ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A932YX88 | ETIEQVKREYKGKRKQIENDHAQAVQRLQAKAAETGEAKTKKAVSELSEERDRKCAELDEDFRLAEGELKELLPLAILSEQEYQERSLKYGHIFHAGIGAEAIRKLLARIDLAATMEAISAELVDAQGQKKEKLIRRLRLLRALHRNHIKPEWMVLTMIPVIPPDLRPMVALDGGRFATSDLNDLYRRVINRNNRLKRLIDLNAPEVIARNEKRMLQEAVDALIDNSARQSKTVMAATGQKRQLKSLADILKGKQGRFRQNLLGKRIDYSGRSVIVVGPDLQLGECGIPKRMALELMKPFVMSKLIAQGLAHNIRGANRV... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 675
Sequence Mass (Da): 75650
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A0A0S7XIB3 | MDFLLEIGVEELPSSYIEPALDELCQKVSSELKEARISCSSIDSYCTPRRLAILVRDIADRQEDIEKEIMGPATRVAYDETGKPTEAGKGFARSQGVPVNSLVKKKTQKGEYVCAIVREQGRPVQKVLSEALPELILSISFPRTMTWADPAARFGRPIRWLVSMLGDKVVPFDVAGVRAGRRTFGNRFLAPRAIELKNPSHYAEKLRRAWVIVDCKERKRLVERLVQEQAGERGGKILEDPELMGIVTNLLEYPVAVLGSFDETFLELPRDVVVTAMREHQRYFAVENEDGSLLPFFVALRNGGAEGEENVRRGNERVLK... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 696
Sequence Mass (Da): 78261
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A0A023BWL6 | MKVLKFGGTSLGSAACFEQVRDIITNIDGSKIVVCSAMAGVTNMLVELVEAIKNDKRDSGKEIILQLQEHHENTVDILRIDAKASKVLKESIASIVKELSYLIDKAFSIELQNQIVTFGEVLSTRVFSGYLASIGVNNTLLMAKDFMYTDSSGSPDITTIREYLNDILQTHKEEKLFITQGFICKDVQGRVNNLGRGGSDYSGTIIGAALQVEEVQIWSDIDGVHNNDPRYVDNTSSIPLLSYQEASVLASFGAKVLHPQTVKPLVDLKIPLYLKNTFTPSATGTKIGDNISPPGIKSIAVKDNMVWLKIRDIPKNENYS... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 445
Sequence Mass (Da): 49387
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A0A4U0VQ46 | MEESRSHWFTEEYTPKRDAAIGAYVHTPASSGAVLREFERALQKAWDEVDKNKELVSDQPTPATETLGDSSSKTTTARPPYRKVLFLRQPYPDNHVDASFLRDLKRNVNVHPANLPALLRQTLPITQHVASIFIFVVVFIRLSRASLSASALLTLCAVLSGTLRAWAWAIGEPTAWVGVTASLMTAARAPLPSTAQNGNGPCCTGDETAPRLRPVDTTASASTSPVGTLIPLVALYLLSPALKTLTRATTSDSIWALSGTLFAINVLLGDYRAIPTSSSFRRDLVPRLFSHASKKPTLSAPERAPHRAPYFARRAPLPST... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Membrane
Sequence Length: 381
Sequence Mass (Da): 41302
Location Topology: Multi-pass membrane protein
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A0A972RDX2 | MQDNLDKKMLLALALSLVVLLVYQVFFTPPPPKKLPHAQKSAQQSVKSTNALQKKSLSATSSKISKEGLSPTKAVNEKKITIETPYYQAVLSTRGATIIGWKLKKYFDDKGQEIVLEKGSPKVPALAIGIDDNFSFGMVNFEVSPDTKKITLTNSGDSASIQFTYSDGQRLIKRTYTFYGNDYKVDVVEEVTGVPNYWLTLGTGFGISGTGGYRGHVGPVILKEADRKEIKPHKVKEPLVFNKDLKWIAQEDKYFFASIVPREKATAKVWRTRSGVVLTAINLPSGKNSYILYAGPKEHDRLKKLGVGLEHIVDFGFFSI... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
C5LZR7 | ILFILTTLTFLVTALSDPGVVPPLEVCAFASIPSFYQIVSYALYVNTVLDLDTARDFSTGHDVRFCTTCKIYRLEGWSHCSECGYCIRGFDHHCAVVNNCIGLRNRRAFV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 110
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 12330
Location Topology: Multi-pass membrane protein
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A0A4R1CHR5 | MSTRKTLVVAGHGMVGHRFVQAAIERGLTERYDVIVYGEEPREAYDRVALTSYYEVGADALSFLPGGKYEDPRAVVTLNTEVTAIDREAKTVALSDGTTQAYDVLVLATGAAPFVPPVPGKDLKNVFVYRTIEDLQAIEEAAKTAKAGVVIGGGLLGLEAANALHKLEVETHVVELAPRLMAVQVDDAGGATLKRHIEKLGLTVHTGVMTEFIDADKDGVEDGKVSGLKFKDVDEVLPADIVIFSAGIRPRDQLARDCGLEVAERGGILVSPNMQTSDESIYAIGECAAPGGRMYGLVAPGYTMAEVAVDALLEGPGEFL... | Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
Function: Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
EC: 1.8.7.1
Catalytic Activity: 3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] = 7 H(+) + 6 reduced [2Fe-2S]-[f... |
A0A2H0Y5A4 | MYRDFFNLPLISKPLWEKLAGSKIKFDLAIASKIIEEVTPLALRELAHSVVIKGFRQGKAPRELLEQHLGKAAIESKILDLALRKSYADFVKQNQLAVIDHPEKTELKQKDPCVFEIIVSVMPELKIGDCQNLKISHQPVETKESEVEDYLNELRKTLAEFKEVQQPAQKGNRLEISLTATDEKNMPVAKLTTQNHPLILGETKILKTLETNLIGMLPKEKKSFQSKLDHLPQDSTLTNQVFNFEVTLNKVEEMILPEVSPEFIQKVTGQSFSLEQFQTEIKNLLLNQKKEQELRRREIELIDALLKITEGEIPLVLVEQ... | Function: 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.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A2H0Y350 | MKILPITQVILSLALIFAILLQHRGAGLSLTFGGTSNSYASRRGIEKILHYATIVLAGLFTLNSILFLVIR | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 71
Sequence Mass (Da): 7740
Location Topology: Multi-pass membrane protein
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A0A521SIC2 | MKEEPMWIDRLDPRVTGGTMKEPPSNILNNLRSLFEEKQKEIRAFHDQGGTGLRVVEALSDLADHLLLRGFQSINPTLVQEWGGAMVAIGGYGRRELSPASDIDLMFLFPQGRAKQAETLASELLPFFWDLGYKIGHSLRSVEECIAAAKQDPLIATSLLESRLLTGDRTLFQQFHEAFFSKVVGKNLKDFLVQLNEGRAEGRKEFGATPYLLEPNLKQSPGGLRDIHHLRWVALARYRTNSLAQLFQWGLLSNAEYSSLTTALDFLWRIRNQLHFKAGKASDHLTMELQEELAPFFHFENRRELMRQYYILTGWVIEIS... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A7C1G6X5 | YAFIPSDELDKERASRKEVFLVRRLGNAIRKLNPWISEENLKKAVREIANVQAVSLMEANEKVHTALVHTISLEQDLGQGKKGQSVHFIDFEHPENNEFVVTRQFRIQGSKKLICPDVVVFVNGIPLVIIECKSPTIQNPIEEAITQLLRYQEIGEKFKGQGAPHLFEPAQILIATCGQVSMFATVGTIHRHYAEWKVPFPMTLDELAGTQPITAKGMYGWGLIHKGRKGRKTRKGGGTPLQSKGGGTPPLQRIPTPQDVLLYGMLYPDNLLDIVRNFIVFEVVGGSTVKKLARYQQFIAVKRAVERILSAKSPARRGGI... | Function: Subunit R is required for both nuclease and ATPase activities, but not for modification.
EC: 3.1.21.3
Catalytic Activity: Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Sequence Length: 873
Sequence Mass (Da): 99701
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A0A7C8E6V1 | KEGNPTPRIVETPSGMLNAIGLQNIGVKEFVSKKLPFLREKNTTVIANFFGDNESEFIETAEILDDTDGIHALELNISCPNKQSNWISFGTDLKLMEGLIKAIRKVVKKTLIVKLTPNTGDIKTSALIAQDSGADALSLINTITGMVIDINTRKPILANNTGGLSGPAIRPIAVRMVWETCQVVKIPVIGIGGIMNLNDALQFFIVGAKAVAVGTANFINPITSIKILDDLRDFIQREELKGINDIIGTIKLHEKTSCPA | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 260
Sequence Mass (Da): 28130
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A0A922WQM4 | MRTVVLENANEAVRALKAGELVALPTETVYGLAGLGLEPEVLAKIFAAKDRPTFDPLILHIARPGQISQLASEVPHDARRLVDNFWPGPLTLVLPKKPHVPDLATAGLGTVAVRCPRHPLMRQVIEKVGSPLAAPSANLFGRLSPTSAEHVVEQLEGRIPYVLDGGACEVGVESTIVGFLPDGVYLLRPGGLPTELIERMIGPLKRPTASGTASGTGSEGGQSAPGQLPQHYAPVTPIVVIDGWHQLLPGDGVLTLKSVPEGHGGPVIQLSAKGNLKEAASRFFEALHELDRAGVPRIAAVRFPEQGLGLALNDRLLRAA... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Len... |
A0A522UXS1 | MDLRCFIAVELPGDLTSRIGAVIDLLSQTGADMKWVKKENLHITLKFLGSTPEASINEIIGALQKKLSHYAPFYIRISGVGSFPPGRHPRVVWIGMDASGQLAAVHKEIDEVMSRYGFKAEERRFSPHLTIGRVRSSRGLTGLITALHEMEPKAFGDVEVRGVALMKSELKPAGPEYERLAEIQFLRRDDVG | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 192
Sequence Mass (Da): 21327
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A0A522UYB8 | MNALPLSDIFGLLPPESKVLLMLPSGNSEERILRSVRRHNRGYIISFHGIHTMTEAALYRNSLVVAEKKILPSLPAGQYFTADIIGLSVVTTAGEILGTVEDVFATGSNDVYVVRDRQREILIPAIKEVVKKIDPEQGVIVVDPMKGMLDET | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A1R4AAN9 | MTTQAIKMPDFGFDRLNTKLEESLITPVTHVTIAESSRSTPIQTLSPQQLERTLFNAATNRNLCQFYSTIQPLLLAGNISLCDDIKALHWASFCGNAEIVKKLLDIGCDVNKVDSINGETPIFFAIKGGSFATIHYLINRFGTPIIVHKNKRGMTPFLVAAAEANQDDISTALRILELFYLYGVSLEEQDENGMTCLLHAARRGSLHVVQWLLARGASLAHRDFLGNAAIHYACFSGNLETVRFICQKGAPSFMDSKSIAKTSEEQTVWGICKLKRNLLLYLLMKIWKLQGVITGHISSLRSPYPFYYWGITIINMLLFM... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 635
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 72872
Location Topology: Multi-pass membrane protein
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A0A967BS39 | MRLAVDLASCGKRTVRSNPLVGCVIVNDGEVVGQGFHRRRGEAHAEVHALDHAGERARGGTAYVSLEPCAHHGLTGPCVERVISAGISRVVIGARDPYPEVDGRSVARLRAAGVTVTTAVCTSDVVHQNRGFFSRLRRSRPWVVAKMACSLDGKTALRSGESKWITGVESRLDVHRLRAEYGAILTGAGTLREDDPSLTVRTSDGREFSPPIRVVLGARHCDVKGKRVTDAGAPSLFFCHEDEEGWDDDRVVRTQGLQGRPDAGECLRALSDRGINNVLVEAGPTLVGALLQQGLIDELVVYIAPVILGSEGRPLLLGNN... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A7X8LAY4 | MSYTALYRKWRPQTFDDVIGQDHIVRTLKNQIAGKRIAHAYLFCGTRGTGKTSTAKIFAKTVNCQHSIEGNPCNQCELCRDQMEGSGMNVIEIDAASNNGVDNIREIREEVKYSPAKGRYKVYIIDEVHMLSTGAFNALLKTLEEPPPHIIFILATTDPQKIPATILSRCQRFDFRRISIGEMTQQLKKYMEIEQVDIEESALSYIAGIADGSMRDALSILDQCISFYFGEQITLEKVLQVLGAVDTQVYYDMTQALIQQDTQQCIELIQEVQMQGRDLIQFVLGLIKHFRDLLVVRATKEAEGILNHSKEQIQKLKEQS... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 548
Seq... |
A0A840QM20 | MRLKRPNISLQNRIIFLVCSVAALILLVTSYLSSTSIEDTTLSMVEEKTKSISRMVALNEDVIGALNGEVEQETLQKEIEKIRETTDVLFVVILNMDRERLTHPNPQEVGKKFVGDDEGPVFVKGNEYTSISEGTLGYSFRYFTPVYDDNDSQIGVVTVGVHLDKVENAVSSNQDHIIIGTILSSIIGISASIFLSTMIKGTLFEMEPWQISKVLEERSAMLKYAKEGVIAVDTNCMITFINNEGINYIKKIGHDHDNLNGKNIEEVIPNSQLSKVLQTGKSEVDKELTYNDTTIVTNRVPIYVGNKIVGAIATFRDKTE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 534
Sequence Mass (Da): 59963
Location Topology: Multi-pass membrane protein
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A0A2G9PL12 | MKKLLPDWIRVKPFEKTAYEQILTLLKQNSLNTVCIEADCPNRYECFSRKALTFMILGNVCTRSCGYCNVKSGRPERPDDTEPKRIAALVKRLALKYVVVTSVSRDDLADGGASQFVKTISAVRRRVPSSRIEVLIPDLAGNWDALKQIVDARPTVLGHNIEVVRELFPTLRPEGGYELSLDLLRRAKDLDASITTKSGLMIGLGEDKQQILKAMRYIRNTGCDILTIGQYLQPSKRHEPVRKYYTPEEFRFFKKQGAALGFRHTESGPLVRSSYMGERAISH | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical... |
A0A944D0P8 | MAKTSHSKHSVTAGEVGQRFDKVLSALIPQLSRTKVQALIVAGAALVNDKAVAKHYFLEEGDVIMYAVPEEKKLTKVVRPTDFMLNVLHEDDDVVVVEKPVGLLTHAAESTHEWTLADELLKKYPDIKGVGDSEERFGIVHRLDRDVSGVMVVARTQEAFENLKKQFQDRVIEKEYRAVVHGVPHRTHDDIRFVITRSTMDPSKMAARPENAEGKSAWTEYDVLRSHRNLSELRVLIHTGRTHQIRAHLLAISHPVVGDTLYTSKQYESNKSFDRLYLHAHRLTFTHLKTAQKVEFLSEIPTEFDQLMTS | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 310
Sequence Mass (Da): 35220
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A0A358C2N0 | MRTHAEWRGLPSHLFFAQLRALLDVDPHFGYCARTNSTRPMDIKRETVSDSEVKLTITVSPEEVQPFLVTAARHISEHMNIDGFRRGKAPYEAIVNNVGEMRVLEEAIEPMVRLHVAKALIDEKIESIGQPRVDIEKMVPGNELVFTATVSLMPEVKKIGDYKKLSVQAESTKAKEEDVAKAIKELTGMQTKEVRASKETGITMAEMVVIDLEMKKDGVPVEGGSTQGFKVYMAEDHYVPGMKEEMIGLKEGDQKSFTLTFPEAHYQKHLAGMPIEFAVTIHEIYTLDSPTVDDAFAVSLGLKDVADLKEKITENLEKEN... | Function: 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.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A7M5XH04 | MTKSRIIRFAVMLPKDKARKIRIPERIESLCQQEGIEVTTIDAFKLKEDKIEANFDIVLHKIFDYFNEPELTVEQMQDVIQNCKDFFEQNPKMIVLDDTEKYRKCTDRLYCTRIMRECSLFVDGIQVFVPKSLEIAAGLPSDQVRDMLSEAKINFPILVKPMYTSDRKMSLVFSLDDVNEKCSPSLVQEFYNHNDVMYKVFVMNNRYNVIQRPSIKNYEKDPHQKPIFLDSRDVSKMGRGFHPEIHKSDPSKQTWQSSFSNPDILNKSVLNSLCVKLRDASGLKMFGFDLLVVRETGHYAIVDLNPFPGFKGIPDDVFAD... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
EC: 2.7.1.134
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 1D-myo-inositol 1,3,4-trisphosphate = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1... |
A0A1E7GUV9 | MPLYPVNLNIANRLCVVIGGGSVAFRKVKTLLDCEGVVRIVSPYVEPGLKKFILEKQVEWFEREYAKGDLQGAFLAFAATSDPDVQLQVKEEAQKYQAILNSADDPVGSDFHVPAHFRRGKMLVTVSTGGGSPAMSKQIRERLELDFGLEYEAVVDFLAMVREAVVSSDVDSATRQKLFRNLLKVDILGLVRESNWFDLQMMLLQELPENIDAVALIKRFLDEHDKK | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 227
Sequence Mass (Da): 25501
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L0N867 | QPGVPPEEAGAAVAAESSTGTWXXXXXGGXTSLDRYKGRCYRIEPVTGEDNQYIAYVAYPLDLFEEGSVTNMLTSIVGNVFGFKALRALRLEDLRIPTAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNKGHYLNATAGTCEEMMKRAQCARELGAPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDYIKQDRSRGIFF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 337
Sequence Mass (Da): 37131
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A0A9D5ZZZ3 | MNISEISASSIDMLYFSYVETKEDIMALREAAKAVGLEVPVVSKVETVYAVKNISEICLHSDAICIARGDLGVEVPHAALPFVVRDITAAAKRAGKPVLLAGEVMYSLVTRAVPFRAELTDVVVAIESGIDGFILSDETAIGINPVTAINYITSIAKEVQDRKAALRLI | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 169
Sequence Mass (Da): 18119
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A0A972KP07 | MAMREIKIYGDPILREKTCLVREITPRTKELIKDMAETMYGSKGVGLAANQIGVDAQIMTVDVGRGLLVLVNPRVLSSFGEESAEEGCLSLPDIRVGVRRAAKVKVEGLNEEGKEVEIEAEGLLARAIQHEIDHLNGILITDRISLARRHLLSSHLKKLEGSSKSLPERR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A972RGB9 | MGYDRVIEEIKSRIDIVELISEYLNLKKTGENYKALCPFHSEKTPSFVVSPSKQIFHCFGCGAGGDVFSFLIKQENISFTEAVRLLAERAGVQLKGYSRDTEGQSRRQTLLEIHRLANEFFHRLLWEQREGYNYLTKRGIREETIREFSLGYAPGGGDVLYRYLTKRGFKEEDILASGVCKKGENSIIDTFRNRVVFPIYNMRGDVIAFGGRIMHESTMAPKYLNSPETILFKKSNELYGLYHARKEINKKGYIVFTEGYLDVIACHQAGIKNVVAPLGTALTEQQLRKIKPLCRKVLLLFDSDEAGVKATKKAFSMIYE... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 567
Domain: Contains an N-termi... |
A0A840QRM7 | MNKRIPLAIGVLLIVFTVIKTGWDEVMSTASQMSLTDGAVMLLFQLLTLFLSSFVWYLFIVNEHVHIKLYDVFRINLTGQFVESITPSVKVGGEGVKIYLLRKKTGLGYQDVSALTVANKLVSTLAFLLIISGTVIMSLIFLELPMIIYGVFACFVIILFTFYQLLKWAERYPVNNESSIIFGKKLPRRFPNVYQWIEKIIQFVTQFSAKTLHIMKYTQYRNLILSVSMFIWMAYPLKVYLVSVMLGFDMSISIILIATYMAYLVSMIPLSPGGLGSFEMTMAFILSVGGVTYGDALTIALMTRVFTFWIPLMISGVTVL... | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistan... |
A0A0S7XAM3 | MQTDRGNILRRIPSVEVVLESHPVKALVGEYPRSLVVSAVRRVLEQERRSILEQSLSDVSSLEEMASRVREILVARTAKSMRRLVNATGVVLHTNIGRAVLAESAVEAITQAARHYTNLEYDGEQGQRSTRQIHLEHLLCESTSAEAAHVVNNNAGAVLLGLNTLAEGREVIVSRGELVEIGGSFRLPEVMAKSGAVLVEVGTTNRTTIDDYERAVNRNTALLLKVHKSNFRMVGFVSEASLEELVSLGRKRSVPVMEDLGSGAIVDFSLYGLPGEPVVSDRIAAGADVVTFSGDKLLGGPQAGIIVGKKELVGRMRENP... | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosph... |
A0A7V1N0D6 | MGKIVFVTGGRRSGKSAYAQNLAESLKNKPMLYIATCPVIDEETKTRIENHKRDREGAGWDTKEETVDIAGVIREAKGYKTILVECLTLWINNIMFEAGKNGEQVTELTVSKLAQDALAECRKSDSTVIFVSNEVGLGIIPDNRLARNFSDIAGRVNQIIAGEADQAVMMASGLPITLK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A7L4QXS6 | MAYEAQYYPGATSVAENRRKHMSGNVEKLREVSDDDLTLVLGHRAPGSDYPSTHPPLAEMSEPECSIREMVEATPGAKAGDRVRYVQFVDSMYNAPSTPYFRSYAAAINYRGVDPGTLSGRQVVEARERDMEEIAKFQLETEMSCPALASLRGATVHGHSLRLPEDGIMFDMLDRCRLENGVVIMHKDQV | Pathway: One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.
EC: 2.8.4.1
Catalytic Activity: coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane
Sequence Length: 190
Sequence Mass (Da): 21185
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A0A521L6F8 | MTESLPPHDVVTQAVEYLRARLPARPAVGIILGSGLGSFAERPPILAAIPYADIPGFPVCSVEGHAGRLVLTEREGACVAILQGRAHRYEGVALATVTHPVAVLAALGVRTLIVTCAAGSLDEAEAGTLMLIEDHLNLMGDNPLMRTGPAKGAPAGRSGIRVSGFVEMAQAYDPALLEIAEQVAGASGLSIRRGVLAAVAGPTYETAAEAEMLRRLGAQAVSMSVVPEVIVARALKLRVLGLALITNRSGAALDGRVGHPQVVAVAESRADSVAALLDGLLRRLASA | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
EC: 2.4.2.1
Sequence Length... |
A0A8J3BB76 | MIPARPLPPRGVTLVELLAALGLLSVVVSLLYTIYHQIQDLGQTASATEDLLAEARLIQTEIVNAMRARQVDKSQGTPENGGNGTPAHEFTLFYQGGGSVAFTWDKQARTLAVDRNGDGFVLSERVAGFSYTPILDNDTAGNSAEVEGYTFTLRLDGDGDGQGEENNKRDLVTIFSVYFPRW | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 182
Sequence Mass (Da): 19795
Location Topology: Single-pass membrane protein
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A0A172YHD1 | MAGAPILVFDSGLGGLSVVAHLRAALPERALAYLCDNAALPYGTKADEWLVERIVSVCRAGVAASEANTLVVACNTASTLALEQLRASIALPIVGTVPAIKPAAEASRSRVIGLLATSATVRRPYTDALIERFAGSCRVIRVAADPLVLEAERLLAGAAPDAEVIAAALAPLFDTPGLDTVVMGCTHFPLLRAWCETLAPRPIQWIDSGAAIARRTAQVAPPGGRRGDLDVSFATAPEHAGLARALARFDFAAPSPITL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 259
Sequence Mass (Da): 26874
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A0A9D5W114 | SKEMTQREALYPQYKAQRKVPPKELTCQIDPIIEIVKALGIPTFAVPGYEADDIIAKLAIDASNNGADVFIVTSDKDLLQLVSTKIKIFDPVKNIVQDREYVINRFSLPPERVIEYLALTGDSADNIPGVKGIGEKTAKTLLSKGTSLDDLMNNPQNIDSPRFRTMITDNIENIKLSYQLLTLKTDMELNLKIPHFNDITPDLTKVKELFMGFELNSLLKNLPKSSAPSVGATLVTAQEDATIEVIELTKADEFNFGDDGISEIFININNIVFAFSLEPNRGFYFTKHELIEPFLNLLKSAKKISGHDFKSMVNINSVGA... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 809
Sequence Mass (Da): 90423
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A0A9D5W609 | MNNTTLLTAFVIDLMIGDPGWIPHPVRAIGVLIERSEKILRNFTKTKRGEFFCGAVMAIFVVLITYVVFYLMSYWINTVFGNYFIASNRIALSDIIIGVIGSFSLAYTGLRDSVVIILKRLMAGDTEGARNALSSIVGRDTKRLDSDGIVRAAIESLSENLSDGVIAPMFYLAIGGLPLAFAYKAINTIDSMVGYKNDRYLYFGRFGAKLDDVANYIPARLTALFIIAGTIALKLPLMIQYSLICIVKRAGGTKSRMVKNRRLSIRNSMKVLLRDGGKHPSPNAGRPEAAMAGALSIALGGASYYGGKVVVKPVIGSADE... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 357
Sequence Mass (Da): 38710
Location Topology: Multi-pass membrane protein
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A0A497IU09 | MPALPTAFEVAVFNALTLVAAFALDLVLGDPPESVQRFYPVVWISRLAYFLDVRVRRGNIRREKLFGVLCAVFVIFVFATPCLLIGYLLCLPPPLRYAYVVVGVLVFKMTFTVKGLERFALATLSPNMEKRRVAVAKIVSRDVSQLDVPHLTSATIESTAENLTDSVISPLFYFTAFSAFGSLFHNAALAIFGAMLYRVVNTLDAVFGYKDERYKHFGWFSAKFDDVLNAPLERLAAALLLVSARFLKLQPAAAAGGDGAVKPPIRAAAQALRVRLEKAGHYVVGERFEFPNDEHVRKCIKLVKVSSLVFMAVCVLFLLV... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 326
Sequence Mass (Da): 36150
Location Topology: Multi-pass membrane protein
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A0A1J1GVP4 | MDVLKYCLVLLLLEHYFKTSLGHIISKKLKFYIKNYKSNNIRKNRNVIIHLTRESNKEIKIVKYPNPVLRKKCEDVINFDDNLKNLIRIMFNIMYENKGIGLSAPQVNISKKIIVWNALYEKRKSENERVFINPSIVEQSLIKTKLVEGCLSFPNVEGKIERPNIVSVSYFDLEGNKHLKILKGIHSRIFQHEYDHLNGILFIDRMTQNEKKKIKAKLNQLTQEYKKNYSEEPAI | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 235
Sequence Mass (Da): 27722
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A0A3S8V1D1 | MFFNFNILIFVSLMVLSLMIGMNSISLIYFWLSIEINMMSFIPMILFFNNYYNYSSMKYFLIQSFSSSLMLFFMLNLYYLSMMKFILMMLILVLFMKLGYFPFHFWYLNLLKDLDWMSGLILMSMQKILPFYMLNYIFKMINYLNMNFTNQFFLFNNYFIMLILMCLSIMSLIYSNNSIKLFMGLSSINHMSWMILLILIDLNLWMYYYLIYTQILMNLIFIFKKYNLNNFNCLYMIKNYNNKFFIFILILLLMMMPPLIGFFLKMFSINLFLKYNFMFMLYLLLNLSIFMCYYYLNLLMFSLLFNNMNLINNMNLIIQY... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A3M1S996 | MKGIPPVPEGECSLIEEIKGRFSSRDSGVLVGIGDDASMLSTPGSPLLVTTDAMVEGVHFDLSIMTPFQVGYKLAVSNISDIHAMGGRPAWAQLALSVDSGRAEGFVDGFFDGLKDALDRYGVVLTGGDLTGSRGVISVSLSLLGLSGERVFKRNGANPGDWIYLTGPLGEPSIGFYLLKRLGLPVAFERGERLELEGETVWMEHLIRRFVLPELPDAPVQYGDRITSMIDISDGLSLDLWRICHQSGVGATLIEDDLPITPQMKMAAEQTGIELLGHILGGGEDYQLLFTSPEDIPDFYRIGRITSDGFLILRKTGREE... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A1M6N225 | MIDRKLIKNIDSGLIMIVLILFMISLVIISSATHVMQEGLTRQVKVQTVAFCLGIIAVAIIFFFDYNTFGEFYTWIYGLSILMLLLVYVPGVGKIQAGARSWINLGPVDFQPSELVKILFVLSFAKFLENKQQNINTFKGLISVAAFAAPPLVLILKEPDLGTAMVLSIIIIGMLFVAELDYKIIGMGLLAGIISMPLAYKFMAPHQRIRIDAFLNPSDPTLPGNYHVIQSKIAIGSGQLFGKGLYQGTQNNFNFLPVQETDFIYAVLGEEFGFVGGAFVLIMYFMFLYRMIRIAKMAKDTYGALIVTGITSMFAFQIFE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-... |
A0A2Z6S539 | MLSQRKSQLSNSIPNEETDNNQTTQTLIPPPPRSPVLHSSPLSSTLLGSLKAILFASWTNILLIFIPFGFIATRLNWSNISIFILNFLAIIPLSNLFEFAVENIGLRVGALTGSFLNFTFGNAVELIVSVIVLKQGQIRVVQASILGSIVSNLLLVLGMCFVAGGIYNKTQSFNMTTAQTSSSLITLACISLIVPAALVSSTNSLNDIKYEKGLLNLSHGMAIILLIIYVLFIFFYLKTHSCLYLSWDEYEKDEHPQLTLIASLLLLAVVAVFVAFSAEYLAGSIDGIVKPIGLTETFIGLILIPNISKITEIVSIVRTS... | Function: Has a role in promoting intracellular calcium ion sequestration via the exchange of calcium ions for hydrogen ions across the vacuolar membrane. Involved also in manganese ion homeostasis via its uptake into the vacuole.
Subcellular Location: Membrane
Sequence Length: 351
Sequence Mass (Da): 38301
Location To... |
A0A7X8EW18 | MMKIQDIIESIQPLDKVAMNAARSYNDNLIKPLGSLGRLEDLAVQLAGITGRVQNDMGKKAILVFCADNGVYAEGVSTAPQEVTAVQATNMLYGKTGVSVLAKQGNIDLKVVDVGIHTRKKLHPQMIEEKIALQTGNILHEPAMTKQQLEAAIEVGFRMVKSMKEEGYSILGTGEMGISNTTTATSVIIALTGISPKEAAGKGAGLTRELLLHKIDILEKIQEKHYHASISPLEVVRRMGGFDIAAMMGAFMGGAYYHIPIVIDGVVSIAAALACFCCNPLIKDYMLPSHRSAEPAYTIAAQTMKINPYFELDMRLGEGS... | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole +... |
A0A532UHT1 | MIALLTGKLRRKEPNEVIIEVNGVGYRVVIPLSTYYRLKSDEEPVTLIIYTYVREDTIALYGFLTDQERLIFEKLISISGLGPKSAIIILSGLPTEELISAVRKEDPSPLSSIPGIGPKTANRVILELRDKLKGVVSLLEEKAMAPYPTAPLTPMKRDLLSALMNLGYKKYEAERAIKETLISLGEESSFENAIREALKILAKH | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A3M5D5Y7 | MLVGAGIMSATLAVLLKELDPNLKMEVVELQESGAIESSNPWNNAGTGHAGLCELNYTPQSADGSIDIKKAVGINTMFEVSKQFWSHLVAKGTFGSPKTFINPVPHLSFVRGSEGIAYLKKRFESLTKHHAFETMVYSEDKATLAEWMPLMMPGRPADEAXXAATRVEGGTDVNFGALTNQLLQHLAQQPGAQIRYNQKVTHLRRADNGWXXXXXAGHRQGHPQRRRPRDPGTLRLPRRRRRRPAAPATFRHPGRQGLRWFPGERPVAALRQPGNRQAAPGQGLQPGRGRLAADVRAAPGHPCGGRQEIPAVRPLCRFLH... | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Length: 563
Sequence Mass (Da): 61280
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A0A660ZH26 | MRRIFLISALIFLASCAPGGHQWVEYGIASWYGPGFHGRRTASGEVFDMYKLTAAHNHLPFGTIVEVTNLENGKKVTVRINDRGPHKRGRIIDLSYRAAQKIGLIGPGLARVRVRVLKWGKRP | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 123
Sequence Mass (Da): 13764
Location Topology: Lipid-anchor
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A0A7C5VZE6 | MNLLKRIIIISLIVAICIVTDQITKNIAKARLSSGQRYSYLFDTFRLQYSENTGAFLSMGESLPDSIGFWVLTIIPAIFLVFLTVYLLISKKVTLPYLIAYSFVLGGGSSNIFDRLIYRRRVIDFMNMGIGPVFRTGIFNFADLFIMIGFFILLITILLEGKTKPRASKDTSK | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A2N1V4K3 | MSTDNKYMQLALEHAELGRGNVSPNPLVGCVIVKDDKVIATGYHKEFGGPHAEVDAISKVDGDLKGCTVYVTLEPCTHHGKTPPCADLLIEKKPDRVVIAMEDPNPIVKGNGISALQGNGIETSVGILVEEAMVLNRVFITNMIEKRPFVTAKFATTLDGFIAQRDHESKWISCEDSRIDVHKFRSEIDAIMVGSGTVRQDNPMLDVRLAKGRNPKRVVLASHLQLPLSSHLLKDENANENTIIYCTNEAQNIKLVDQLRSEGLNVKSISKNSKGKVDVSLALRDLLKEYHIGHIMLEGGAKLFSEFYELDFIDEIITYQ... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A7C1H6S8 | MTKRLFLAINLPPEIKEEIFNLALKLKKLNKNKPIKWVEKDNFHLTLHFLGSVPEEKISTINQALAPIVANFPTLNFALSDSINAFPDSNNPKVIFWEIKELNDGQTIKLQKQIGEGLARLGFAIDKRPFRLHLTFGRVKFKTAIQIPNLQFPVSNFQISSVDLMSSELTSAGPIYSIVKAYNFKNN | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 187
Sequence Mass (Da): 21224
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A0A520JUN5 | MQVITSTEMAALDANCEYYGLARIQLMENAGASLANIIKQKFPQDTPVTIFAGKGSNGGDAFVAARHLAGYNVQVFLLGRGDEIKTAGARWNFNILKKAGTPIIEITDSTQIPEPDDDCVIIDAIFGTGIKGRLRPLESTAIDRINNCASEVVSVDVPSGLDPDTGDFEKTVRSNLTITFHKPKPALLHQGLKKYIGELVTAPIGIPLFFERLVGKGDIGRLVTRKPESHKGDSGSMLIIGGGPYSGAPALCAMAALRCGVDLVHIAAPEAVSNIIASFSPNLITTALTGNHLTENDIPLLKKIIPTVDVVVIGMGLGKH... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A521SRN7 | MTVEIIGAIALALLFDLLLGDPSWMPHPVRGVGRLIEAGEQILRRRFPGHEKLAGVFLAASVVLGVYALGRGLSSASEQIDPALGVVVQALLIYFSLAPRDLAVHALRVRRELKAGNLEGAKAKVSMMVGRDVAPLDEKGVIRATVESVAENTVDGVTAPLFFAFLGGGAVAIAYRAANTLDSMVGYRHAPYTDIGWASARFDDLLNLLPARLTAAVMPLAGIFLGGSIPGGYRALLRDGRKHDSPNSGLPEAAMAGLLGVRLGGPHWYRERHYPSPWIGFDRRPIAPGDIVKAIGVMAITTLILFLLFSWMRWTVAG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 318
Sequence Mass (Da): 34048
Location Topology: Multi-pass membrane protein
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A0A660ZJ09 | MKGRALLSPLAVLYRIGLELWNFSWNFRKAVKIDVPVISVGNLTAGGSGKTPLTIYLAERFLERQTKPAVLIRGYRRKGKGDLFLLTDTKVVPPVENTGDEAQLIYRRLSGEVPVGIGRRRERTARFLLEKENPDLFILDDGFQYRKLHQDVKIVIINVGSLKEPVRLLPAGDWREPLSALKRADILIYNFKFEAEEAGVPDGIPLNKPCFKMSYRATGVVAPELKMLGVEYIKGKKAFAFAGIADPRGFLKALEATGMKVVGSMFFPDHHWYSDRDLRKITEGSKKSGAEITITTEKDLIKLGERGSEILALRVEPSIE... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A972KP28 | MTLKVKDRLVLALDVDDKETALGLVEQLEEYVGVFKVGVQLFSGEGPEIIRCLRGKGKKVFYDAKYHDIPTTVAKAGKMAVRLGAYIYNVHTLGGYEMMRMTVEETEKEAAALEVEKPLVLGVTVLTHLDQGMLKEVGIEKSLKKEVVSLAKLAQRAGLEGVVSSPREIRLIREACGDDFLILTPGIRPCWAEGNEQRRSMTPGEALEAGADFIVIGRPILQADDPAGAAQRVLREMEEAVAKGK | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 245
Sequence Mass (... |
D3E0M5 | MKNILISNDDGVMGPGILASKQALEGLANVVVVAPQENNSAVGRKVNIMKHMYLENYELADGSMAYGLSGTPADSVNVGINYVCDEVPDLVVTGINPGINISRLQITTSGTVCAAIEAVGLGIPAIACSLFLDDDCFKQDDEGNWYVDTDYSFAQKILAKLVKKVLDEGMPDGVDLFNLNIPSKPLSDKIKITRLADSMLKFNILERVDDDGNDTVMNVPELIEDYEEGTDGYCLLVERRPSLTPLNVHFGAEISNLEDWEF | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 262
Sequence Mass (Da): 28523
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A0A662RYQ6 | MRFEEFKGWLSLASPPKFSTTLIPFVLGSVLAWSEGHSPDFLSFFISLLAVILLTAFCFVLNASSVYEDLRNSRILPAHDSTHHRHHRTHLSGFHTTATTGRFEEFLSGRISVEKAIFGAYLCAALAIPLGFILQFILNTGELTLPIGLIGIFIAYSYSRGLKLSYIGLGELALAIGVGFITILSGFYIQAHSISITPLIA | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 22022
Location Topology: Multi-pass membrane protein
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A0A934AXY5 | MSASHSECVPAGTYSIRSDQKGSLKAYLGTCVGVVLLDRISHVGGLMHLLLPEPPSPDNPWQPESYASTGLPIFIEALAAAGAQIDRLEAFVAGGALTGRLSETDLFLDIGGRTTDVVMDVLRRYGIAVKRSETGGLFNMVIEVAFAVGDCSIEPMVAAPAASDSNAKKPSREEIIQAAARIRAVPQVALKIIRMISDDYHSMIDIAAEVRQDQVISARVLSLANSAMIGWNDTIDSVDEALMVLGEKAILRLVVSASMELFFPESERGYSQCKGRLFHHAIGVGLVAEQLARVTGKSDPGVAYTAGLLHDIGKVVLDHF... | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 452
Sequence Mass (Da): 48902
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A0A7C4MPM6 | FALMGSTYCRFMLGREKPRVALVSTGEEDSKGNELTKEAFKLLKETELNFMGNVDGKDIFTGEADVIVCDGFTGNVILKTSEGLADALIRMLKREVAALTTGRIGYLLLKPALRNFKKKTDYDEYGGAPLLGIQGTCIISHGRSTAKAVKNAIRVAADFARKKVHEIISSAIKEDISRHERLSLGKK | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-... |
A0A8B5VUN2 | MTMKDKNIKKYKRIANKIIKLIPTYKAMSDSDLQNQTILLKERLANGEKAEKLLPQAYAIVAEADRRVLGLEPYYVQILGGIALFYGNVAEMKTGEGKTLTATMPMYLRGLMGKGNFLITSNSYLAWRDAEEVGKVYRWLGLTISVGVPKDASEEEVDKEAVYGSDIIYTTHSALGFDYLFDNLATTLEEQYVNTFNYVLIDEIDAILLDMAQTPLIISGAPKVQSNLFETSDWFVKSLSEGEDYLKSEDKRNVWFKEEGIKKAEKYFGIHGILTEEWRDLYRHLVLALRANQLLEENRDYVVEEGEILLLDEANGRKLI... | Function: 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 c... |
A1HTH9 | MALRVYNTLTKQKEEFVPREPGKVKMYVCGVTPYNHPHIGNARPFITWDVIRRYLEHRGFAVFHVQNFTDIDDKIINTANQEGVTWDTIANRYIAAYFEVMDKLNVRRAHVYPRVSDHIGDIIAIVQRLIDKGYAYTVGGDVYYSVEKFAPYGQLSGRSLEDMKAGARIDVDERKRHPMDFALWKSAKPGEPAWDSPWGPGRPGWHIECSAMALKYLGNGFDFHGGGSDLIFPHHENEIAQSEAYTGEAPFVRYWLHNGFITVNEEKMSKSLGNFFLVKDILAHYPPEVLRFFILSTHYRSPLDFSDERLAEAGRSLERL... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 370
Sequence Mass (Da): 42063
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A0A849QUC7 | MADKPEKFIDENGIRSDGRRANEIRDVKIEVGVLSRADGSCYLEFGKNKVMAAVYGPREVHPRHQQKSNRAIVRYKYNMASFSVEDRKRPGPDRRSIEVSKVSREALEDQIFTEYFPKSAIDIFVEVLQADAGTRTAALNAASVALADAGIPMRSLVSACAVGKVDDTLVLDLNKDEDNYGQADMPIAMTPDGKITLLQMDGHLTQEEFKQGLEMAQEGCRQVYEMQRKALMDHYSKKAEITTTAEDIKTDAPKEPENVTPVEVTEEIEEVKETGDTEDTVKAGDVEELEDSGEEVPDTGEYAEKTDGQMDEGEEESSNE | Function: Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteropolymeric RNA-tails.
EC: 3.1.13.-
Subcellular Location: Cytoplasm
Sequence Length: 320
Sequence Mass (Da): 35567
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A0A931YMU4 | MLSVVAHRKIWYTISGTLVIAGVLAIAFWKLNFGIDFVGGSLMEFQFTGAPPAPAVLTQEIAALGAHRIQLQSAGDRAVIVRTETLTPELHATIVRALQDRASELRFETIGPSIGQELARKTAIGVVLALLLILCYVAWMFRKAGVQVSSWAYGFVALVVMVHDVIIPTGVFAVLGRFVGVEIGAPFIAAVLTILGYSISDTIIVLDRIRENVGNARGGDFATVVERSVHQSFARSMYTTITTILALLAVIMFGSAGVRYFALALAIGIGVGAYSSIFIAAPLLVTWQQRGSRPNVR | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 297
Sequence Mass (Da): 31901
Location... |
A0A3M1GIK4 | MVKTVLLIGGARSGKTKLAIEMAENSGLRPWCYLATAVAKDQEMAERIK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A1J5BCP0 | MSIIVNDNLFALAPLKKEGFQIEGKSKANIDKNNLLKIAILNLMPNKQTTELQLLRVLNNEQYAIDIEFVYVSSHQSKTTSEEYLKKSYHSFDEIKNSHWDGMIVTGAPVELLDFKEVNYWNELKQIMDWALSNVTSTFFICWGAQAALFHYYNIPKYKLSEKMFGVFNHQINHEIAILKEIHNPYLAPHSRHTSIVRDDIEKVSDLKIISTSEKAGIYILANEAKKQFFVTGHSEYDVNTLKDEYFRDLQKGLPILKPQNYFPNNDENKAPINTWKTNAHLLYGNWLNYYVNSKK | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
EC: 2.3.1.31
S... |
A0A4Y8I7X4 | MSETLTLFEIMEGIEYTLKSGQDTPVSGIAYDSRTLQEGDVYFALTGGTFDGAEFIDDAIEKGCSAVVTEKAVDRSFAPLLITPDSRSALAFASSAFHGHPSRELKLIGITGTNGKTSAAFILRYLLQSGGHRTAIMGTIGNDLGSGLTDSKLTTPEAPEINKFLRDALKAGSTHAVMEVSSHSLNMKRTAGLAFDVALFTNLTHDHLDFHGDFDSYRESKAMLFSDLSSSAKAILNKDDPAWEKMVSSSPAGLITYSLSDSTADYHALSYSYSPDGLRLNLITPDAETEIKSSLIGEFNIYNLMAAYAAAETVGAEPGS... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A0Q5DYR8 | MHALPHPFIATPIAWFDIDAAPVATTGSQRCFHIASGALRVGARTDQMQVLLGSCVGIALLWKKRGRCGLAHCLLPGSSAPPANLGARYVSQAVPSLLRLMGACAADYADIEVVVAGGANMLEGCSSRLRIGQQNIDAARRQLDLHGLRLRFADVGGNCGRTLTVDCATQEVKVCAIAPTAPARARSRVALHA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 193
Sequence Mass (Da): 20261
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A0A3D1CRF0 | MIKKLFNSASPTIASAAIIVGVFSIASRVAGFVRDRILLHLFYGHDQITDAYYQALRIPDIILQLFVIGALSASFITIFSRYYFAHNEEKAWKYTNAMLVTLVIGFLGLAILGEIFAPLLAIPLGINFPPETRALMVKMMRIMFIGQAFFSISMVFGSVLQGAKRFFLYSLAPIVNNLGIIFGAIFFVPIFGPLGLAYGTVFGALLHAAIQLVGVFGLGYRFAFVKFWKESDVWHSLKQMGPRVMGLAINQVNFLVMDILASSLVAGSATLLNISYALNYFPIGVFAVSYAIAAYPTFCDFANKNDKESFRRSFSDTVRQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 536
Sequence Mass (Da): 58406
Location Topol... |
T0XWS2 | MPSPLKIGLIGSRGQLGQELVRRFSEPDLSRKVSLLCLDRPAFDITSPSSLGEIPGAGFDIILNTSAYNAVDRGETEVRECFELNAFAPLLLARACREAGTALLHVSTDYVMSGGIHEEEQIPYPEEAPTRPLSVYGLSKATGERLVTGAWERSWIVRTCGLYGGSGSGQKGGNFVTTMVRLAREGKPLRVVSDQRVGPTAARDLARGIARLVTAPLPFGLWHLNHARNVSWYEFARRIFELSGLAPDLSPVPLALYRPVAPRSPFSVLSNEKAHRTGIVLPSWEIALADYLERSGLLAGS | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 301
Sequence Mass (Da): 32720
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A0A9D6LI95 | MPVYFIQSRALQDNQLTLNDDLAHHLRDVLRCRPGEIVNLVDEKQVRYRAALSRVTKMEVIAKILQKDDPQIRPAVSITLAQAILKGDKMDWVIQKATELGVNALLPVVTERTIARPRVEREAHQIDRWQKIAKEASQQCGRSDIPMIWPAVSLDALLKNPPDTSLKLVPWEQEQEPSLKAVLTDSSFYDPTGQWNNSMIVLIGPEGGLTPPEVEKARKTGWISVSLGPRILRAETAALAVLAILQYELETRR | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A428P2C0 | MDGIPPEQRRRGSSGVYNAPNSYTELGEILAQQPIDEDAVSDTEAPALDPVQRRDSGVYSVPRSYSNLDEVSPVPPIEEPPFDSVQDVQGRQRRRSSFARHEGPILEPEPIPEEAKERRVSRLATELYTHSYLIFFAILGTLARLGLTALTRYPGTPVIFNTIWANFTGSAVMGFLAEDRKLFRNEWGNATYDEAINQAKQKRKDEEDGSSSSQQKDVDLAAAKKAHLAMKKTIPLYIGLATGFCGSFTTFSSFIKDTFLALSNEMVTPGWSESPTSRNGGYSFMAMLAVIIATVSLSLSGLFLGAHIAIGLEHVTPTIP... | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 883
Sequence Mass (Da): 97716
Location Topology: Multi-pass membrane protein
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A0A3N2NQH1 | MLQYITSTSSPVPVTEQVRQVLEGGCRWIQVRMKDASDEEIAGVIEEIKPMCLDKEAFLILNDRVELAKTLDVGGVHLGKTDMLPSQARLILGPAAVIGVTANTVEDVEAVKALDIDYIGIGPYRFTETKKNLAPTLGIEGIGSICGNMHEREINIATVAVGGILPEDVAPLMESGVNGIAVSGAIAFAPDIKAATEEFLRLLEPYEKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A6P3HB52 | MSGYEKPSRGWGFCALSPVLLSLLMAAPLGLLGEETRQVSLKVISNRLDFSQNLLHIRAVGTNSTLHYVWSSLGPPAVLLVATNTPNSTLSVNWSLLLSSDPDGGLMVLPEESIQFSSALVFTRLFEFDSTNMSDAASRPLGKSYPPYSLANFSWNNITDSLDPATLSATFRGHPIRDPTGAFTNGSLAFRVQAFSTSGRPAQPPRLLHSADTCQLEVALVGASPRGNRSLFGLEVATLGQGPGCPSMQEQHSIDDEYAPAVFQVHAPGCGHPSSGCLVPTSPRHHGSGPRCSSTHAAGRRPASAAGPQAGL | Function: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization.
Subcellular Location: Lysosome membrane
Sequence Length: 312
Sequence Mass (Da): 32946
Location Topology: Single-pass type I membrane protein
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A0A3M2AMP4 | MWQDGVLNVNKPAGWTSHDVVAKLRKALGIPKIGHAGTLDPMATGVLPILVGKATRLSEFLLDWDKEYEAVLRLGQTTDTQDATGTVIRDEVVHPLSVQSIVNVVAQFQGRISQLPPMYSAVKKNGVPLYRAARAGQTVERTPRWVMIHQLDVQSIQGTDVALRIRCSKGTYIRTLCADIGERLGVGGHLYQLTRVRVGPLEVKHALSLEQACLWNTQEGDQWMQAFLPMAQVLREFPAVVVPVERMRHVLNGRSLSLNALPHGAEVEENQVIQVVNEAGQLVGLGRGIRKNGQAREDGLELKMIKVFMSPSGKTVSGTV... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 327
Sequence Mass (Da): 35908
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A0A1F9X0P1 | MGNAIKEVFSGQGFEMKLDEPLAKHTTFKIGGPAPVYIEPKTHEELQNIVSACKANSFPFFIMGLGSNLLIDDKGFEGVVLHLRGIFIQTQALNQGNKVVIKAGAGVTLPLLIKKCADNFASGTECLAGIPGTVGGALIMNTGTKYGSISDKLSSVTVLKPDGGIIDLRKNELSFSYRHSSLAQYIVLSAEFLLDFAPNETIVKKITDYMLNRAETQPLSVPSAGSVFKNPPEKKAWQLIDACGLRGLKIGGAQISEKHANFIINTGNAKSSDVKELIETIQKKVKENTGIMLEPEIKIL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 32348
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A0A5E4QIM8 | MSKIYRTIIAVADRFVPGPIRPLWNHPAVETISTSQTLSLAVTGMIWSRYSLVIVPKNYSLFAVNIVVVFINCYQLARLYSYQKAV | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 86
Sequence Mass (Da): 9765
Location Topology: Multi-pass membrane protein
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A0A7C6FTK9 | MENENAKERFEIHVSARHLHLTQETVDILFGKGHVIEPVEPTDSKQFLSTTRATVVGPKGRFENVAVMGPCRRINQFEISATDARTLGVPAVIRMSEDIEGTPGIKIIGTVGEVTIDKGVIVAKRHIHMSPSMAEKYDFRDGDNVLLAIESDARTLIFGDTIVRVGAPPEEGAMAHIDTDEGNAAGIGRVAYGYIAGKTEDIRKL | Pathway: Polyol metabolism; 1,2-propanediol degradation.
EC: 2.3.1.222
Catalytic Activity: phosphate + propanoyl-CoA = CoA + propanoyl phosphate
Sequence Length: 205
Sequence Mass (Da): 22319
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A0A931Q587 | MKIVIAGGGTGGHLYPGIALAKAFQNYFKGVQILFIGTEKGIESRVLPGEGFTLKTIEVEGWIGKNRMTLLKTLIRFPKSLGQSYRLLKAFRPNLVIGVGGYASGPVLLVAAFLKIKRIILEQNVIPGLTNKILGHWVHQVFGSFEGSKAYFPRKKFFFSGNPVRKEIINIRAGKESGELTLLVFGGSQGAHAINQAVVDALDILKKDPRLSIQWIHQTGPKDFQWVKEQYEAKKISARVEPFIFNMAQAYETSDLVICRAGATTLAELTACGKPAILIPFPFAAHRHQEKNAYFFKKMGAAEVIDQADLDGRLLAKKIE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: 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).
Catalytic Activity: di-t... |
A0A9D5ZTP3 | MIELQKWFFVLLANFIVLIILLRIILFKPLLALFAQRRNIVEEAMAAVRRYNEERTRNQSLIENEVINTNEKINTIIDTLKNEGVTLQKEYIQKAQEEALSMIEKAGKEISLEAEKARQSLKSDIVTYASEILTKVL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A4Y8I8N5 | MMIRTFIAIELPVEVKRVVRQIQDQLGGSIEGIKWVKQENIHLSVKFLGNVEENGINDIADAVKNAVKESSVMNLKTGHLGAFPNEKRPRILWLGVEGDVREFISMSKNCELELAKLGYEIDDRENKPHITIGRIRSTKKQKSVINILKDIHIESILFKVDALKLMRSELNRNGAVYTNLQSVKLDK | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 187
Sequence Mass (Da): 21259
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A0A9D6Q204 | MAKGIFITGTDTGVGKTIVAGGLACALMREGLDIGVMKPIQTGCVVKKNGNLIAPDTEFLIRMSGVKDKINLVTPYCFKEPLAPSAAAEAEGNEIDIEKIISAYNLLTEMHDSIIVEGAGGILVPIWKDFLFIDIIKRLSIPIIIVARMGLGTINHTLMTVRCARSAGIEIIGIIFNHTNNIKDGIAEKTNPNIIKRLCNIPILGIIPFIDKLKTEEIAADDLCAISSENVDIKYIRSFLSF | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A485FC90 | MGTEEIKGNQQVKLAASLLQKAQGLNFSGYIEGDGLYRGEADVVVCDGFVGNILLKASEGLAAMVSARIEQRFRDGLAAKLVGALALPLLRRLRGDIAPARYNGASFLGLQGIVVKSHGSAAEEGFQSALRRAALEVRENLPQRLHGRLEHLLL | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-... |
A0A3M1QX63 | MRGEKSGGRPRCARTRGSLCCPCRGAAGGGRAAPGAPGGETVETETHRDRAELASLTAEAWREQLASLPPEEARRMLEPIEPDRLAEVVRRLDEETAGRVIGLLPPDRAAAVLSHLPDETAAAALARPTLQRAVEVVQELDPDDAADIVAEMEDRQRDALLEASGEAGEVIEELLYYPEDTAGGLMTPEVLAVRRQWTVAEAIDAIRRRASELEQIYYTYVVDRDDVLIGVVTMRDLILAPPSARIEEITNPEVVSVSVDTDQETVAEIISRLNLLALPVVDHQGKLVGIVTVDDVIDVIQEEASEDFQRLVGAGADERV... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 499
Sequence Mass (Da): 52868
Location Topology: Multi-pass membrane protein
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A0A934AVY4 | MKKSLMQKMKGYQESFAGKLFTSFMLITIVLSLTFFVIDFWQESRVMMQNVENKGRLISTILAYHVKAGVFAGNRDMLKTAIEGVIRSKDVTSIRILDLQDRLLFEHGKGEITAGDFGRLPGSKEVMEMRGRNDDLLVLRSRKKILFTTPVFIERPSYAEEFLYLGIDEASQQELIGYVQVVIDRSYHEKKIRKIIMTDIAISLFFLLIGGSLIYWHIRKRTKPLVSLMNAVRSFGAGHALEKVPVQSRDEVGKLSHAFNEMAESLLQKEAERQRLETQFRQAQKMEAVGTMAGGIAHDFKNILTAISGFSSLAKMSLEK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 657
Sequence Mass (Da): 73310
Location Topology: Multi-pass membrane protein
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A0A1V5CGJ0 | MNQERFLNRTLKGIAVSSGICIGKVYLLERGKIHVTKHSIKEEQVAKEIAKFKAAIKSAVDELNNIKQSIPDDEIRKHAFIIDAHLLILQDRYFYDDIIDTIRRQRINAEWALDLVVSKFLSSFEKVEDPYLRERGQDLNHILQRLLRIMVKGKVSGIDDVKALKGKAVIVAHDLSPADTIQLNLSKVSGFVTDVGGRTSHTSIVARALEIPAVVGLGSITGLVKNNDTIVIDGEEGVVIINPSKEMQKEYLTRQAHLTAQRKEFLRIAKLKSETKDGFKIKVGANIELLVEMDIVERYGAEGIGLYRTEYIYLSRKTLP... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A0S7XFX4 | MGCELSLLVLGIETSCDDTAAAVVADAKKVLSSVVSSQAIHQLYGGVVPEIASRQHIRLIVPAVRTALEGARVELHEIDAIAATMGPGLIGSLLVGLCFGKAISFATGKPFIGINHIEAHLFAVLAESDDLRPPFVGLCVSGGHTELIYVTGFADYELLGSTVDDAAGEAVDKVAKMLGLGFPGGPEIEALANRGNSERISFPKARLKRRGYDMSFSGLKTAVKYFIEKHPRPLSEELKADVAACFQKALIEALVEKLVQACRSRGVKQAVLAGGVACNTALRDAARSACATVGVKLLTPSPALCTDNAAMVAIAGALRL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 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, togeth... |
A0A6P3JA22 | MGADNQTWVREFILLGLSSDWDAQVALFILFLVMYLVTVLGNVLIVLLIRLDSRLHTPMYFFLTNLSLVDVSYATSIVPQMLVHFLAEHKGIPYVSCAAQLFFSLGLGGIEFVLLAVMAYDRYVAVCDPLRYSVIMHGGLCARLAITSWVSGSVNSLVQTTITFQLPVCTNKYIDHISCEILAVVRLACVDTSSNKISIMVSSIVLLMTPFCLVLLSYIRILSTILKIQSTEGRKKAFHTCASHLSVNLL | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 250
Sequence Mass (Da): 27717
Location Topology: Multi-pass membrane protein
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A0A522UK57 | MSLSGELPLHVGVIMDGNGRWAQLRGLPRIEGHRVGAERAKEVIETSAGLGIKCLTLYTFSTENWQRPVSEVSMLMKLLELYLRKEMADLMKKGIVYRAIGEIWRLPENIQALIRDTEAKTASNSGMTLVTALSYSGRNEIVRAVRKLMTTAGRPEDLTEESFNDCLDTAGIPPPDLIIRTSGERRLSNFLLWQSAYAELYFSDTLWPDFDKEEFVRALRDFQGRERRFGAIPVRSDAS | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 239
Sequence Mass (Da): 27029
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A0A3S0ZGG2 | MVFTKRKTILMLLIPLTICMFVMIKLQTVSLVPSWPNTIPVVRSLGSQFSLERSPSRFSPKNPEDIMPSKKAHISVSGAPSSLKLTQKKQPQNLSKGSAKDHPKLTTVTTKSSQNSLANKPSCSPLQNVTKPYFFYVTDDMSGINRTFFKLSDTKVSEIPMVFLSSATHICSQGARTIFVVPSVVASFEDRLEIRQTWASGLYDENWEQTSERRIAFFFGSSGLSATDMAELWYESDTFGDIVVGDFHDTYANLSLKMAVTISWVAKYCPNIDAMVKVDMDTFVNVDLLSTLLKELPVEAGLNYVLGHRYNDDRSPVMRE... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 431
Sequence Mass (Da): 48594
Location Topology: Single-pass type II membrane protein
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A0A7M5XIG5 | MNIIFGKIISMILTFLIIWNVWILMTQKDDQKKPSEKDIFIDRFDEFLAQQDHDKKNIMNGRQGKLDSRVGSIGKNTFLDSTHLKRGYINVYYYIDICHNYDNYATKWNILFPEFPAKAELQENFYDERIVNSERVSRRMIAFLQPDLTENYSFRIESQTGCEVRIIEGPYFGKERHYDTFMLQFGLYKGQLQAEKNTNKPGKVYTVTSHEILLQKGKKYLIDVLHALPGKGFLRLKWKCKKEEHYMKIDPSLLTTLYSKPKVTDILPNVKYDVRVTEKSELLAKDRRLMFHQLQNIEQKMVKECEYWASYIPDRFPPDH... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 645
Sequence Mass (Da): 76647
Location Topology: Single-pass type II membrane protein
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A0A7M5UYK8 | MAENSKVEKSENLSTDHQLGHDKDMETVWLETHPECPVCLQPCLQPVQTPCLHVFCFLCLKGFVYRSKRCALCRSEVPFEYFQNPVVVKIKNGEASLTSSTSIEITEKYNWFYEGRNGWWEYDERAQVTLEEAFKTEARSCELLISGFSYFVDFGDMVQFRKSHPTRRRRIKRDRIGVDRKGVAGLKVSSCTTSSESQNLDSSKSDTDLTSSEKIKEKSQSDLALDTDDSEQELVSQASGSVDIPKPVSSTTFDENELAEQLDKTL | PTM: Ubiquitinated; autoubiquitinated.
Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Catalytic Activity: S-ubiqu... |
A0A081NCN7 | MSIQVGDHLPDIDIYEYIDDGSHPEGPKIWRLPDLAHKKKVLAIGIIGAFTPICSSNHVPGYIRAYDEFVKQGIDELWCISVNDPFVMWAWSEEMRCRDKMRMLSDGSAELVSLMDVTLDLSGRGMGVRSDRFAMVVDNGVITDFLREDPGHFCYTDADTLLARL | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
EC: 1.11.1.27
Catalytic Activity: a hydroperoxide + 2 glutathione = an alcohol + glutat... |
A0A367MH93 | MRRLLLVLLLLLPLPALAAEARPKIGLVLSGGAARGLAHIGVLKALDEQGIQIDAIAGTSMGAVVGGLYASGYTPAELERIALEMDWQQALSDAPPRKDVPFRRKQDDRDFLVKQKISFRDDGTLGLPLGVIQGQNLAMVLESLLVHTSDNRDFDKLAIPFRAVSTDIATGEKVVFRKGHLPQAIRASMSIPAVFAPVEIDGRLLVDGGMVDNIPVDVARDMGVDVVIVVDIGNPLRDRKDLSTVLDVMNQSITLMTRKNSEAQLATLKPGDVLIQPPLSGYGTTDFGRVPQLIDAGYRATTVLAARLAELRKPKDLNSE... | EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 744
Sequence Mass (Da): 82630
Location Topology: Multi-pass membrane protein
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A0A433SZK4 | MASNSEVRSNDRRRLRRHQNIRNDDAVIVLESGTDCIDLTTENNTDDIIDMTEHASGLMDLPVVVLTPTDYVGPVRHRTRRGSGRRGRHRSSTRRNRRNSRSLEASPRQSSAYVYLSDESDSELPDPANQPEASSVANSSVLQSPENVSIVCPICLDDTRQMRRNFKELKSTTCGHIFCNVCIETAIRMQHQCPTCRKRLTLRSIHPLFI | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 2... |
A0A7M5UYB9 | MIFFLYFSEIVMTVRKRYNENKALEPSQKVQNVNPKENNNYFQNPQNFFTMSLMLRISSVLLTQTFFVPDEYWQSTEVAHRQVFGYGYLTWEWKAQIRSYLYPFIFEMYFQLLKILTVDFYVLVRYGPHFIQAVLTAYYDISLQKLTLNVTDNLEIANYSYYLNLMSWFLFYTGSRTLSNVAEMCFSTIGLSFISFGKPSDVNSLVFALLFGGIGCIIRPTCFLIWIPLVFILLLKNEIHILTLLKACFIAVPVLLVLLFGIDFYFYGSFTVVHWNFLQFNILENIGEFYGAHSWHWYLSQGLPVVLGVQVLFFIVGVFC... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 520
Sequence Mass (Da): 61281
Location Topology: Multi-pass membrane protein
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Q5KZS0 | MTPDLLDPIFTCLDCRACTTACPADVDVGGLIEQVRGQLRQAVPLTGWKALVSDVFLKGIFPHPSRLDWLGRLLKWYQKSGLQTVARKTGLLRVMPDHLAEMEAILPAVGTPVRRKYKHQPLIKAKGETKRTVAILTGCVMDVMFSDINEATIRVLTHNGNDVVIVPNQTCCGALHVHAGDRETGRKLAKQNIEAFQHVDHVIVNAAGCGCMLKEYPELFRHDPEWHEKAEQFAAKVEDVSKFLHDTGFKPPKAELNVRLTYHDACHLAHGQGIRQEPRALIESIPGVEMVAMPNADRCCGSAGIYNLTHPEMAQAVLES... | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 377
Sequence Mass (Da): 41930
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A0A496U422 | MLKDCKHVTFLTGAGISKESGIPTFRDKDGYWSKYDPMKLASPQGFLENPALVWEWYRHRLKIISSARPNQAHEAIKEMEKYFNITVITQNIDNLHIEAGSTCVLELHGNIFRSRCTQCDSKFDTSLLKEKIPRCPKCGGIIRPDVVWFGEMLNEDLLKRCYEVLTITDAIFVIGTSNQVYPAAGFPLLVKQHGGKIIEINLNNTPLSPIADVFLQGKATLWMKAILEKLKEWKNSMSLS | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysy... |
A0A3G1RGY5 | MAFPRLNNMSFWLLPPSLSLLLMSSLVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAINFISTMLNMRPKGMVLDRMPLFVWAITITAVLLLL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A3M2D6I1 | MAFDESIAGVRPFFLFQVFWMSRQEKATLTKRVEFCASHRYHNPAWDAETNRRVFGRCNNEPSHGHNYLLEVTLSGDIDPVTGMIINIYDLKQYLWEILEEFDHKHLNLDTPYFQRTIPTTENLVHVLWRLFSHHPRIPTLEHIRLYEDEDLFADLSRAWVEESRATGVPRARVTRMYRFSAGHTEDEHLWGHDYSVSVAVDGPIHPETGQVVDLSDLDALVTRNVLDRFHGKDLRWDPAFQGQSVSEVALAGVIYRSLANRLRMGQVAGISVRASHRSEACYMAAEHDAVFSAFPPS | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 298
Sequence Mass (Da): 34320
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A0A5E4Q8D1 | MLSLLGASAVVVAVGRISASRILAVIPTPSISHQVVFRPLVQELARRGHEVTIITTDPVFTSSKFENLTEIDVHDVSYDIWTKNYIEHPEFGTKDFVFDNIYDLLEVHVRLIEVQLLSKGVQDIIHNKNIKFDLIMLEAVSRPSLIFSHLYKVPVIQVSSFGMMLDSGDVVGAPTHPLLYPIMLSQRIYQRSFWEKICELYKYWKVMRAYYNLEKQEHKILQRIIENDLPNYDVLRNNIEMLFLNIHPIWVDNQPIPPNVISIWGIYEKPKNDLPQDLKDYLDSSKNGVIYLSFGSNAQSSKLPQETLQMFIRVFSNLPY... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 519
Sequence Mass (Da): 59969
Location Topology: Single-pass membrane protein
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A0A7J4NVM4 | TGQMGHTDPEVFGEGLEAVCTALARMIAKDGEGATCLIEARVTGAASESDAVLAAKAVIASPLVKSAIFGRDPNWGRVVAAVGYSGAEMEQDRISLTFANNYTSASLVEKGRIISTSEDTLKEIMGSKEVIIMVDLGVGSGCATAWGCDLSYDYVRINAEYTT | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
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