
|
MAPSLKKIVLWSFLALPSPVNISIWWNIGSLLGLLLAMQIMTGIFLSLHYTPMMVSTFSSMVHIMRDVPGGWLVRASHANGASMFFMLMYAHIGRGVYYQSYILQPRTWLVGGNDFLLSMATAFLGYVLPWGQMSYWGATVITNLLSAVPYLGDSLVTWVWGCFSVNQATLNRFYSFHFLLPFVILVFVLVHLLLLHDKGSSNPLGNMSHVSKVSFHPYFTWKILWVFVLLCFLLYVLLCYITLMYLRTPKTFIEANPMVTPTHIQPEWYFLFAYAILRAIPSKIGGVVALAMSVLYLYTFPLALYSSAAATAYNFIGQLLFWGYVSLFFLLTWLGACPVEEPYISLALPLTVMFFVVPGLYMISSSYIIRSFQFLLSLK
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q34179
|
Q4FQB7
|
TSDA_PSYA2
|
Tetrathionate synthase
|
Psychrobacter
|
MKIIPYRKRSVLIATIFAISAVGITGCSDNTETKAVERVEEAAALARVKDLEARAEALKSNMPAANDMTATAGGTDTASGKPTIKMPDESTIPDDEFGAAVRRGLQISNHTYKELPNNVGNQLNCTSCHLGNGSEAYAAPWNNTPSVYPNYSKRTGRINTIQERINGCFERSLNGKALDLNSDDMNAMVSYMSWLSQDMPFGVSPEGSGFVKVDKTLEPNTDNGKKLFAEKCSVCHGATGEGQYNDDGTYVYPAIAGDKSFNDGAGMARTYTAASFIKGKMPFGQGGSLSDQEAVDIASYFTHLPRPIKANKDKDWPNGDAPKDVRR
|
Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.
|
Q4FQB7
|
A8A7Q7
|
PSD_ECOHS
|
Phosphatidylserine decarboxylase beta chain
|
Escherichia
|
MLNSFKLSLQYILPKLWLTRLAGWGASKRAGWLTKLVIDLFVKYYKVDMKEAQKPDTASYRTFNEFFVRPLRDEVRPIDTDPNVLVMPADGVISQLGKIEENKILQAKGHNYSLEALLAGNYLMADLFRNGTFVTTYLSPRDYHRVHMPCNGILREMIYVPGDLFSVNHLTAQNVPNLFARNERVICLFDTEFGPMAQILVGATIVGSIETVWAGTITPPREGIIKRWTWPAGENDGSVALLKGQEMGRFKLGSTVINLFAPGKVNLVEQLESLSVTKIGQPLAVSTETFVTPDAEPAPLPAEEIEAEHDASPLVDDKKDQV
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
A8A7Q7
|
A2C4J8
|
ATPF2_PROM1
|
F-type ATPase subunit b'
|
Prochlorococcus
|
MPTLFLFGASEGGLFDFDATLPLMAVQVVLLTFILNALFFKPVGRVVEEREDYVNTSRAEAKKKIAEVELLETELKDQLKEARLEAQKVILEAEQDSENLYKEALALATSEANASREKARREIDSQRDEALNQLKSEADNLGDLIIERLLAKK
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
|
A2C4J8
|
Q7BSW5
|
ESPP_ECO57
|
Autotransporter protein EspP translocator
|
Escherichia
|
MNKIYSLKYSHITGGLIAVSELSGRVSSRATGKKKHKRILALCFLGLLQSSYSFASQMDISNFYIRDYMDFAQNKGIFQAGATNIEIVKKDGSTLKLPEVPFPDFSPVANKGSTTSIGGAYSITATHNTKNHHSVATQNWGNSTYKQTDWNTSHPDFAVSRLDKFVVETRGATEGADISLSKQQALERYGVNYKGEKKLIAFRAGSGVVSVKKNGRITPFNEVSYKPEMLNGSFVHIDDWSGWLILTNNQFDEFNNIASQGDSGSALFVYDNQKKKWVVAGTVWGIYNYANGKNHAAYSKWNQTTIDNLKNKYSYNVDMSGAQVATIENGKLTGTGSDTTDIKNKDLIFTGGGDILLKSSFDNGAGGLVFNDKKTYRVNGDDFTFKGAGVDTRNGSTVEWNIRYDNKDNLHKIGDGTLDVRKTQNTNLKTGEGLVILGAEKTFNNIYITSGDGTVRLNAENALSGGEYNGIFFAKNGGTLDLNGYNQSFNKIAATDSGAVITNTSTKKSILSLNNTADYIYHGNINGNLDVLQHHETKKENRRLILDGGVDTTNDISLRNTQLSMQGHATEHAIYRDGAFSCSLPAPMRFLCGSDYVAGMQNTEADAVKQNGNAYKTNNAVSDLSQPDWETGTFRFGTLHLENSDFSVGRNANVIGDIQASKSNITIGDTTAYIDLHAGKNITGDGFGFRQNIVRGNSQGETLFTGGITAEDSTIVIKDKAKALFSNYVYLLNTKATIENGADVTTQSGMFSTSDISISGNLSMTGNPDKDNKFEPSIYLNDASYLLTDDSARLVAKNKASVVGDIHSTKSASIMFGHDESDLSQLSDRTSKGLALGLLGGFDVSYRGSVNAPSASATMNNTWWQLTGDSALKTLKSTNSMVYFTDSANNKKFHTLTVDELATSNSAYAMRTNLSESDKLEVKKHLSGENNILLVDFLQKPTPEKQLNIELVSAPKDTNENVFKASKQTIGFSDVTPVITTRETDDKITWSLTGYNTVANKEATRNAAALFSVDYKAFLNEVNNLNKRMGDLRDINGEAGAWARIMSGTGSASGGFSDNYTHVQVGVDKKHELDGLDLFTGFTVTHTDSSASADVFSGKTKSVGAGLYASAMFDSGAYIDLIGKYVHHDNEYTATFAGLGTRDYSTHSWYAGAEAGYRYHVTEDAWIEPQAELVYGSVSGKQFAWKDQGMHLSMKDKDYNPLIGRTGVDVGKSFSGKDWKVTARAGLGYQFDLLANGETVLRDASGEKRIKGEKDSRMLMSVGLNAEIRDNVRFGLEFEKSAFGKYNVDNAVNANFRYSF
|
Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.
|
Q7BSW5
|
Q73XZ5
|
HRCA_MYCPA
|
Heat-inducible transcription repressor HrcA
|
Mycobacterium avium complex (MAC)
|
MGSADERRFEVLRAIVADFVATKEPIGSKTLVERHNLGVSSATVRNDMAVLEAEGYITQPHTSSGRVPTEKGYREFVDRLDDVKPLSAAERRAIQNFLESGVDLDDVLRRAVRLLAQLTRQVAIVQYPTLSSSTVRHLEVIALTPARLLMVVITDSGRVDQRIVELGDVIDDHELSRLREMLGQALVGKKLSAASVAVADLAEQLRSPDGLGDAVGRSATVLLESLVEHSEERLLMGGTANLTRNAADFGGSLRSILEALEEQVVVLRLLAAQQEAGKVTVRIGHETAAEQMVGTSMVTTAYGTSDTVYGGMGVLGPTRMDYPGTIASVAAVAMYIGEVLGAR
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
|
Q73XZ5
|
Q3YT10
|
DAPE_EHRCJ
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Ehrlichia
|
MAIDPIKLSQELISFPSITPTDNGAIDFLSNTLSQYGFTCHVLTFGDDQVQVRNLYAQLGNGSPNLCFAGHTDVVPTGDSEKWKFDPFSGKIEDNILYGRGVVDMKSAICAFVAAVSRIDFNQINGSISFLISGDEEGNYFKYGTPAVLKWLTDNNKKIDFCLVGEPTSQSSVGDTIKIGRRGSINFKIVCNGVQGHVAYPHLAENPVDNMISILYKISNTVLDNGNEYFQPSNCEITSVDVGNTATNVIPDKITANLNIRYNDMHTSESLFNIINNICAEITEKYELFTAVSGSSFITHPGKHSDMLSSAIKKVTGQDAILSTSGGTSDARFIKDFCPVIELGLSNETAHKINEHAPVDDIYKLTDIYEEFIRQFFNIS
|
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.
|
Q3YT10
|
Q49YY5
|
CH60_STAS1
|
Chaperonin-60
|
Staphylococcus
|
MAKDLKFSEDARQSMLRGVDKLANAVKVTIGPKGRNVVLDKEYTSPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVEVAIEALHEISQNVDNKNEIAQVGSISAADEEIGKYISEAMEKVGNDGVITIEESSGFNTELEVVEGMQFDRGYQSPYMVTDSDKMVADLERPYILITDKKISSFQDILPLLEQVVQSNRPILIVADDVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLELKEATMDMLGTANKAEITKDNTTVVDGDGDQNSIDARVSQIKAQIEETDSEFDKEKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEEGIVAGGGTAFMNIYEKVAKIEAEGDIATGINIVLKALEAPVRQIAENAGLEGSIIVERLKNADIGVGFNAATNEWVNMLEAGIVDPTKVTRSSLQHAASVAAMFLTTEAVVANIPEESNNDAQAGMGGMPGMM
|
Together with its co-chaperonin GroES, 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.
|
Q49YY5
|
C4K764
|
COAD_HAMD5
|
Pantetheine-phosphate adenylyltransferase
|
Candidatus Hamiltonella
|
MSIRVIYPGTFDPITNGHLDLLSRACALFDHVILAIAESPNKKTLFSLNERVDLAKGATAHLNNIEVTSFHGLLIHFAQQKNIPILLRGIRSLSDFEQEWQLCHMNHRIMPELETLFLMPSEKWAFISSSLVKEIAQYRGDVSAFVPDCVKEALLR
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
C4K764
|
O34385
|
MNTA_BACSU
|
Manganese-binding lipoprotein MntA
|
Bacillus
|
MRQGLMAAVLFATFALTGCGTDSAGKSADQQLQVTATTSQIADAAENIGGKHVKVTSLMGPGVDPHLYKASQGDTKKLMSADVVLYSGLHLEGKMEDVLQKIGEQKQSAAVAEAIPKNKLIPAGEGKTFDPHVWFSIPLWIYAVDEIEAQFSKAMPQHADAFRKNAKEYKEDLQYLDKWSRKEIAHIPEKSRVLVTAHDAFAYFGNEYGFKVKGLQGLSTDSDYGLRDVQELVDLLTEKQIKAVFVESSVSEKSINAVVEGAKEKGHTVTIGGQLYSDAMGEKGTKEGTYEGMFRHNINTITKALK
|
Probably part of the ABC transporter complex MntABCD involved in manganese import.
|
O34385
|
B2SZ54
|
TATA_PARPJ
|
Sec-independent protein translocase protein TatA
|
Paraburkholderia
|
MGSLSIWHWLIVLLIVALVFGTKKLRNIGGDLGGAVKGFKEGMKEADAPAAEAQQRELPRNGAVDVEAKEKTPRSGDYR
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
|
B2SZ54
|
A3MX14
|
DPCKG_PYRCJ
|
Dephospho-coenzyme A kinase
|
Pyrobaculum
|
MTCYRLAKRRDLFAFPYPIAIWRDPPKSVEIVRNLVADGGFKHIYTVGDVVTRNFLEYGLIPTSAAVDEKTRRGIRVERFSAFRSVVEVVNPPGYITDEAWSAVEKAVEGGVVVKVRGEEDMLSLAFIRLAPPRSIVAYGHYMGALIAIPVDWYRRDLLKLFDFLEKC
|
Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
|
A3MX14
|
O83958
|
RLPA_TREPA
|
Probable endolytic peptidoglycan transglycosylase RlpA
|
Treponema
|
MMDKRVVAVAAVLWNVQMLFAAGEVIVPEGYASYYAESFNGRPTASGEIFDMNAYTAAHRTLPFGTVVELTNLDNGKKVIVRINDRGPYAANREIDVSKAAAVALDMLNAGVARVSIHKADPNAHASQQRNDRQTSPGVLPQDSFGVPPTAPTSSAPVMYADPHNPPPAPVGRRAGTPGVPGVANTTDVPASEYGAPPVAYAAPGSTPSRVPYGTAVPGSAAPNSHAQPVPSSSSYAAAAPLPYAAGGGKVSGMKSVYTPTHSGETRGVLWRIQLGAFVREENALRLVVKCARRALILHMSEQSTRCAWCCRGYAPRT
|
Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
|
O83958
|
O43513
|
MED7_HUMAN
|
Transcriptional coactivator CRSP33
|
Homo
|
MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKTEPMDADDSNNCTGQNEHQRENSGHRRDQIIEKDAALCVLIDEMNERP
|
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
|
O43513
|
Q92349
|
MUG79_SCHPO
|
Meiotically up-regulated gene 79 protein
|
Schizosaccharomyces
|
MDFRITEGSSPTSLSVSEKIAKLESCNDSRITCRPVRESKPTYTSGQKHSALLSKLKRSKVTTDFCKLEESKGIICQENLHTEGAKSKTENISGEDKSSQRRTRLKQIQEFISHRRSFLNSNANSVESEKILAENNHMFNVKSKLSNKESFIKTRRPRTNGELSDLSLQPKRIFSEPVNSHPSQSMFGNGVRASSGSYSLKRDLKDYEEELPSSKKRQRTPPPIVVTNFPQEIFPSKKISLSAKRRIQGKYSGENVRARIELARERNRKRDYVSNLSKGHTTNALEENPFNLGPNYRASTRKCNRIKEAINLFAAKNGSMEVPPKVSVGDSVLTTSQKFLQVIREKTALLMNQDSNSVQPQALAAAESPTTKAPTTKAPTSEAPPKGHVKQLAKQLGNIYMPQSINNVEPTSHSSISKVVNPSEKVISKIERACLAGNGNVHPSIKMEKNLELNPHPRTLNATEHKINSRIQVSKLNTKNELANADPKMYLLENLSDRLYFCKLAKLLLRKYPLDIAEHQFALVYSRFQRIPLKQISCLKQSLVAYYSVLSEVGITNEIMLRENRFSSPKTPEGLVSISKLLLDDREHLSHDERSYIQQLQSQIKSQSVHHENAAEEIRKMRNLRNSRINSQQVGEKVFVNPDVKTMDIQETFLQDYEDETFANEGLSASKFKEEFLLISDSKSDLNSEEIATPNSLEFKNNPRIKVPRSLLTILNLHDRSQLKLFEVCHNSEFKDPINLSNCLRNLLEKQLLSYNFTDWFASLGSEYENVYVKFISHYDFSSLNVYASFQKLCCDLYYGSDDYIHSPILQVFASCWLKQNSNYGFLNEDIIVKIVLILIDLHKSTYSKKLNSYVVPMETFVKYALEKLRPLISPDSVCILSKEDKKHWLKYKKNRSTFAKLLFSTWSNLPSDIGFILECMLKEYYDTFLKSPFAVPNAVQAQLHNQVRGDLTPKRNRSSLISELMKSSKLLKQESSGNKNSTSLESDAFKESSFVLNEENGGIYAGKEIDLPEPSVIDGRPHFSVFNYTHHMQEEKTHNRLPWHRRGMISYKKMVLSKNNRWVAGYWKKKYCIVDSGKLIFYKSDHLDPNACSNVSPIHREFGLQSCLASPNLPPSINSNRNNVFYLNIPGNECYLFEAPSVLAMNEWIHSLNFNAAMITCPPLPENITNTEYGWGYILTRAEKKAYYTAADGTKTFVGDLAQLTRWSPMDIQGLQDIPRPLRDKVHILRDCVPSLLETCLLFQSLPEKMEKCFAAGSKNYLKAMDNWNRKMKFLYERSMMYKEYQRVLECEYEYRKSHDFYPTLSPVRYPYDFKGL
|
Appears to have a role in sporulation.
|
Q92349
|
B0B8U8
|
GPMA_CHLT2
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
|
Chlamydia
|
MTLLILLRHGQSVWNQKNLFTGWVDIPLSQQGIQEAIAAGESIKHLPIDCIFTSTLVRSLMTALLAMTNHSSQKVPYIVHEERPDMSRIHSQKEMEQMIPLFQSSALNERMYGELQGKNKQEVAVQFGEEQVKLWRRSYRIAPPQGESLFDTGQRTLPYFQERIFPLLQQGKNIFISAHGNSLRSLIMDLEKLSEEQVLSLELPTGQPIVYEWTGQKFTKHAPSLG
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
B0B8U8
|
P51349
|
CH60_PORPU
|
Chaperonin-60
|
Porphyra
|
MSKQILYQDDARKALEKGMDILTEAVSVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEISLEDHIENTGVALIRQAASKTNDVAGDGTTTATVLASAIVKQGMRNVAAGSNPMAIKKGIEKATNFVVSKIAEYAKPVEDTTAIVQVASISSGNDAEVGKMIADAIDRVGREGVISLEEGKSTSTSLEITEGMQFEKGFISPYFVTDLDRMEVLQENPFILFTDKKITLVQQELVPLLEQIAKTSKPLLIIAEDIEKEALATIVVNKLRGILNVVAVRAPGFGDRRKSLLEDMSILTGGQVITEDAGFSLDTVQLDMLGKARRVVVTKDSTTIIADGHEATVKSRCEQIKRQIETSDSLYEREKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAINATKAAIEEGIVPGGGSTNVHISGELFVWAKNNLFEDELIGALIVQRALTYPLRRIAFNAGDNGAVVVEKVKTNDFCIGYDASNGKIVNMYDAGIIDPAKVARSALQNATSIAAMVLTTECIVVDKLEA
|
Together with its co-chaperonin GroES, 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.
|
P51349
|
Q9FPF0
|
DJ1A_ARATH
|
Protein DJ-1 homolog A
|
Arabidopsis
|
MASFTKTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLKNCKSLENMVKKQDSDGRLNAAICCAPALALGTWGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGRIVTSRGPGTTIEFSITLIEQLFGKEKADEVSSILLLRPNPGEEFTFTELNQTNWSFEDTPQILVPIAEESEEIEAIALVDILRRAKANVVIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPYGGICASPAYVFEPNGLLKGKKATTHPVVSDKLSDKSHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQLGKATLV
|
Involved in oxidative stress response. Confers protection against diverse stresses by binding both CSD1 and GPX2 and mediating the cytosolic activation of the Cu-Zn-dependent superoxide dismutase activity of CSD1.
|
Q9FPF0
|
B0UUD1
|
ACCA_HISS2
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Histophilus
|
MSQEFLDFELPIAELEAKIEALRSVSQQDQQINLDDEITRLQKKSAELTQKTFANLDAWQVSQMARHPNRPYTLDYIEHIFTDFQTLAGDRAFADDQAIVGGLARLEERPVMIIGHQKGRSIKEKVKRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSMLKVPIICTVIGEGGSGGALAIGVGDKINMLQYSTYSVISPEGCASILWKSAAKASTAAEVMGLTASRLHELKLIDSIIEEPLGGAHRNYDTMSNNLKKRLLADLADLDKLDQETLLDRRYKRLMSYGYC
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
B0UUD1
|
B0BR42
|
RPIA_ACTPJ
|
Phosphoriboisomerase A
|
Actinobacillus
|
MTQQEMKKIAAQAALQFVKPDTIVGVGSGSTVNCFIDALASMKDQIKGAVAASKASEGRLRAIGIEVFNANEVSELDVYIDGADEITPQGAMIKGGGAALTREKIVSSLAKKFVCIVDGSKQVDVLGTTFPLPVEVIPMARSYVARQLVALGGSPEYREGVVTDNGNVILDVHNFHIIEPLKMEHTINNIAGVVTNGIFAQRYANVTIVGTPEGAKIIE
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
B0BR42
|
A1AV12
|
HLDE_PELPD
|
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
|
Pelobacter
|
MDRKSIESIFNRIRTANCLVIGDLMLDEYLWGKAERISPEAPVQVVDVVREEMRLGGAGNVVNNLVELGAEVTVCSVVGDDDNGQALLEAFGRRGVATDAIFLDATRRTSRKTRVVAAHQQIVRIDRESRVPLSAEVERRVSDWITANAGGFDVILLSDYQKGVLTPGVISATLAAARPGAIPVLVDPKGTDFSRYSGATLLTPNRREAEAASGIAIHDIESLVRAAGVIMERVGLEHLLITRSEEGMSLFSRSAAPMHIPTVAREVFDVSGAGDTVLASLAAGMAAGMEMIEAARLANITAGIAVAKLGTSTVAPAEIINAVALAHSDSDSKIKNRDVLAVLIEAEKARGKRIVFTNGCFDLLHAGHVKYLQKARTLGDLLVLGLNSDASVRRLKGEKRPLIGEQERAHILAALDCIDYVVIFEEDTPLELIAALKPHILAKGGDYTPEGVVGRELVESYGGRVELVSFVDGKSTTNIIERVLERYS
|
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
|
A1AV12
|
O66615
|
SPEH_AQUAE
|
S-adenosylmethionine decarboxylase alpha chain
|
Aquifex
|
MAKTLGLHILADLYGVDADKIDRVEDIRELLEGAVKYANLTKISSHYYQFQPHGATGVVLLAESHISIHTWPEHGLATVDVYTCGDPSKAYRAMDYIITQLNPKRIDKQVHERGIVEEESNQSEAEKLRSILLQV
|
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
|
O66615
|
P36265
|
NUSG_SYNY3
|
Transcription termination/antitermination protein NusG
|
unclassified Synechocystis
|
MSFTDDQSPVAEQNKKTPSEGHWFAVQVASGCEKRVKLNLEQRIHTLDVADRILQVEIPKTPIVKIRKDGARVQGEEKIFPGYVLIRMIMDDDAWQVVKNTPHVINFVGSEQKRHYGRGRGHVLPMPLSHGEVERIFRHVDEQEPVVKIDMEIGDHIMVLSGPFKDFEGDVIEVSPERSKLKALLSIFGRETPVELEFTQVEKQN
|
Participates in transcription elongation, termination and antitermination.
|
P36265
|
A5N361
|
UVRC_CLOK5
|
Excinuclease ABC subunit C
|
Clostridium
|
MFDFEQQLKILPDKPGVYLMKNSLGEVIYVGKAKILKNRVRQYFQKSKNHSEKVRTMVKHISEFEYIVTDSEMEALVLECNLIKKYRPRYNILLKDDKIYPLIKITLNEDFPRIICARNKIKDGAKYFGPYISTGAVYETMEVIKKIFPIRDCKLNIKKGNVKVRPCLNYHIGLCKAPCTGHISKEEYGKIISGVMDFLSGKNKDIIRKLKEDMDTLSENMEFEKAAELRDKIFALEKIIEKQKITTGGFEDEDFINIHSDEKDSCIQVFFSRTGKIIGREHFIIEDTQDLPKGEIVANFIKEFYGGTAYIAKTIYVPEIYDVQLLEDWLSIKKDSKVYIKIPQKGDKKAILNLVEKNARTTLQNFKLKFIQDKKMYETSLEELMEILNLDDIPHRIEAYDVSNIQGVDSVGTMVVFENGRPKHNDYRRFKINEVKGANDYESMKEILRRRFQNGMEEIKRIKERKLEFSAGKFSFFPDLILMDGGKIQVSAALEVLKEFNIDITVCGMVKDDKHRTRGLIYRNEEMPLNRNSNIIKLITRIQDEVHRFAVTYHRSLRSKRVLHSVLEDIPNVGVKRRKELLKRFLSVENIKKASMEELISTPSIDMRTAESIISYFRGYKS
|
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.
|
A5N361
|
P53257
|
TPC1_YEAST
|
Mitochondrial thiamine pyrophosphate carrier 1
|
Saccharomyces
|
MFKEEDSLRKGQNVAAWKTLLAGAVSGLLARSITAPMDTIKIRLQLTPANGLKPFGSQVMEVARSMIKNEGIRSFWKGNIPGSLLYVTYGSAQFSSYSLFNRYLTPFGLEARLHSLVVGAFAGITSSIVSYPFDVLRTRLVANNQMHSMSITREVRDIWKLEGLPGFFKGSIASMTTITLTASIMFGTYETIRIYCDENEKTTAAHKKWELATLNHSAGTIGGVIAKIITFPLETIRRRMQFMNSKHLEKFSRHSSVYGSYKGYGFARIGLQILKQEGVSSLYRGILVALSKTIPTTFVSFWGYETAIHYLRMY
|
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
|
P53257
|
Q8XMY2
|
AZOR1_CLOPE
|
FMN-dependent NADH-azoreductase 1
|
Clostridium
|
MKKLLYITVNSKPEKLSSSKTIGRAFISRFVELNPEFEIEEVDLYKDFIPRLEHKHFSGRSSVVDCETASIDAKTKEEVKRIIELSEQFKNADLYVIAAPLWTLSFPAPLKEYIDCVVQNKITIKVTPEEVKGLLDDKQREMVYIQSSGGEIPWLTKGIFNKGLNYVEDVMKFLGIKKFHQLLVDGTGFSIEEKFKAEDKAVEKIDNVIKDIHFSNKG
|
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
|
Q8XMY2
|
A8ALM5
|
LEU1_CITK8
|
Alpha-isopropylmalate synthase
|
Citrobacter
|
MSQQVIIFDTTLRDGEQALQASLSVKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQTIARQVKNSRVCALARCVEKDIDVAAESLKVADAFRIHTFIATSPMHIATKLRSTLDEVIERAIYMVKRARNYTDDVEFSCEDAGRTPIDDLARVVEAAINAGAKTINIPDTVGYTMPFEFGGIISGLYERVPNIDKAIISVHTHDDLGLGVGNALAAVHAGARQVEGAMNGIGERAGNCSLEEVIMAIKVRQDILNVHTRINHQEIWRTSQLVSQICNMPIPANKAIVGSGAFAHSSGIHQDGVLKNRENYEIMTPESIGLNQIQLNLTSRSGRAAVKHRMDEMGYKESEYNLDNLYDAFLKLADKKGQVFDYDLEALAFINKQQEEPEHFRLDYFSVQSGSNDIATASVKLACGDDIKAEAANGNGPVDAIYQAINRITDYNIELVKYSLSAKGHGKDALGQVDIVANYNGRRFHGVGLATDIVESSAKAMVHVLNNIWRAAEVEKELQRKAQNKENNKETV
|
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
|
A8ALM5
|
Q9FX68
|
ZWIP6_ARATH
|
WIP-domain protein 6
|
Arabidopsis
|
MYNNNQYSFSGDEDSVVLSLGPPGQQYPSHNKPTSTKPSSDHEFNHPLTNPNGVTVALHIGPPSSDKETLSGGNNQEGLTARQGQYWIPSLSQILVGPTQFSCSVCNKTFNRFNNMQMHMWGHGSQYRKGPESLRGTKSSSSILRLPCYCCAEGCKNNIDHPRSKPLKDFRTLQTHYKRKHGAKPFRCRKKCEKTFAVRGDWRTHEKNCGKLWFCVCGSDFKHKRSLKDHVRAFGDGHAAHTVSDRVVGIGDADEDDEEEEEEEEDDVEEEDAHEENVRGEKNYGIRYDHFRRYGQISDDNY
|
Probable transcriptional regulator (Probable). Involved in leaf vasculature patterning .
|
Q9FX68
|
P20474
|
PA2B3_BOTAS
|
Phosphatidylcholine 2-acylhydrolase
|
Bothrops
|
MRTLWIMAVLLVGVEGSLIEFAKMILEETKRLPFPYYTTYGCYCGWGGQGQPKDATDRCCFVHDCCYGKLSNCKPKTDRYSYSRKSGVIICGEGTPCEKQICECDKAAAVCFRENLRTYKKRYMAYPDLLCKKPAEKC
|
Snake venom phospholipase A2 (PLA2) that displays local myotoxic activity. It also displays anticoagulant action in plasma and edema-inducing activities . In addition, it shows cytotoxic activity to a variety of cell types and bactericidal activity to a variety of Gram-negative and Gram-positive bacteria . PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P20474
|
Q5PFR0
|
PHNW_SALPA
|
AEP transaminase
|
Salmonella
|
MTSRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNIGVVEQIRQQLTALATASEGYTSVLLQGSGSYAVEAVLGSALGPQDKVLIVSNGAYGARMVEMAGLMGIAHHAYDCGEVARPDVQAIDAILNVDPTISHIAMVHSETTTGMLNPIDEVGALAHRYGKTYIVDAMSSFGGIPMDIAALHIDYLISSANKCIQGVPGFAFVIAREQKLAACKGRSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQALKELAKEGGVAARHQRYQQNQRSLVAGMRALGFNTLLDDELHSPIITAFYSPEDPQYRFSEFYRRLKEQGFVIYPGKVSQSDCFRIGNIGEVYAADITALLTAIRTAMYWTK
|
Involved in phosphonate degradation.
|
Q5PFR0
|
Q0SWK0
|
MSCL_CLOPS
|
Large-conductance mechanosensitive channel
|
Clostridium
|
MWKEFKEFAMKGNVIDLAIGVIIGGAFGKIVTSLVNDIIMPVIGRLVGKVDFSNLYINLSGQQFNSLQEAQAAGAATINYGLFLNNLINFLIIAFSIFIVIKQINKLKNFTKKKEEVQVEATEKDCPYCCTKIDIKATRCPHCTSVLEEATNQSS
|
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
|
Q0SWK0
|
Q0BQH9
|
AROA_GRABC
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Granulibacter
|
MSENHSEGASRPVISRRPAAGLRADHPVHVPGDKSISHRALMIGALAVGETRISGLLEGEDVLRTAAAMRALGAEVVRDAPGSWRVAGRGIGGLTEPADVLDMGNSGTAARLLTGVLASHDLFAVMTGDASLRKRPMRRVTDPLAACGAGFHTRSGGRLPMAVRGTGEALPLHYRLPVASAQVKSAILLAGLNARGETVVEEPHATRDHSENMLRHFGATVQVEPTGDGAGRIVRLQGQPELRAADIVVPADPSSAAFPLVAALLVPGSEITLAGVGLNPLRTGLFDTLVEMGAALTIANRRIEGGEPVGDITVRASTLHGVEVPPERAPSMIDEFPILSVAAAVASGTTRMRGLAELRVKESDRLAATAALLSVNGVQVEIEGDDLIVIGCGGPPPGGGLVTTYMDHRLAMSALVLGLTTQAPVTADDAAFIDTSFPGFATLMTGLGADFSCA
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
Q0BQH9
|
O79434
|
NU3M_RABIT
|
NADH dehydrogenase subunit 3
|
Oryctolagus
|
MNLMLVLLINTTISLVLVTIAFWLPQLNIYSEKSSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWAAQFNNLNLVLIMALMLISILALGLAYEWIQKGLEWVE
|
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. Essential for the catalytic activity of complex I.
|
O79434
|
O94556
|
APC8_SCHPO
|
Cell untimely torn protein 23
|
Schizosaccharomyces
|
MTVSLNTMMGVDGLEDQEQLREIRNCLLKCISECSERGLVYAVRWAAEMLNGMNPIEMEHIPFSSTPTGEFDLDPDMANEKLLEVEEKNIYLLAKSYFDCKEFERAAYTLQNCKSSKSIFLRLYSKYLAGEKKSEEENETLLNTNLTLSSTNREFYYISEVLESLHYQGNKDPYLLYLSGVVYRKRKQDSKAIDFLKSCVLKAPFFWSAWLELSLSIDSLETLTTVVSQLPSTHIMTKIFYVYASHELHQVNSSAYEKLAEAEIIFPNSRYLKTQRALLTYDSRDFDEAESLFENILTNDPYRLDDMDTYSNVLFVLENKSKLGFLAQVASSIDKFRPETCSIIGNYYSLLSEHEKAVTYFKRALQLNRNYLSAWTLMGHEYVELKNTHAAIESYRLAVDVNRKDYRAWYGLGQTYEVLDMHFYALYYFQRATALRPYDQRMWQALGNCYEKIDRPQEAIKSYKRALLGSQTNSSILVRLGNLYEELQDLNSAASMYKQCIKTEETEISPETIKARIWLARWELGKKNYREAELYLSEVLNGDLELEEAKALLRELRSRMEHSYD
|
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 is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates.
|
O94556
|
Q8I6R5
|
CA12_CONIM
|
Alpha-conotoxin ImII
|
Stephanoconus
|
IVRRACCSDRRCRWRCG
|
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks neuronal mammalian alpha-7 (human and rat) and alpha-3/beta-2 (human) and muscle alpha-1-beta-1-delta-epsilon (human) nAChRs . Acts voltage-independently . Does not competes with alpha-bungarotoxin for binding to the receptor . Binds to a different site than alpha-conotoxin ImI .
|
Q8I6R5
|
A4VPN7
|
RS15_PSEU5
|
30S ribosomal protein S15
|
Pseudomonas
|
MALSVEEKAQIVNEYKQAEGDTGSPEVQVALLTANINKLQDHFKANGKDHHSRRGLIRMVNQRRKLLDYLKGKDTTRYSALIGRLGLRR
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
A4VPN7
|
P43415
|
RL15_STRSC
|
50S ribosomal protein L15
|
Streptomyces
|
GQMPLHMRLPKLKGFKNPFKTEFQVVNLDKLAALYPEGGEVTVADLVAKGAVRKNSLVKVLGQGEISVALQVTVDAVSGSAKEKITAAGGTVTELV
|
Binds to the 23S rRNA.
|
P43415
|
Q6GJA7
|
SDRC_STAAR
|
Serine-aspartate repeat-containing protein C
|
Staphylococcus
|
MNNKKTATNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNEATAPSENKTTEKVDSRQQNNVEQSTTSNQPKVNESDNTSVKETTEEPQNTTSTQPTKKNNDATANKDNLAAQNISTQANDVSATPKTTTIKPRTLNRMAVNTVAAPQQGTNVNDKVHFSNIDIAIDKGHVNSTTGKTEFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSTTNTTTYTFTNYVDQYTNVSGSFEQVAFAKRENATTDKTAYKMEVTLGNDAYSEEIIVDYGNKKAQPLISSTNYINNEDLSRNMTVYVNQPKNTYTKETFVSTLTGYKFNPDAKNFKIYEVTDQNQFVDSFTPDTSKLIDVTDKFKITYSNDNKTATVDLMNGQTNSNKQYIIQQVAYPDNTSTDNGKIDYTLDTDKTKYSWSNSYSSVNGSSTANGDQKKYNLGDYVWEDTNKDGKQDANEKGIKGVYVILKDSNGKELDRTTTDENGKYQFTGLGNGTYSVEFSTLAGYTPTTVNAGTDDAVDSDGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKGVKVTLQNEKGEVIGTTETDENGKYRFDNLDSGKYKVIFEKPAGLKQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYFEEETSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMSATKDHHNKAKALPETGSENNGSNNATLFGGLFAALGSLLLFGRRKKQNK
|
Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion.
|
Q6GJA7
|
B5FRF3
|
NRFA_SALDC
|
Ammonia-forming cytochrome c nitrite reductase
|
Salmonella
|
MARKTLRARRFFSLIFPFFFITSVYAEQTPESAKTVTVEAKNETFAPQHPDQYQSWKATSEQSAREDALAEDPRLVILWAGYPFSRDYNKPRGHAYAVTDVRETLRTGAPKTAEDGPLPMACWSCKSPDVARLIQQEGEDGYFHGKWARGGPEIVNDLGCADCHNTASDDFAQGKPALTLSRPYAERAMEAIGKPFDKAGRFDQQSMVCGQCHVEYYFDGKNKAVKFPWDEGMKVENMEQYYDAIAFSDWTNSLSKTPMLKAQHPEYETWSAGIHGKNNVTCIDCHMPKVQNAEGKLYTDHKIGNPFDNFAQTCANCHTQDKASLQKVVAERKQAIHDLKIKVEDQLVHAHFEAKAAWDAGATDAEMKPILNDIRHAQWRWDLAIASHGIHMHAPEEGLRMLGSAMDKAADARTKLARLLATKGITHEIPLPDISTKEKAQKAIGLNMQQINAEKQDFLKTVVPQWEDQARKNGLLSQ
|
Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.
|
B5FRF3
|
A9BD32
|
RSMH_PROM4
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Prochlorococcus
|
MKDKVNVATSTFNHTPVLANELIEIIKKLPEDLIKNCLIIDATIGGGGHSSLVLETFPGISVIGLDQDPKAVAAASEHLKIFGDRAKIETTNFSNFTPSKKVAMVFADLGVSSPQLDEGSRGFSFRLNGPLDMRMNQIDGTNAAELIDRLSENELANLIFKYGEERFSRRIAKRIKHDLAKQGPYSGTIALAYAIAGCYPPKLRNRRVHPATKTFQALRIAINHELDVLSVLLKKAPEWLLDDGLFAVISFHSLEDRLVKKSFLTDTRLERITRKPLIATTNEISINPRSRSAKMRVARRIEAIK
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A9BD32
|
Q9C8M3
|
GSTUS_ARATH
|
GST class-tau member 28
|
Arabidopsis
|
MGKENSKVVVLDFWASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVHKKVPVLIHNNTPISESLIQVQYIDETWTDAASFLPSDPQSRATARFWADYADKTISFEGGRKIWGNKKGEEQEKGKKEFLESLKVLEAELGDKSYFGGETFGYVDITLVPFYSWFYALEKCGDFSVEAECPKIVAWGKRCVERNSVAATLPESEKVYQQVLKLRQIFGVE
|
May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
|
Q9C8M3
|
Q03L46
|
METE_STRTD
|
Methionine synthase, vitamin-B12 independent isozyme
|
Streptococcus
|
MSTTIIGFPRLGEFRELKFTTEKYFRNEITADELLAAAKDLRAKHWNIVKEKGITEIPSNDFSHYDNFLDAAFLFNVVPESVKNLDLTELEQYFALARGYQGEKGDVRALPMKKWFNTNYHYIVPKFEKTTAVKLAGHKIFDEYQEAKDLGLDTRPVVVGPFTFLQLSDFEDGVKAEDFVDSFIAAYQDVFAKLAELGATRIQLDEPALVKDLTADEKALFLNLYNKILADKKGLEVLIQTYFGDVRDVYNDLVNLPVDAIGLDFVEGKKTLELVKGGFPADKTLYAGIVNGKNIWRNNYEKSLAVLEQIPAEKIVLTSSCSLLHVPFTTANEEFEPAILNHFAFAVEKLDELRDLDAIRNGQGAESLAANKELFAIERVGANAELRARIAGLTEADYTRLPAFAEREAIQKDAFKLPLLPTTTIGSFPQTKEVRAKRLAFRKNELSQEEYDAFLAEIIDEWIKWQEEVGFDVLVHGEFERNDMVEYFGQNLSGYLFSKNGWVQSYGMRGVKPPIIWGDVTRLNPITVKWSSYAQSRTDKPVKGMLTGPVTILNWSFPREDISIKDSTLQIALAIKDEVLDLEAAGIKIIQIDEAALREKLPLRRSDWYEDYLDWAIPAFRLVHSTVAPDTQIHTHMCYSEFTDIIPAIDNLDADVISFEASRSNLEILDELKAQNFQTEVGPGVYDIHSPRVPQDGEIDHTIEAILAKVPSSKVWINPDCGLKTRGIKETKESLTKLLEAAKAARKNL
|
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
|
Q03L46
|
B0BWA6
|
RL1_RICRO
|
50S ribosomal protein L1
|
spotted fever group
|
MSNKKDIAVKISGGKKIREAREKVKSDTLYNLTNAVERLKSASYVKFDPTLEIVMKLGIDSRHSDQMVRGVVNLPAGTGKTVRVAVICKEEREEEAKSAGADLVGSTNIIDEIKAGKINFDVCIATPDVMAAIGSVARILGPKGLMPNPKLGTVTLDIKNAIKNAKSGQVEYRAEKAGIIHAGLGKLSFSDQDLLKNLNAFIEAVIKAKPAGLKGSYLKAMYLSSTMGASVQIDLTSIA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
B0BWA6
|
O83940
|
RSMI_TREPA
|
rRNA (cytidine-2'-O-)-methyltransferase RsmI
|
Treponema
|
MGTLYVVATPIGNLADITLRALDVLRTVDVVACEDTRRTRALLSHFGIHKRLVSCRAHNEAQAARRLIHFLSTPISAFLSPEKGRGRQSARRTRARPGETVGTAALQLAAEATGEQEVCGSPHAQVAYVSDAGTPGVSDPGAVLVRAVRDAGHTVVPIPGASALTTLLSVAGVRDKTVLFEGFLSPHPGRRRARLVQLCAQRVAFVLYESPYRVQKLLEDLVAVAPESQVVLGRELTKVHEELCVGTALRVMESFCARTRVRGECVLLVSAEKF
|
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
|
O83940
|
B8F5K4
|
MDH_GLAP5
|
Malate dehydrogenase
|
Glaesserella
|
MKVAVLGAAGGIGQALALLLKLQLPAGTNLALYDIAPVTPGVAVDVSHIPTAVKVVGYAGEDPTPALEGANLVLISAGVARKPGMDRSDLFNINAGIVRNLIEKVATVCPTACVGIITNPVNTTVAIAAEVLKKAGVYDKRKLFGVTSLDVLRSETFVAELKGKDVNDVKVPVIGGHSGVTILPLLSQAFEEDKIDFTAEEVAALTKRIQNAGTEVVEAKAGGGSATLSMAQAAARFARSVLKGLTGEQVVEYAYVEGNGEYARFFAQPVRLGLNGVEELLPIGTLSAYEEEAVQAMIPTLKADIELGEKFVNG
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
B8F5K4
|
A0A2I6PIZ7
|
NODD1_HYPPI
|
Nodulisporic acid biosynthesis cluster protein D1
|
Hypoxylon
|
MDAASTLTHAPVSQPWQSLAQGLGFVNEHEGYWWSKLGPPLGKMMNWARYSTSEQYRVLAFLYKYLLPACGPKPGDDGELFWKVFISYDYTPIQLSLNFHNGKMTLRTANIPISDKSGTADDPINQQASVDAIIRQERVLPSQDLRWFNHFASQYFFDKDTAASLKTKVDKLRVQQGVQCMLSHDFPERDVQCKVAFCPLWKAVATGLSNKEIIWDSILGLGDDIIPYKRALAVLEQYTSSENAAKAGVRPVFFAFDTVLKDNYKSSRIKIYYLTTRTAFNSMVDIYTLGGLLKGPDIQKGVEALEVLWKAVLNVPEGWPDDKDLPMNPHRCAAVIFNFELWPGAEFPSPKAYLPAHYYGRPDLEIADGMDYFFKQQGLDGVYGSYKENYLKCLSEVRTHRTNSQPSTMIFLFHSKGPMPTLRCTTSPSYL
|
Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed . The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB . The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA . NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD-dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable).
|
A0A2I6PIZ7
|
Q4L3K6
|
RS12_STAHJ
|
30S ribosomal protein S12
|
Staphylococcus
|
MPTINQLVRKPRQSKSKKSDSPVLNRGFNSKKKQFTNLNSPQKRGVCTRVGTMTPRKPNSALRKYARVRLSNNIEINAYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYHIVRGALDTSGVDGRRQGRSLYGTKKPKN
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
Q4L3K6
|
Q9XAR1
|
NUOH_STRCO
|
NDH-1 subunit H
|
Streptomyces albidoflavus group
|
MSPYLAAEDLSMFGTDPWWLVVIKAVFCFAFLMVTVLFSIVWERKVVAWMQLRIGPNRHGPWGMLQSLADGIKLMLKEDVIVKRADKAVYVLAPIVAAIPAFMAIAVIPFGPAGNEVSIFGHRTAMQLTDLPIAMLFILAVASVGIYGIVLAGWSSGSTYPLLGGLRSCAQMISYEIAMGAAFASVFLYSGSMSTSEIVAQQDDRWYIVLLPVSFILYIVTMVGETNRAPFDMPESEGDLVGGFNTEYSSIKFAMFMLAEYVNMVTVSAVATTLFLGGWRAPWPISTFWEGANHGWWPLLWFVVKVQLLLFFFIWLRGTLPRVRYDQLMKLGWKVLIPVSLVWLMLVATVRALRNENYGFSDIALYIGGGVLVLLLLSFLVDMYRDKGGKAADQPAETGTGTGTGTETAFDPMAGGFPVPPMPGQQVPPVPRRRPRRERELIVSGGPDTHSDGPAGGPTDGKEASDG
|
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.
|
Q9XAR1
|
A1BGP1
|
HSLV_CHLPD
|
ATP-dependent protease subunit HslV
|
Chlorobium
|
MKHDEQLLIRSTTVLGVIRDGKAALGSDGQMTLGNTVLKHSTRKTRRLYHGQIIAGFAGATADAVTLLDRFEEKLEAFSGRLERAAVELARDWRTDKYLRRLEAMLAIVTAEKALIISGTGDVIEPEDGIVAIGSGSMYALAAARSLLAHTTLSAREIVHESLKIAADICIYTNDHIVIEEV
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
A1BGP1
|
Q7MYF7
|
RS3_PHOLL
|
30S ribosomal protein S3
|
Photorhabdus
|
MGQKVHPNGIRLGIVKPWNSTWYANTKEFADNLDSDFKVRQYLKKELAKASISRIVIERPAKSIRVTIHTARPGIVIGKKGEDVEKLRKTVAEIAGVPAQINISEVRKPELDAKLVADSITSQLERRIMFRRAMKRAVQNAMRQGAKGIKVEVSGRLGGAEIARPEWYREGRVPLHTLRADIDYNTSEAHTTYGVLGVKVWIFKGEILGGMAAVEQAEKPAAQPKKQQRKGRK
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
Q7MYF7
|
P01346
|
IGF2_RAT
|
Preptin
|
Rattus
|
MGIPVGKSMLVLLISLAFALCCIAAYRPSETLCGGELVDTLQFVCSDRGFYFSRPSSRANRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTSQAVLPDDFPRYPVGKFFKFDTWRQSAGRLRRGLPALLRARRGRMLAKELEAFREAKRHRPLIVLPPKDPAHGGASSEMSSNHQ
|
Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
|
P01346
|
P02549
|
SPTA1_HUMAN
|
Erythroid alpha-spectrin
|
Homo
|
MEQFPKETVVESSGPKVLETAEEIQERRQEVLTRYQSFKERVAERGQKLEDSYHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKVKELCAKAEKLTLSHPSDAPQIQEMKEDLVSSWEHIRALATSRYEKLQATYWYHRFSSDFDELSGWMNEKTAAINADELPTDVAGGEVLLDRHQQHKHEIDSYDDRFQSADETGQDLVNANHEASDEVREKMEILDNNWTALLELWDERHRQYEQCLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSLGSAEALLQKHEDFEEAFTAQEEKIITVDKTATKLIGDDHYDSENIKAIRDGLLARRDALREKAATRRRLLKESLLLQKLYEDSDDLKNWINKKKKLADDEDYKDIQNLKSRVQKQQVFEKELAVNKTQLENIQKTGQEMIEGGHYASDNVTTRLSEVASLWEELLEATKQKGTQLHEANQQLQFENNAEDLQRWLEDVEWQVTSEDYGKGLAEVQNRLRKHGLLESAVAARQDQVDILTDLAAYFEEIGHPDSKDIRARQESLVCRFEALKEPLATRKKKLLDLLHLQLICRDTEDEEAWIQETEPSATSTYLGKDLIASKKLLNRHRVILENIASHEPRIQEITERGNKMVEEGHFAAEDVASRVKSLNQNMESLRARAARRQNDLEANVQFQQYLADLHEAETWIREKEPIVDNTNYGADEEAAGALLKKHEAFLLDLNSFGDSMKALRNQANACQQQQAAPVEGVAGEQRVMALYDFQARSPREVTMKKGDVLTLLSSINKDWWKVEAADHQGIVPAVYVRRLAHDEFPMLPQRRREEPGNITQRQEQIENQYRSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKAENTGVELDDVWELQKKFDEFQKDLNTNEPRLRDINKVADDLLFEGLLTPEGAQIRQELNSRWGSLQRLADEQRQLLGSAHAVEVFHREADDTKEQIEKKCQALSAADPGSDLFSVQALQRRHEGFERDLVPLGDKVTILGETAERLSESHPDATEDLQRQKMELNEAWEDLQGRTKDRKESLNEAQKFYLFLSKARDLQNWISSIGGMVSSQELAEDLTGIEILLERHQEHRADMEAEAPTFQALEDFSAELIDSGHHASPEIEKKLQAVKLERDDLEKAWEKRKKILDQCLELQMFQGNCDQVESWMVARENSLRSDDKSSLDSLEALMKKRDDLDKAITAQEGKITDLEHFAESLIADEHYAKEEIATRLQRVLDRWKALKAQLIDERTKLGDYANLKQFYRDLEELEEWISEMLPTACDESYKDATNIQRKYLKHQTFAHEVDGRSEQVHGVINLGNSLIECSACDGNEEAMKEQLEQLKEHWDHLLERTNDKGKKLNEASRQQRFNTSIRDFEFWLSEAETLLAMKDQARDLASAGNLLKKHQLLEREMLAREDALKDLNTLAEDLLSSGTFNVDQIVKKKDNVNKRFLNVQELAAAHHEKLKEAYALFQFFQDLDDEESWIEEKLIRVSSQDYGRDLQGVQNLLKKHKRLEGELVAHEPAIQNVLDMAEKLKDKAAVGQEEIQLRLAQFVEHWEKLKELAKARGLKLEESLEYLQFMQNAEEEEAWINEKNALAVRGDCGDTLAATQSLLMKHEALENDFAVHETRVQNVCAQGEDILNKVLQEESQNKEISSKIEALNEKTPSLAKAIAAWKLQLEDDYAFQEFNWKADVVEAWIADKETSLKTNGNGADLGDFLTLLAKQDTLDASLQSFQQERLPEITDLKDKLISAQHNQSKAIEERYAALLKRWEQLLEASAVHRQKLLEKQLPLQKAEDLFVEFAHKASALNNWCEKMEENLSEPVHCVSLNEIRQLQKDHEDFLASLARAQADFKCLLELDQQIKALGVPSSPYTWLTVEVLERTWKHLSDIIEEREQELQKEEARQVKNFEMCQEFEQNASTFLQWILETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRQLTKIVDLGDNLEDALILDIKYSTIGLAQQWDQLYQLGLRMQHNLEQQIQAKDIKGVSEETLKEFSTIYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEDEHEPKFEKFLDAVDPGRKGYVSLEDYTAFLIDKESENIKSSDEIENAFQALAEGKSYITKEDMKQALTPEQVSFCATHMQQYMDPRGRSHLSGYDYVGFTNSYFGN
|
Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
|
P02549
|
C5BN45
|
RS6_TERTT
|
30S ribosomal protein S6
|
Teredinibacter
|
MRHYEIVFLVHPDQSEQVPGMIERYTSAVKDSGGSVHRLEDWGRRQMAYSINKIHKAHYVLMNIECGDQALEELTTNFRYNDAILRNMVIRCDEAVTEESPIQKAEKENRERKNRAERRAAEAAAATETEKSESEESAEEETSTDTTGEEE
|
Binds together with S18 to 16S ribosomal RNA.
|
C5BN45
|
C4K2D9
|
KDSB_RICPU
|
CMP-2-keto-3-deoxyoctulosonic acid synthase
|
spotted fever group
|
MRHQDVAIIIPSRLSSTRLKQKPLQLIGSITLIERVFKQVNQAGLEHTYVATDSEEIASVITKVGGKVIFTDSAIPTGTNRTYEAFKLIPNNQNINYIVNVQGDMPFIEPSSILKIIEYLKNSKYDIVTPIVKVDRESVKASSNVTVAVDSAGTALYFSRSLIPNGAEEFLYHVGMYGFRKNALEKFVSLKPTFLEKTERLEQLRVLENGMTIGTCLVENVPISVDTEEDLKKAVKFYENISKLGL
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
|
C4K2D9
|
Q5PXQ6
|
CHQB_NOCSI
|
1,2-HQD
|
Pimelobacter
|
MSTPVSAEQQAREQDLVERVLRSFDATADPRLKQVMQALTRHLHAFLREVRLTEAEWETGIGFLTDAGHVTNERRQEFILLSDVLGASMQTIAMNNEAHGDATEATVFGPFFVEGSPRIESGGDIAGGAAGEPCWVEGTVTDTDGNPVPDARIEVWEADDDGFYDVQYDDDRTAARAHLLSGPDGGYAFWAITPTPYPIPHDGPVGRMLAATGRSPMRASHLHFMVTAPGRRTLVTHIFVEGDELLDRDSVFGVKDSLVKSFERQPAGAPTPGGREIDGPWSRVRFDIVLAPA
|
Catalyzes the ortho-cleavage of the aromatic ring of hydroxyquinol.
|
Q5PXQ6
|
O26680
|
DHQS_METTH
|
3-dehydroquinate synthase II
|
Methanothermobacter
|
MKFAWLLAPDTYWDEKKTFITAALESGIDHIVDTADSGRIKKLGNLTLISPDEDADIVLVGRDGEGDGTLELPETLEYSRDIEMASELSESGRQVAAYVEIRSKAHEELARRLGRVVDYLILVGEDWKIIPLENIIADLQEEDVKLIAAVADVDEARVALETLEHGTDGVLIEPADISQIKDIAALLENIESETYELKPATITRIEPIGSGDRVCVDTCSIMGIGEGMLVGSYSQGLFLVHSESLESEYVASRPFRVNAGPVQAYVMVPGGRTRYLSELETGDEVIIVDRDGRSRSAIVGRVKIEKRPLMLVEAEYEGMKVRTLLQNAETIRLVNDKGEPVSVSELGEGDRVLVYFDESARHFGMAIKETIIEK
|
Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
|
O26680
|
P44226
|
VPF_HAEIN
|
Mu-like prophage FluMu F protein
|
Haemophilus
|
MNITWNWYEQLESAHARAFTVAKATKAEVLDTIRWATEQAIANGTGEREYIKKLEPMLKELGWWGKAKDENGNEVQLGSPRRLRTILRTNKITAYHAARYAQQMENVDEQPYWRYVAVNDSRTRASHLALHGKIYRADDPIWQTMYPPNDWGCRCRVEALSEYAVQSRGLKISSSDGEMEMEEAVVGIDKDTGEEIRTTVSKIKTDQGEMKVGAGWNYNVGSAAFGTDVAVLRKLQQVKNRELRQQTIQAINNSEARHKAFADWVLANLGKRGASARYMSAGLVTTEIAEAVTEITQGGKNAELVLVMSEKRLAHANSDKHHEGGVGLTAEEYASISRIVANPSLVLWDTLEGHNNLIYINQERTIQVIVDVPNKHSIKPKEKVDAIINAYKVDMNNVKRQLSGGNYVLLKGKL
|
Involved in virion morphogenesis.
|
P44226
|
Q0RFX5
|
HIS3_FRAAA
|
Phosphoribosyl-AMP cyclohydrolase
|
Frankia
|
MTVRPSALDPAIASRLRRNDAGLFPAIAQQHDTGEVLMLGWMDDEALHRTLTTGRATYWSRSRGEYWVKGDTSGHQQWVRSVALDCDGDAVLVRVDQIGPACHTGTRNCFVADPLPTRVGDPGVTADAGPAR
|
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
|
Q0RFX5
|
Q7WFC8
|
ANMK_BORBR
|
AnhMurNAc kinase
|
Bordetella
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MDSTTHGPRTHVPGRLFIGLMSGTSMDGADGVLVRLDGPRPEVLASASLPMPAALRDELFALNHAGANELERAALAANGLARLYARAVRQLLDQAGLQPGDVAAIGAHGQTVRHRPDLGYTLQLNAPALLAELAGIDVVADFRSRDVAAGGQGAPLVPPFHAALFAGGQARAVLNLGGIANVTLLEPGRPPRGFDTGPANVLLDAWCQRHTGQPYDADGRFAAQGQVLAGLLEHLIASEPWFALAPPKSTGRDLFNLDWLLARLQAFDGPAPQPQDVQATLQRLTARTVANAIDASAAAPRDVLVCGGGARNPGLMRELAYCLQRPVHPTDDAGVPAQWVEALAFAWLAQACLDRIPAGLPTVTGARAARVLGALYPA
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Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
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Q7WFC8
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