ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A173GH67 | ETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEAVPGEEEQFIAYVAYPLDLFEEGSVTNMLTSIVGNVFGFKALRALRLEDLRIPPAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL | 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: 164
Sequence Mass (Da): 18007
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A0A420Z3H1 | MEALYSKYRPTNFEEVAGQVVPKQILLNSIRKNKINHAYLFYGIRGTGKTTLARIFAKTINCAADTAPCNMCDSCKSINQSTSLNVIEMDAASNSGVEDVRSLIANSSLISPDGKKKIYIIDEVHMLSKSAFNALLKTLEEPPRDTMFLFATTEINRIPDTILSRTLVINLQTLSDEDISSTLENIVIKEGSDFEKGSIEYIVSLSGGSMRDAITLLELCLLYSNSLKIGDVIKVLGIIKKEEIEDMLLRNPMLIKEVFERPEIDPKRLLLLVIETLNSFFINGSMTKNLSILSADLLQVFMTIKDPNLLRSAIPSIILR... | 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: 534
Seq... |
A0A090SWR9 | MIPTPSSHPSLPEVLYTSAQVREGEGLAAQACHVDMYSLMLRAGQAVFDELLHRYPNVKHILICCGKGNNGGDGYVVGKLALERDLAVTLWQVGSEKELKGDAANARDAFVKAGGVISPEQNTVPNSVDVIIDGLLGTGIKGEVRPYFAHLIERLNQAQKPIVAIDTPSGLNTDTGAVAGTAIIADYTVTFIGVKQGLVTGRARAHTGVLSFAGLGIDQVFAKQNTANTLLALSSWLELMVSRARDTHKGRQGSVFVVGGNDGMSGAAYLASCASLKSGAGLVATFVNQGSCLAIRALLPEAMVSSGEADSVWLEQRVHW... | 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... |
H5TMN5 | MTLSCLRGQSGERRRVPADAAAPANDIEHASDAAGHYVLDNMAAVLAVKHLGDAKSRLVATLHDEPDDLAVHVDSPPHAAVHDAAGVLSPVQRDRLKADPGAFVLAMLADTIGALHDAGVGDVVVVTPDDRVRATAYGLAAQVVSESTDGTGGLNAAYALGASTARRLWPDRRWILMIQADLPAAEPQSLRQIVSAAAAQGESMVTDRAGTGTSLLLRRASNSDAPCFGPDSAAAHRAAGIAELDPDHHLWPDIRTDVDTVSDLTAAIRLGVGDRTLSVLGDL | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
EC: 2.7.7.... |
A0A7S8HC88 | MCSRPTRSRSSEGLSVTQSDQQATWHGTTILTIRKGGKVVIAGDGQVSFGNTIIKANARKVRPLGQGNVIAGFAGATADAMTLFERLEGKLEQYPQQLLRACVELAKDWRTDRYLRRLEAMMIVADARASLVLTGTGDVLEPENGLMGIGSGGHYALAAARALEDSEMSAEDIARRAMAIAADICVYTNDKVVVESLDAPS | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
EC: 3.4.25.2
Subcellular Location: Cytoplasm
Sequence Length: 201
Sequence Mass (Da): 21514
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C7QJS0 | MHDFIAIGLGPYNLGLACLTDPIEGLNGLFLEARPEAGYAWHPGMLLPTATLQTPFMADLVTLADPTSPYSFLNFLKETGRLYPFYIRENFYPVRAEYDEYCRWAAARLRTIRFGQTVSRVEYDEAEGCYVVHSVGTDNGAVNEHRARRLVLGTGTPPHIPEPCRGIGGDLVHSADYLANRALLQSKESITVIGSGQSAAEIYLDLLADAGADTYHLSWVTRSPRFFPLEYTKLTLEMTSPDYVDYFHALPEATRYRLEAEQKGLFKGIDAVLINEIFDTLYLKSVRGQVATRLVTNTELRGASYDEAGGTYMLDLHHEE... | Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 1.14.13.59
Catalytic Activity: L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+)
Sequence Length: 432
Sequence Mass (Da): 48275
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C7QKP9 | MSGSPADEGSPAPGPERALRLGTRASTLALAQSGMVAEALTAATGRAVELVHVTTYGDTSREALSVIGGTGVFVNALREAIYAGDVDFAVHSLKDLPTAAPEGLHLAAITERAAVNDALVARDGLKLADLPAGAKVGTGAARRMALLKMIRPDLEIVPIRGNVDTRVNHVRSGDLDAVVVALAGLQRLGRAEEATEVFGPDVILPSPGQGALAVECKDPELAELLAVLDSPLTRAAVVAERTMLAVLEAGCSAPVGGHAIALDDNVLSLTGVVATVSGSRGLRLSHAGAVSEPEALGRRVAQALLADGAAELMEAGA | Cofactor: Binds 1 dipyrromethane group covalently.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.... |
A0A9D3S0X6 | MPAYATNMRLKFPILALTLEILTIILFAFFVVYDDGKPSSHGAHDGHAPSNKTEDKNLRLYPVFQDVHVMIFVGFGFLMTFLKRYSFSSVGVNLLLAAFGLQWGILMQGFWHMSDGKIKMDILRMINADFSTATVLISFGAVLGKTSPVQLLIMTVLEITIFSLNEHLVAEVLGVSNQSAARLHAQLPINSHTTSPATNQQPDHTPSYQSAARPNTQLPISSQTTHPATNQQPDHTPSYQSAARPHAQLPISSQTTCPATNQQPDQTPSQSSYSCSFFCLYLLY | Function: Functions as an ammonia transporter. May play a role in the elimination of ammonia in the gill.
Subcellular Location: Cell membrane
Sequence Length: 284
Sequence Mass (Da): 31347
Location Topology: Multi-pass membrane protein
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A0A9D3WNT3 | PVYLQTIQHSNILKQESGSGCVMEGDTFLPSNSSSPYSKNDSRNRVFREKYTFSSYYQHSSPIAVMFILAYIFIFLMCMIGNLLVGVIVLKNRQMRTVTNMFILNLAISDLLVGIFCMPSTLVDNLITGWPFDNAMCKMSGLVQGMSVSSSVFTLVAIAVERFRCIVYPFRQKLTLRKALITIVIIWVLALIIMCPSAVTLTVTRDEYHFMVDAYNNSYPLYSCWEAWPDKGMRKIYTTVLFSHIYVAPLTLIVIMYARIAFKLFKSSAPIGGSQSEENEGRRVSKRKVKVINMLIIVALFFTLSWLPLWTLMLLTDYGN... | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinosit... |
A0A101J092 | MKELVVGVTGASGMIYAERLLMELEKQCRVHLVVSGTAGTIAALEGISFSNFSVICEENSDLAAVIASGSFRFDGMVVVPCSMKSLAGIAHGISDTLIGRAADVCLKERRPLILVPRETPYSRVHLQNMLAAHDAGATILPASPPFYQKPETIEDIVDMIVSRILDHLGIEHTIGSRWSGCHA | Function: 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.... |
A0A496NB99 | MKKNTTTNWNDPNAKTEADKYQNPIPSRLLLLQTVAQMTNQAKAATVESLAMHFDILYDDERFFALNNRLKAMLRDGQLERSDGIHFNVAPLPSTYKGTVASTAKGFGFVVLPDMPDLFLHEKQLRLVFDGDIVEAIATEFKGKPEAKITQVLKRANTEFIGTLDQDDEGYFVQLSGSNSHQPITVTDDNVATINAAIGDSVKVSLIDFPTYQEYATGKITELLTSLNDRELIIETTLHHFAIPAAFSQKTLEQASQYQEPNEKDFVGRTDLRDLPLITIDGEDARDFDDAVFAQKRAGGNYRVVVAIADVSHYVTAGSD... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 745
Sequence Mass (Da): 836... |
A0A4Q3CRY7 | YQALQRIAPVVTPLLQAHDYTPALTELAALRTPIDAFFDSVMVMADDAAVKQNRLRLLAQLRALFISVADVSVLQ | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 75
Sequence Mass (Da): 8266
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A0A2N1W2P9 | MSEKKKTLTAAVKFVTAFFMALLSAVIFCFFIPVQPLSGEKVNVYINYGSGIRAISRELKNAGIIRNRTVFRIYSIITGNTTKLKAGEYEFGFGENIAGIMDRMAKGDVIKHPVTVTEGMDVSEIAAALASKNMADPVRFMALCRDAEFLKRNGFPKNNAEGFLFPDTYGFVKGETEERIIAAMYARFKQKVNLNIDENYVINGYKISGYGILKLASIIEKEAQLDSERPKVASVFYNRLKSEEAYLQRLESCATVRYAKNKKKGALLYKDLKFNSPYNTYIAIGLPPGPICNPGIESIEAAMAPADTKYRYFVVKADGG... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 341
Sequence Mass (Da): 38021
Location Topology: Single-pass membrane protein
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A0A1B8V328 | MSTSPSLADPREIIARRAAREIRDGQLVNLGIGLPTLIPGYVPEHIQVWIHSENGIVGVGPQAGAHNLDAELIDAGGGYVTVVPGGAIVDSATSFGIIRRGLLDITFLGALQVSQHGDLANWLVPGKIVAGIGGGAELAQKARQVIVTMPHCDKDGRAKIVEHCELPLTARRCVTRIITEHAVFDIDDEGLLLREILGDLSLAQLQAITAPFRDARH | Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; acetyl-CoA and succinyl-CoA from 3-oxoadipate: step 1/2.
EC: 2.8.3.6
Catalytic Activity: 3-oxoadipate + succinyl-CoA = 3-oxoadipyl-CoA + succinate
Sequence Length: 217
Sequence Mass (Da): 23086
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A0A7X8GWJ0 | MFEDELIHVGFVSKTHGFSGIFRINFLPVFRLSSPLKGFIFIAVHNKPVPFHILEVREYSESYILIRTEEITSKEQAAAFGGMKVLLKKKNLQRYLKEGWQELQLTGYLVVNQHHEETGRVVAVEKTPAHYLLVLDDERLIPFHSDLIINIIEEEKTLIMNLPEGLD | 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 ... |
A0A935TRG6 | MQQTQSPYLNLLITGCNGQVGYSIKQYLQQQQYPEIKAIYTDRNSLDIANPTKVRQMFEQNPGINFVINTAAYTYVDKAESEPELAFRINTYAPQLLAQTCAQYGAWLLHLSTDFVFDGQKTGPYLPTDTPNPLNIYGKTKLQGEQAVLAANPNKTCVIRTSWVYANHGSNFVRTMLRLATERPQLQVVNDQRGSPTYAPDLAQALITICQQIGASNSHSYKIKPIYHYANGGSCTWYELAKTTLEYAQINCPVIPIAAHQYPTPAKRPRNSQLDTTDIVNDFNIEIPNWKISLKKCIGSLKNGNLLSKTKT | 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: 312
Sequence Mass (Da): 34990
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A0A0S8FHW8 | MSRAPGRQRELPTFYYHQHFLELLDFVSTHYRHVLNGEELSLVRDFRQLDRPAQCLYVRLVNRKGRIFAANRLRYPEIGGLSRAIAALREREWVGSPGTEFFEDVLGFLTKTQIQDRLVCSLPGISRSLKKKELVDLALRHCDPREFMAQMDVERLLVQRRVDWVRFLLFLYFGECREELSRFTLRDMGLVRTHSFRNSYEPRFVDREEAMETYYFASRLRQFEHSDEGARKAMMESTGDWPQPVFDVAADLRDRLAYAVGRELETTGRGDAAMDVYLRGESPACSERLVRLLFAAGDRDGARAHLEACLENPRSDEEWL... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
R7CJI7 | MKLLLHACCGPCSLEPVRLLKEEGHDIAIAYMNSNIAPASEYQHRLSTLLDWAKAQDIPVIEGPYEPTRWQEAIRNAWHPHSSNSDSTQTSAHTKQTSAHTNHEASAPRASFPLEASSAFVTSSELDASPASEANSQTITPSFNTGIDPEFDPARNPKFAHLYHDRENRCRACYRIRLEELARFAHEHGFEGIGTTLTVSPYQYTAIIQEELQRVAKPYQGLSVVFRDYRPYYPEATKRSRDLGMYRQNYCGCAYSDKEAAAEREARKAARKKKKAEERRAKLQALTTDDFDYELPEELIAQEPAPIRDECRLLVMKRDT... | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L... |
A0A2G9N661 | MGKTISVTFLSSYLYCARKLYLECVLRIVEPPKETLVLGGLRHEVYEYINNIEERIVKGIKERSSFEDVLEIYRKEYSELLMKTIGKYGRILSDLKLEPKEIFKKNWPLIVKEADKRANNVFSFMERTGLSGEELWAKLTPKLVSELNIMSENLGLKGRIDQVEVYDDIVVPIELKTGKSPNEGAWPSHRIQLLAYLLMLSERMDGSSSAKDVKEGKIIYLDSDKVVNITLNPFAEKEIKELVSKTNAMLNSGKLPDFCGNENKCSACGLKENCYDEVFLKERLEALPKAR | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
A0A0J0YSD7 | MTYWIGLTGGIGSGKSAVAALFSKLGVPLIDADNISRSLTAENGAALIPIRNLFGNQMFDTTGRLNRTALRTLVFNNPQAKKQLEALMFPLILDNIRLQQQQAAAVYGIIEIPQLIENPLFWPLVQRILVIDAEESIQIKRVISRSGLSEHEIIRIMANQANRRQRYKLADDVLANNTTLEILNDKVQRLHTYYQEIFSHSQQKTS | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A850T5F9 | MSRTLFSHAYGETESSRKRLAVQAATFIVMLMAFYIGSFYNFLLFHTLAEMFAVVTACSIFMVTWNARPFFKEKSFFSFVGIAYLFVGILDLTHTMTYKGVNILPGIDPNVPTQLWISARYLESVSLLGAFFLFKSRIKAQIYLFGFSAATLLILLSIFHWQIFPDCYLEDAGGLTAFKKNSEYIICLILGLALSALQHNRNRFESTLFNWLQASIIVTIISELLFTTYVGVYGPAIMLGHYFKIVSYYCLYKALIETGLSRPYSTLFKNLTDSRESYQALFSNMIDGFARHRVIWDKNGIPADYEFLETNPAFEELTGF... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A0N0KIF6 | MTGLLEPHTSRFSSPPHARPATGARPLLEVRNLSLSFTTAHGALPVTRNVSFSIAPGERVGLVGESGCGKTVTGLSLLRLLPTHSARIEGDVLFDGTDLLKLSPRRVRAVRGRDIAMIFQEPMSALDPVFTVGDQISEAYRIHFPASKAEGRERAIAALREVGIPAPERRCDEYPHQLSGGMRQRVMIAMALICKPKLLIADEPTTALDVTVQAQITDLLRSLSERTGTALIFITHDLGVVAETCTRMITMYAGEVVEDAPVDEVLTRPRHPYTSGLLRSLPGLSQRRGVLSSIPGRVPSPQAMPAGCRFRSRCAHAVPG... | Function: Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Cell inner membrane
Sequence Length: 351
Sequence Mass (Da): 38148
Location Topology: Peripheral membrane protein
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A0A1G6ZNI0 | MRPFLKMHGLGNDFIIFDAREDDLALADEAVRALSDRRRGIGCDQLIILRTSGKADIFMEIRNADGSRVGACGNATRCVGQLALDESGKEKVLIETDAGLLTATRAEAGISVNMGPARLAWDEIPLARETDTMKIDFAMGPLFEPTCVNMGNPHAVFFVEDADTVDLPYWGPQVEKNAMFPERVNASVGTVKGDTIRLRVWERGAGITDACGTAACASVVAASRLALIDRKATVMLDGGPLEVEWLADGTVQMTGAATLAFKGEVAL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A8D3EF26 | MSKDTEGKSEKIMDMESKVLWYPDSKRNTQMDKFRIQVNGNYGLNLVNYNDLYQWSVDSYAEFWAEVWRTCGVVSSKPYEEVVDVTKQISDVPEWFKGARLNYAENLLKHADQDKVALYAAREGGEEIVKVTFGELRRDVALFAAAMRKMGVQTGDRVVGYLPNGIHAVEAMLAAASIGAIWSSTSVDFGVNGVLDRFSQIQPKLIFSVAAVVYNGKTHDHMEKLNSVVKGLPDLEKVVVIPYARSKHETDLSKIPNSVFLDDFLASGRGDADQFPQLEFEQLPFSHPLFIMYSSGTTGAPKCMVHSAGGTLIQHLKEHI... | Function: Converts acetoacetate to acetoacetyl-CoA in the cytosol.
Catalytic Activity: acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP + diphosphate
EC: 6.2.1.16
Subcellular Location: Cytoplasm
Sequence Length: 577
Sequence Mass (Da): 64406
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A0A955G836 | MANLSVGDVLALARLARLELNEQELKQAIVELNSILGYVEQLGDVDIKNDKPTIQVTGLKNVMREDKVIDYQASPDDLLKNVPSQEGRYINTKRVIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A955GBP0 | MREFTYYLFNLLVFLPVLVLSFTTDVKPHRHVRGLLAGFLLVSVPFMLWDIWAAQAGHWGFNVAYITGPYLFGVPLEEYLFFITVPFAMIYVWGVVKKYVTDRATAGFFPLLAFGITAGYSVWLLVNYWGNGYTRSVAIAAIIAVLVAAVSRIAYTWRFWTFQVVLLGLFLVFNSLLTMLPIITYGPDAIIGFKIGDIPIEDFLFNFAFINLFLLVYTFVDQPRIVK | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 25919
Location Topology: Multi-pass membrane protein
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K7AHM6 | MLLAAMVIFPGLTPAKALGGLGLVSVAIRFAFKEIFENFFAGIMLLWKYPFEKGDFIECESIMGKVEDISVRMTQIRRPYSELVETPNSFLFKNLVRVLTDSDFKRLTIMTGLAYSEDANESLQIVEIALTTCNTVNQDLPIEVFLNGFGDSSIVIEVIWWTDPTPLGQRKSRGKVVGAIKRALDQAGIKIPFPCRTMTFKEPLRIHQIKESSPTE | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A3B9AHP4 | MSSRSGMKFNNRELSWLAFNGRVLQEAADASNPLLERIRFLGIFFNNLDEFFRIRVAGLRRAASLGRAAGKDAAGLKPQQVLALIHEKVMLQQEEAEKLWSALALSLKRHHIIVESGDTLTRAEHNWLNRYFTMHLKSRLFPILFQESEVMPELKDRAIYLLTACVFKQEKQKRLGVLEIPRDMERFVRIGEGGQKSKLIFVEDIIRLFIHDLYPGTATVGSAYSIKMTRDAELDIDDDVSRSMLEKMTRSLNQRKRGAYVTFSYDRSMPVELLNSLLKSTKIKDPHQLLPSGRYTSLRDLLNFPDFGKKNLRYPPLVQV... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
A0A7W1KGJ0 | MNPNNDITPPQTPTSPGLPQGQSSYPSQQPTVQDQNEDKVFSSANTAMPSYSESRRDGWRSITSTLLLFLLAPVIALAIAAFVVQSYQVDGESMETTLQHQDRLIVNKLSRTWARITNNDYIPRRGEIIIFNQPSSNDSNFAQDRQLIKRVIALPGERIVIRDGKITIYNEQSPAGFNPDDSSSYKLSERYTSENVDQTIPDGEVFVCGDNRQNSEDSRWFGPVPSELIVGKLVLRILPFDKLKTY | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 246
Sequence Mass (Da): 27641
Location Topology: Single-pass type II membrane protein
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A0A2U9BRP4 | MAAYKLVLIRHGESCWNQENRFCGWFDADLSGTGEQEAKRGGQALKDAGYEFDICYTSVLKRAIRTLWFVLDGIDQMWLPVHRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSFDTPPPPMDEEHDFYQTISKDRRYADLTEDELPSCESLKDTIARALPFWNDEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGMSEEAIMELNLPTGIPIVYELDKNLKPTGPMQFLGDEETVKKAMEAVAAQGKRPIGVDSSPKPQPITGQSALLENMSPMKLCVPGDKLCSVEDCIPGTGVYLRHGYIYSSLAGYVLKKNEG... | Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
EC: 5.4.2.11
Subcellular Location: Cytoplasm
Sequence Length: 468
Sequence Mass (Da): 52389
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A0A415IX80 | MSVKSAVEKWNSDYLRYNVLASEKDEMGRYQTEHDLTALKMIIEEAKQATMRFESKKQRMEFMIRNGFYKEDLLRGDITYSDIEGLYNTYKKHDRGDIAFISQLVFLSSNYAYKLLESEVEGLVEDWQLPPKRYDDKYILMEDKSDRAVAIALEVSGGKLDLAHDVVKGMAMRSYHPATPTYANAGVKGDGQLTSCFILKFKDSLQSVADMDSYTIHLSDMGGGIGFDATDVKAVGEKVGNIDNRSIGVLPLANRAEQALSIAVQGGIRKGNGVFFLDVFHPDIYALLDAKKENTDEKTRLSFLSVGVIMRDKFMELFEQ... | Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 727
Sequence Mass (Da): 82818
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A0A8C3U9W2 | MRVNTRLKNWFILVSSLLSVVCPTTAVPLSAKLWVVPLFLIKGGLAGAAVYVAYDQGLLGSGTEGAAALKKAQETLPPAIQEWTNYLGWEVRAAQLPPTPKFDFSISNYWNKGVHSVMSALSVAPTRACEYTVEGWKYMKDLVK | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 144
Sequence Mass (Da)... |
A0A356I883 | MNTVVLKASVQQKQAMMAHYDRYRQDSKNPYIEAFFKLTGASLSIYTSGKVVFQGEMAEQEARLWGYEPESSEQTTNPGQNLPMIGTDEVGNGSYFGGLAVVASFVRPEDHAFLKSLGVDDSKKMTDQKICRIAPL | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 136
Sequence Mass (Da): 15090
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A0A4Q2ZJX8 | MAEVIRMPLLSDTMKEGVIATWHKKVGDAVKADDAIADVETDKATMEVMPYVDGTLLYVSPEKAIPVNGILAIVGKSGESYQELLDNESKAVPETAPAETGKPESKEATDVAEVKNPANEVKASPAGKQENTTGEIPNGNVSNENAVNIEGALPKDVTVVRMPLLSDTMKEGKIVAWHKKEGDSVKGDDVLADVETDKATMEVMGYADGTLLHIGVPEGEAAQINAIIAIIGPKGTDISAILNAPAAPQPATEDRPETTQSTAPEAKQPEQKQPEASKATPAAAETAASEDSGDRVKISPLARRLAEDKGIDIHALKGSG... | Cofactor: Binds 2 lipoyl cofactors covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E... |
A0A9D7I4K3 | MKNSYLFSLIFPSALLSCHKGADLDVAQTRAFPIEYNSGIKEKALNYANMLPNPSGINKDHPELVALGKKLFYDNRLSGNGTQSCNSCHNLSTFGVDNKTLSKGADGRLESRNTPTVLNASLHFSLFWDGRAASLEEQIEGPILNPHEMGMSSKVELESRLSRDPEYIALFRRAFPAATEPLNFDNLSKALGAFERTLLTPSRFDKFLLGDESALSEQEKRGLSLFVDLSCIKCHSGNTLGGNIFQKFGLVRDYWEYTQGKNRDEGLFQLTKDPADKYVFKVPSLRNVAKTAPYFHDGSVETLEHAIAIMAKAQLGMELS... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 344
Sequence Mass (Da): 38024
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A0A4Q3BXX2 | NFATKYNLFGFKGRLASISFNHQSNGRDMPLSRSWNRVILQTGFERGDWQAYFRYWFRVPDENKSDDNPDIVERIGRGEVIAIYCKDRHTVTLTGSTNFQMNDSFSGYLEASWSYRIAGNLKGYLQFTHGYGESLIDYNNRQTTIGLGVSLIEWL | Cofactor: Binds 1 Ca(2+) ion per monomer.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Cell outer membrane
Sequence Length: 155
Sequence Mass (Da): 17959
Location Topology: Multi-pass membrane protein
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A0A951NVN3 | MNQPFIGHVHELRRRLSWSALLVFAVAVAAYFWREPILRWLSAPLGQTLYYDRVTGAFEFVMQACLLAGVLAATPLIIYHLIAFIRPALPRPLSNKAIISTIILATLLIGAGVLFGYYVSLPAALTFLSHIDTTNLHPLIAANSYLTFVMAFLAIFGLVFLLPLLIILSDNIRPIPPSALIKARKWVIIGAFAAALILPIAPDPVSQVMLAMPIIIMYEISIWLIKYKAWRRRGAIATPVVALPLPEAAAQHVGPPASVSRPPRARHAPMRPQVIDLRSR | Function: 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.
Subcellular Location: Cell membrane
Sequence Length: 280
Sequence Mass (Da): 30898
Location Topology: Multi-pass membrane protein... |
A0A2N1W7F7 | MRIVLDAMGGDNAPQVEVKGTVDAIKKNRDLNVILVGKKEEIEKYLNTYKLSEKERARLEVVNANEVITMSDEPAKAFKQKQDSSMIVGAKLVKEGRADAFVSAGNTGAMLVTSLLTIGRIPGVIRPAILVPMPSKSGTTAVLDAGANVDCKPIHLAQFAIMGSIYASHIFKINKPRVGVMSVGEEEGKGNELTIEAKEIIKKLNLNFKGNVEGRDVFNGNADVVVCDGFVGNIILKVGEGAGVLLVSEIKKGAKKSLLTIIGGLLMKKVFIQVKDRINPDAYGGAPLLGIQKPVIICHGSASAEGIKNALIVAYEFVDG... | 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-... |
A0A3T0RMH1 | MIHTHQLSGAGNTFSVTWDSPEAKGINDRPKFVRAVCGSTKTDGFIFLSWLDEDQHHLQWDFYNNDGSMAEMCGNATRCVAYYAKNIMHIQGNHLKLQTIAGPIDIKILDKELFEVKMTAIQKLEHAKFFWCDTGVPHIVMEIPDFTDYRKYLSHCRELRFHADFQPRGTNVTLVLLDTAANKLKAVSYERGVEDFTEACGTGAMAAAYYNLNKREQKETLVEMPGGLLKMNLSDLQNPLMTGSAVQLGEYNAT | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
EC: 5.1.1.7
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Length: 254
Sequence Mass (Da): 28650
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A0A3T0RR25 | MGMIFYNLLYNFLRFLVVVLSPILDKKTNAWIELRHNGEIFKTSVSPNSKKLWIHASSGEIEYAKSFIREFKKSQPEAQIFVSYSSLSAPLLFKNIAGDVTQFFPLNWDITSDNDKLLDFIKPDLLIFSRTDYWPNLITQAHRKNIKLATIAANPTRSILSSFWLKFCCSGFKYMSCVEENQVKYLQKLLPYTKVEFIPDTRFDQVFHRLQQKSLVQLDASQKRITLGSTWPKDDEVIKPLAFKLINQGYSLVWAPHDIKHAPELLNDLKNRLPRKKIIKLADFNGSETFDILIVDRIGVLADFYRFSKISFVGGSFVSK... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A3T0RSF9 | MTEMSRNLFNYQNNELHFAGSRLSDLSVVSNYQEPVLVYQKSMISERIAWVKSWAKLKQLHFAMKSNYHPEILKLFKNAGCGLDVVSLGEIKHGLECGFSPKDFIFSGVGKTIAEIEFAIDQQIYQINVESAAELRRISEIATRKNKKISIGLRVNPLIETPTHPYISTALKDSKFGIDLNDVPECLDVIRKNPLVEFKCLSFHIGSQILDPLVFKESVEKMKVYFLDLKKQFSNLDRFDVGGGLGIDYKNHDLTLDFDRWNSLKSAYDESLKDFNADVLSELGRFIVARSAVFICQVQYIKNKNMLVLDLGMNNNLRPS... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Length: 396
Sequence Mass (Da): 45303
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A0A9D3S2B1 | MVGRTARGPFSFSSDDISGKRADEPDRTCVHFIVAKRPTDLWPGITKDSTGKIDTVTIKSEVLSDPGGKMNKVSTQCKTEQRCSANVPIGFVGAGNMAFGITQGILMSGEVSAENVRVSAPSSNNLGRQSEMGVGITHSNAEVVSSSRLVFLAVKPHLVPGVLQEIASHVTREHIVVSVAAGVTVATVEALLPPDSVVLRLMPNLPCLVQEGALLFARGSKARPEHGALLRDLLAPCGLVEEGPESWIDAHTGLSGSGVYLFAEALAEGGVKMGMPSALAHRIAAQTVLGAGRLLRDSGKHPAQLRADVCTPGGTTIFGL... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
EC: 1.5.1.2
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
Sequence Length: 367
Sequence Mass (Da): 38285
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A0A2H0W0Z1 | MTNHEQTCLSVAEEEAYEDIHAALKKLLGKNYTKAPIIIGYPPSPELGDFAVPLFHLAKELKRKPQQLAEKLAAEFKPTKYLSAARAAGGYLNFYADKPQFAELILMQILHERSRYGNNECGGNQKVMLEYSQPNTHKEFHIGHLRNTVLGISLTKILQANDYQVIQANYIGDTGAHIAKSLWLLQQKDFNEFKQAKNKGKALGQNYSEAVNKLEDRPEAKLDVSEIHRKLENGNPELTKLWQETREWSLDEFKEIYKELGANFDVYYFESEVEDDGKKLVQELLDKKILQESEGAIIADLEQYGLGVLILLKSDGTASY... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 578
Sequence Mass (Da): 65496
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A0A2G9N5R2 | MKFGGTSVGSVAAVQNVHKIVKERLDKAPIVVVSALSGITDALIKSAKDAEQGRIDDSAIRKKHNDLLKGLGLDDGLVDDELSELLEVLKTIAEEGLTKRSLDHVQSFGERMSSKIVAAYMTKKGMNARALNSYDVGLVTDSNFTEAEIDSCSYENLKKNPLLKEKGIVNVVTGYIAKDHKGDITTLGRGGSDFTAAIIGAALDAEEVQIWTDVDGILTSDPKIVKNAVTIDEISFEEAAELAYFGAKVVHPKTIIPATENNIPVLVLNTHNPSHKGTRIVKSARDAEHGIFKAISSKKNVTIIRIVSSRMLGVYGFLAV... | 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: 439
Sequence Mass (Da): 47418
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A0A2H0VYC0 | MSKDEFFIETALKLAQKAGPLTYPNPKVGAVIVKNGKIIGRGYHKKFGMPHAEVEAFNNCIMDPSGGTLYVTLEPCSHHGKTPPCTDLILSKKIKRVVCSSLDPNPKVEGAKILKEAGLEVSIAARNKEAIEINKAFFKYQQTRLPYITLKIASSMDFKIWSPRVAKLTGKKSLKLVHELRAQVTSILVGINTILKDDPKLNVRLVKGRSPAKIILDSKLKVPLKAKALTDKNVIICTEVKSSPKRSQLESMGVKILTFPTLQSLRKVMEKLAKLGHINILVEGGQRISSSFMAQGLADKLILFVANKSLGGTGLEAITN... | 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... |
A0A0S8FDP0 | MDKDVKFAFVGGGNMAANLIGALVSGGCNPKNFRVADPDPSQRNRLRQRFGVEITDDNAAAATGADVVILAVKPQVAAAALQDMAPAPDASLYLSVIAGIREADLRRWLDTDGSIVRAMPNTPALLGCGITGLYCAPSVPGAMRELAEGIMRSSGAVAWVDDEALLDPVTALSGSGPAYFFLLMEVMTRTGIDMGLDPEAARLLTQETALGAARMALESESGVAELRERVTSPGGTTAAAMEVLKSRGVPEAIADAIRAAAERASELATEYGNNRGS | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A0M2U1X8 | MVIKCGIDLVEINQIRKAIDISGERFIHKIYCPAEIKYCESKGWQRYQGYAARFAAKEAVAKAIGLGFSQGVSCKEIEVTNDTQGKPCVILRGLTKEIAEAEGIMNIQVSLSHSNCHAIAMVVCYDNSK | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 129
Sequence Mass (Da): 14228
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A0A177R348 | MHRPRILVPMIRFVLCRPQHPGNIGSAERAIKTMGFTDLRLVAPERYPAPEAQWMATNAGDVLQETKVCSSLKEAIADCVATFAMSARGREWSPQVLDVRTAAVRAREVQGDVAFVFGNEQAGLTNEELFACQNLVHIPASKGFSSLNLAQAVQVVAYELHMAVDVAIPSARSEQLATVDDIEGLYAHLEEAAMKSGFMTPQSRVRERWRRLFSRVPALEREEVNILRGLLKALLK | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length... |
A0A2N2GDJ2 | MTRMRIITSMIPLLPSVQHLDGYCASRFSYLTKDQWQQEIHAGKLSLDDVTVYDPAVLLTGGEVLSWDGSGIIEPEVDEKFTILHEDEWFVAVNKTGNLPVHPSGRYFNHTLTAMLEDRCARKVYPVHRIDRETSGVILLAFDGRRAGVLSEALAEGSKEYLALVHGYFPDEELIVDLPLGRDTQSAVSKKYKAWPGGVQKALTRFRKILTAGDMSLVRCFPETGRLHQIRAHLLAAGYPIVGDKLYGRDETAFLTFIKQGFTAGLRESLVLPRQALHAARLVILHPQTGKALVIRAPLPKMFAGVLLLT | 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): 34529
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A0A841CT25 | MPSATAERDVAPHGLPVHEVVLIAETDADTGLSGATAGERLATSGPNRLPERRGPGRLRRMLGQFHNPLIYVLLGAAALTAVLGEVVDASVVLGVVLVNAIVGYLQEVRAERALDALEAMVRTEATVIRDGTAVRVTSEELVPGDLVVLEEGDQVPADLRLVRTRELRVDESALTGESQPVAKDPLPVPHDTALADRTNMAYSGTLVTTGGGRGVVVATGADTEIGHVHRLVGSTRAVQTPLTRKLARFSKALTVVIMGLAVVSVVIGVLRGEPFADMVTAAVALAVGAIPEGLPAAVTVTLAIGVARMARRNAVIRRLP... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cell membrane
Sequence Length: 861
Sequence Mass (Da): 91166
Location Topology: Multi-pass membrane protein
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A0A7X6SMD9 | MENNLEQPGPQSSEEPSTPLRISKKSSSLIKWLIGGVVTFIAVALSVVGAGYLWYKDGLSSPSPQDSTTQRIVVKKGSTIGVIAKQLQDAGLIKSAKAFEIYYRFNGENPLQAGEYSIKRNLGVADIVNELAEGRNREHSITFLPGQNLMDIYNTFRRAGFKDSEIKFAFNNQYSRYGMMRQIPEGGDIEGFVFPDTYSFNENYTVGNILKRPFDYMQDYIIKENLESAYKKHGLTLYQGIILASIIQKEVNNQTDMGHVSQVFHSRLKKGMPLGSDPTFVYPAKKHKLQPHPDLDSPYNTYKITGLPPGPIANPGKEAL... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 369
Sequence Mass (Da): 41398
Location Topology: Single-pass membrane protein
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A0A4Q3BUD8 | VKDYKTAIQEVKNNQPDIIFSAIPIDNDSKNDMAPQQLSSFAQVPFVILSPSDAVETTTHSISFGADDHLFKTELTTAALKKSIQYCLERRKNNAQLREIIERFELLAKATNDIVWDWELTKRRSLWMGNGLKSSLGYNHQTIVVDTDFWEKGLHPEDIGRVLEKLEKIFKDGKVNKWEEEYRFKTQSGEYRNFYDRGYIIYEDGKPVRMIGTMEDITNRIALERKLEIETLLRQKQIAEAVVTAQEKERTEIGKELHDNVNQLLSASKLYIDAAANDISNNEVLLSQASGYIKNAIEEIRALSKVLHAPLIYELGLCES... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A1W0WZN2 | MVPGSVASQTPSAAANESSSPTISEEQHFLDLAYQIQRANRATHSAVEQSESSESSVSIITVETAPESLREEEEAEPVRELGQIDRLNLTKIILKRNKSRVTGEANPRKHETTKGSMADLRTLANFHVIETLKKNPKLVEEVSEVAKDAASSLGLLLKDPVIADAFLPVPVTLLPSLTSHHAVHEVLQLQPEINLLMHRVSHDRNFLTQSLAGVSSVDPFIKSLLNIYNQVDIDAQWELDFIRSDYLLHCNDPTLSFVDAVKAGSYKQVEVNMICIAFAGLSSRMQDVHNRVLNFLECDVVPAENAGDVLPLYGGALKLA... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Length: 608
Sequence Mass (Da): 67490
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A0A640TI07 | MNERPRRAAPWQGQWPVIGVVAVGGAIGAAARYGAALLWPTGNGSFPWTTLAVNVVGCALMGVLMVMITDVWPAHRLVRPFLGTGILGGFTTFSTYAVDIQRLIEARHPAAAMAYLAGTVLAALAAVRCAVTGTRALLELRRRTA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 145
Sequence Mass (Da): 15327
Location Topology: Multi-pass membrane protein
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Q8ITE6 | MGLSEGAEVVPFKHKLVKHNVIKFGYMHLAALYGAYLCFTSAKWPTLLWAFLLLEFAKIGITAGAHRLWCHRSYKAKLPLEILLLIFNSIAYMNTATYWVRDHRVHHKFADTDADPHNVNRGFWFSQIGWLFVRKHPDVIEKGKTVFMEDIHKNPLLRFQEKYAFFVIGLWAYVIPTVVPMYFWGETLSNSWHICTMLRHVLTINQIFLVNSIGHRWGNRPYDKNIKAVENLAVSLMSTGECFHNYHHVFPFDYKASELGMTKFNAATMFINFFAWLGWAYDLKTIPDEMIISPGPRRARGWGRKSFGGLGGGMFDPTGK... | Subcellular Location: Membrane
Sequence Length: 327
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 37685
Location Topology: Multi-pass membrane protein
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A0A924UV64 | MEKKSHHRHHHLTAEANKKRTTDSQSIEFIQHVHELRNRIFWVALLFIGASALAYQFRDILVHLVLSPLGDQKLIYLTPSGGFSFIFQITMYAGAIFAAPLLVFQLYKFVVPALPGRARRHAALVFISAFLLMCSGVAFGYFVAVPSALSFLTTFAGGYVNASLTADSYLGFIIAYVFGLGALFQIPLLLIFWHWISPLTPKQLLNSERFMLIFALIAAAIITPTPDVVNQMIIAGPILVIYQVGVIAILIMIKAERKRPRRVVVGDLLVSLVAQRAQSMHLPSLTLPSIEDLAPRRPVATVSGERSNSLNKKLLTTQKP... | Function: 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.
Subcellular Location: Cell membrane
Sequence Length: 387
Sequence Mass (Da): 42713
Location Topology: Multi-pass membrane protein... |
C7Q4D7 | MQPRAPYQSTQSAAAGADAPLEQIKKLALSRPVEYGALDRLCTGGIAVIAEIDPTDPAAADLVSRFEDGRVRAIAFSAGSLTARAERMVHIRTHTHVPLLCLEPADTSHQLWQARACGADLIVLRAATLSDLALFSLVERAASIGMEALVEVRTGADLVRALRAQARGVLLRPSADAIPGTPQADLHDLLSMVPDGVVKVAECGPGGRSDLIACARNGADAVLLGARLLTCPDPGSVVADLAAMGAHPALSRRGSRTV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 258
Sequence Mass (Da): 26855
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A0A4Q3BNG7 | MNTIIILSCLGLVTMFTGVYHLRKLILPLVVAGLLAGLAANYFSWNTDISYYNNMLHFDNYAVAFTGLLIAVSIVVFFVSDQQYRADGSNVADIYALILFTLVGGIIMVSYSNLTMLFIGIEALSIPLYVLAGSKKLNLESNEASLKYFLMGSFSTGFLLFGIALMYGTTGSFDLLVIKNYVVNNADALPLIFKAGLFLMMIGLLFKVSAVPFHFWAPDVYSGSPTLVTTFMATVVKTAGFAAIFRLFYICFGAILHEWFYTIWAVTALTITVGNLSAIRQTSVKRMLAYSSISNAGFLLMGVLALNENAASAMLYYTAA... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
A0A4Q3BYC9 | MDSDATKQVYDILAKAAQICVEQDITVAVLCPGSRSAPVALSFLRNKNIKSYILPDERSAAYTALGLAKALQKPVILVCTSGTAALNFAPAIAEAFFSEIPLLVLTADRPQEWLGQADNQAIYQQNLYGKHVKQSYTFPLDLEHADSQWFALRQLNEAINFSTQKPAGPVHINIPLREPLYLTGTESFLPKEIPYKVTKLAKTKAFLDDSIYAELKKFKRIICIAGMNLPDENLQEIISENTAKYLVFIADITSNLHDTKNSLLYAELVLDNEAFTDEFSPDLIISFGGPIVSKTIKQFLRKSNAKHWHVGFSPAAADTF... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A3S0CSU6 | MDDESQGPKPVIVDATAPVEQPDTQQSADPNATTNSVETEAPAPESEEEQNKKEGIKGIFSTIAILVIAPLIALSLTLFVFQSYEVDGPSMETTLQDNDRLIVYKLPKTVARLTGRDYLPKRTDIIIFTRNEGMGSRQLVKRVIALPGERVVLKNGVMTVYNNKKPEGFQPDKVFPYGKVITTTAGDVDVVVPEDSVFVCGDNRPQSLDSRAFGPVPLKDITGKLSLRVYPFGNGQKF | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 238
Sequence Mass (Da): 26084
Location Topology: Single-pass type II membrane protein
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W9GL13 | MSTPPTRPTASGLPLADLSTRLGLRTPPADVRVTGVTLDSRAVRPGDLYAALPGFNVHGARFASDAVRAGAVAVLTDPDGAALLTGNDAPVLVVEHPREVLGAVAAAVYGNPADELTMVGITGTNGKTTTAYLIESALRAHRVRTGLIGTVETRIGDERIPSVRTTPESPELHALLATMRERGVEACVMEVSSHALALHRVDGVVYDVALFTNLSQDHLDFHGSMEDYFAAKAQLFTPARARRGVVCVDDEWGRRLAAEADIPVATFSTTGVAADWTARSAGADVRLRCEADGTELHLVSHLPGSFNIANTCLAGLALLS... | 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... |
A0A2N1W4H3 | MTNGFSETTYWIIFAAVMASYALVVMVFKLKKEHPVRDWAQAVFEAMLIATFLRITVVQTFAIPTPSMENTMLVGDHPVAMKFYYGYYNPFTDKLIFDINKPKRNEVVIMRDPTNRTNEMWIKRCVAVAGDTVEIKDKKLYVNNIRQEEAYVVHASPLSISGFFSPRDNFPLTTIPEGHIFVMGDNRDNSYDSRFWGPLPLKKVRGKAVFVYWPLNRIKAIN | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 25647
Location Topology: Single-pass type II membrane protein
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A0A951NUH9 | MAEQALYRKYRSADFSQVLGQDHIVTTLVSAIANDRLSHAYLFTGPRGTGKTSVARLLARALNCTGTGMRPCNECANCKAIINSSLDVVEIDAASNRSIDSIRDLREKVALAPAIGRHKIYIIDEVHMLTSEAFNALLKTLEEPPAHAVFILATTEAHKVPETIISRTQRFSFRPIPTPEIVKHLVDIAAGEKVEVEPAALELIAVGARGGFRDAISAFDQVASSGQRPVTVEVVRTLLGYSDGELIGTVSRAIATSDARAAVVGLADLVAGGAQPGQLAIQLIEQWRAIMLAATGASEPTPGVVAELAAIVSPARAAMV... | 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: 503
Seq... |
A0A090RW10 | MSKRLLKSGMIVSAMTLVSRVLGLVRDVVVANLMGAGASADVFFFANKIPNFLRRLFAEGAFSQAFVPVLTEYHASGDKDKTRELIAKASGTLGVIVTIVTLLGILGSSVVTALFGFGWFLDWLNDGPAAPKFELASLMLKITFPYLWFITFVALSGAILNTLGKFAVSSFTPVFLNVMIIGSAWFISPNLAQPEIGLAIGVFLGGFVQFAFQIPFLIKEGVLVKPKWGWRDPGVTKIRTLMIPALFGVSVSQINLLFDTFIASFLATGSISWLYYSDRLLEFPLGLFGIAIATVILPALSRKHVDAHSEGFAHTMDWGV... | 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 inner membrane
Sequence Length: 392
Sequence Mass (Da): 42754
Location... |
A0A2N1W4K7 | MVNDFLLKTWERLKSFWQGQDKSRRILWITVPSLILIGLIAIAFWTTAPNYSPLFSNLTSEDAGNIISELKDRKIPYKIGNNGKTISVPFKNVYDLRLEMASKGMIKGGGVGFEIFDKTNLGITDFTQRVNFVRALEGELGRTIGNIDIIEDARVHLVLPKKELYEEKEKEPTASVLIKMKSGLKLSYDNVKSIIFLVAGSVEGMKPVNVTIIDSNGIVLSDIIKDELMEEGSASYSYSKQLKLTNQQITMQKEFEKDIQRRVDSMLSNVLGDKRATVRVNAELNFDQVEKKDEIYEPIVGGKGIIRSSKRNLENYTGVG... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 537
Sequence Mass (Da): 60032
Location Topology: Multi-pass membrane protein
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A0A3S2UTJ3 | MPDLGAYAVEVLSAYAVSLSLIVGIVLLTALRGRRVKRQLEEMERRRG | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 48
Sequence Mass (Da): 5357
Location Topology: Single-pass membrane protein
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A0A6H2DIK6 | MTEAFSPEFGESWNENQCRSMLSLPGTKLILAQTNQDYCGFIISRTVLDEEELLMIAVSPGYQKKGLGRILLKKLIENARNRGITSIFLEVRSTNKAQILYGKFGFQKIGFRKAYYTGNDAQKFDAISYRLDL | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 133
Sequence Mass (Da): 15143
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A0A1Y0IM93 | MKAKSQDLMAGKGQKLTSRIITGVMVGVVVSVLFFLWGDVREVKDVIFSISWYTYVLAVVTTLASYFVRFFKWQFFLQVLGIKVPWKESLNIHFIGLSMSITPGKLGELLKSYLLKNTAGVEMARSAPAVFTDRLTDLFAMLCLVGVGISLFAFGKLAFFIVLGGLLLITLVLQSKGISLRVIDWLARLPFLTKHKGSMLTLYESTFELLRWKPLLFATVLSVIAWFMECISLYVLIVNLDLGLTLTHVVFIFSLGTVAGALSMLPGGLGIAEGSMTGMFMYFGLAKGTAVSITLLIRLVTLWLGVLIGIVIFFLKRKVY... | 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... |
A0A1G2VP28 | MISFLRGKVIELGKTYIILDVNGVGYSVYLPTKAIDSLSDINNEVKEIGVYTQMFFNQREGTSRLYGFLKKEDLGTFDLLTSISGIGPKNAMHILSSIEIGELVAAVSKEDEGYLRKVSGLGPKTAKRLIVELKDIAKKPEFARFLQGNVANESEAIDALISLGYQKNMAIEAIRKISSKKKDVEEIVKEALKALSKK | 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 ... |
A0A1Z1WHW9 | MKIHKYDTVIVGAGGAGMRAAIEATKRSRTAVLTKLYPTRSHTGAAQGGMAAALANVEEDNWEWHTFDTIKGGDYLVDQDAAEILAKEAIDAVLDLEKMGLPFGRTPEGQIDQRRFGGHSRNHGEAPVRRSCYSGDRTGHMILQTLYQNCIKEGVEFFNEFYVLDQLIVEEDGVRKSAGVVAYELATGEIHVFQAKAVIYASGGTGKFFKVTSNAHTLTGDGQAACYRRGLPLEDMEFFQFHPTGIWRMGILLTEGARGEGGILRNKDGERFMEKYAPVMKDLASRDVVSRSIYTEIREGRGCGPEGDHVYLDLTHLPPE... | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.
EC: 1.3.5.1
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Sequence Length: 584
Sequence Mass (Da): 64846
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A0A9D3M4C3 | MELGESAESSQKEGRSPPPPHPRRTARWKQSKGRRRARRRARGGHRNIRGLAVLSTTACLSMDTPTKEGPPAAPSLRGFLESPLRYLDTPTKSLLDTPIKTDEDFPSCDCVEHIVEKDEGPYYNHLGSGPTVASIRELMESRYGEKGEAIRIEKVVYTGKEGKSSQGCPIAKWVIRRASEAEKLLCLVRPRVGHRCANAIIIILILAWEGVPRALGDKLYRDITDTLTKFGNATSRRCGLNDDRTCACQGKDPNKCGASFSFGCSWSMYFNGCKYARSKTPRKFRLQGDHPKDEENLRDNLQNLATGVAPLYKQLAPQAY... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development.
EC: 1.14.11.80
Catalytic Activity: 2-oxoglutarate... |
A0A1Z1W4A6 | MAETVRDAGGALKVAVVGTGGVGGYFGGRLAQAGHDVGFVARGAHLQALRREGLTVESPAGGFTVAPARASDDTHGFGVVDVVLLCVKTWQLPPAVAALKPLVGPDTAVVTLQNGVEAPEQVAQEVGRDAVLPGTAKILAHLDGPGRVRHVGGPGTLAFAEWDDRATPRVERLRAALPGAGVSVTVPDDIWAELWAKFLFVVPFGGLGTVTDAPFGVLRSRPGTRRLLAEGMTEIERVARAMDVRLPDDIVPRTLDFVDQQPAEGTSSLHRDIRSGRPSELEAWNGSVVRLGARTGTPTPVNGYFYEVASVLAATRAGEP... | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 326
Sequen... |
A0A1G7C048 | MSNVKNITVKADDDGIRIDRWFKRHFPEVPFGTLQKKMRKGEIRLDGKRVKGPERVEEGQVVRVPPLGEMPEPPKREPKPRLSDKDIKEVQSWVLYKDDHVIAINKPAGLPTQGGTGQTRHLDGLLDALRFGSEHRPRLVHRLDKDTSGVLLLGRTPNAAAALANAFKTKETDKRYWALVIGCPNPRDGRIILNMSKAPIKGNERMVADPNGQHSLTDYAVVDNAGQQAAWVALKPHTGRTHQLRLHCMEMGHPIVGDGKYGGGDAFLSGAISKKLHLHSHTVRFPHPAGGRASVKAPLSPHMAESFNMLGFEVGEYEDP... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 324
Sequence Mass (Da): 35904
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A0A2H0VZV9 | MNEVTIPQQDFDITLNEVDELLNQKDYDTLEANLVQCDVSLLVDIIDGIIDGRKKIFSLLPPERQANLILKLSENSQDEILSALSNEALARIIRFMEDDNATDLIQLLPSDRTEGILAALSPRKRTRVSQLLKFDPDTAGGIMDMYFIQVKPSETVEAVRKKVHEYQKEHGGFPRVLIEDAQGNIAGYAPTRKLIGEPGKTEIARLSRPAIYVSYDEDQEVVLNKALEHNFTGIVVTDEQNKVVGVIRQQDFLKVAQEEATEDILHLSGLSKEENLLDSPLLALRRRYGWLLIHLIMTSMAASLVTLFHGTLAGFVILAA... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 451
Sequence Mass (Da): 49955
Location Topology: Multi-pass membrane protein
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A0A173TPY0 | MRCIFAPAQERGGTVLTQALKGRKLLLVGFTLFSMFFGAGNLIFPPDLGAKAGTNFWPAFLGLAISAVGLPVAGVIAVARADGLDKLAGRVHPVFAQVFMILIYLSIGPCLAIPRTASTSFAMLTPLLGSSAGLQLGYSVLFFSAAFLVALHPDRLTRWLGRLLCPCLLVLILILFGGCLLHPLAAQYAAPTETYRSTVVLQGVLYGYQTMDALAALNFGAVIAMNIRAQGVAREQDVQRSAIRAGFVAGGLLLAVYTMLGHAGALTGAAVPGLATGAEVLTVLAERLFGKAGLVLLAAIFMLACFNTCVGLIACVGEYF... | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 441
Sequence Mass (Da): 45948
Location Topology: Multi-pass membrane protein
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A0A9D3RW01 | MGWIDNFNGPSGVFIAAGKGILRTMRANNDAVADLIPVDTVVNLTLAAGWYTAVHRPKSALVYNCTTGGINPFHWGEIEHHVMSTFKRNPLEQAFRRPNANITSNYLIYQYWILVSHKFPALIYDLFLRLSGQKPQMMRIFNRLHKAIALLEYFSSQDWEWNSDNMSMLLSQLSPEDRKTFNFDVRQLNWPEYIENYCIGTKKYVLNEDMADIPAARQHLRKLRNIRYTFNTLLLVFVWRVFIARSQMARNIWYFVSFP | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Catalytic Activity: 2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) + octadecan-1-ol
EC: 1.2.1.84
Subcellular Location: Peroxisome membrane
Sequence Length: 259
Sequence Mass (Da): 30353
Location Topology: Single-pass membrane protein
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A0A2H0W2S6 | MKVLFAGGGTLGSVNPLIALWQELQLRESSLQALWLGTTSGPEQEVVESYGINYRAISTGKLRRYFSWRNVIDPFKVLWGYIQSRKIIKNFKPDIVISAGGFVAVPVVWAAHAKKVPSLIHQQDKQVGLANKLMAKKATRISVTFEASINEIKKFKDKIEIIGNPVRQEFFQVEFEASKKYFHLTHDLPVVLILGGGTGASTINQAVYDSLPNLTKFSQIIHLTGRGRGRSDGSYQNYYPYELLVQEFPKALAAADVVVSRAGMSTITEAAILKKPLVLIPMPDSHQELNAQELQKNNAAKVLAEKNLSPASLVTALKSV... | 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... |
A0A024HH81 | MLQKIKTRLPLEKLRFDPRLSLLGLAGGAALLALGSTWYLWRDQGAFHPLYGAGEAFPAAEVMQVLDAEGVAYRLHPQSGQVLVRDDQLAHVRMLLAAKGVKVAVPAGYELFDKDEPLGTSQFVQDVRLKRSLEGELARTVMTLEGVQQARVHLALEQDSSFVVSQRDPAKASVMLQLAPGYKLKPDQVAAVVNLVANSVPQLQPESVSVVDQHGVLLSRGLSAWGGSQENGQLVDDFQQKAVANVEQVLAPILGAGNYRVSVAADIDFSQAEETRQTYGDNPRLRRETTRDDRTLDELALGVPGSLSNLAPAKPNDPQQ... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 569
Sequence Mass (Da): 61310
Location Topology: Multi-pass membrane protein
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A0A9D3M3T1 | MILIIMGVSGSGKSTVGSLLSEKLGWTLYEGDDYHPKENIEKMASGIPLTDQDRTPWLLLLHDIIQREMAAGTNAILVCSALKKLYRQLLLFGRCALDAGRG | Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 102
Sequence Mass (Da): 11189
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A0A3D4ITD9 | MTQISRDDVVHLATLSNLQLEESEIESLRADIEKILEYVEQLNELDTEGLEPTYQVTDLENVWRDDSPKQDAADREALLALAPEAQNNSVKVPKVL | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A8A1MDG1 | MAPKIPPPDRKEKLTLSQLASYDDVITDALVDRAYFWTKIRKNRTKYISCRGILEEQVTAILLHDVIVGKDVPKAEKALLAIPGLKKFVDRLKSDREKEWFRRHLRKYISIYLPDCPFEVMTTNRYTITIHEAAVSARKYIASGTTIRGLSGTLVPMTREEEIDLDLTRKDFSIVMSSRKKTPSIFLGPARFANHDCNANARLVMRGPESMEVVAIRDIVVGEEITVSYGENYFGEDNCECLCHTCELALRNGWSPNGALISSRTNSGASTPLELCEGRDPSTLSSPSSPGSSNNNRKRKRNSELQLLSAESSTPCRRRK... | Function: Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Catalytic Activity: L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.372
Subcellular Location: Nucleus
Sequence Length:... |
A0A975LM57 | MRVRISPSFLKGQIKIPPSKSYSHRAIICAALSNGKSIISNIQFSDDVLATINALKAIDAKIEVLDDKLIIHGVDEIVLKDKIVDCNESGSTLRFIIPILALSGERFLINGKESLLTRPLGIYEDIINDLSGTFLKKNSMIEVQCDFVSKEYHIPGNISSQFISGLLFILPLLKGDSKIIIKDKFESKNYVLMTMHILKKFGIEIKIEENVIKIKGEQKYKPSDYYVEGDYSQLAFFAVAGVLNGDISCLGMNHNSLQGDIAIIKTLKEMGAKLDIIENGFIFKKSLTLGKEIDITQTPDLGPILALLASLSVGVTIIKG... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A388QJB3 | MSQVRFAIPKGSLEEATFKILERSWTKVNRESRTYRVYLDDPNIVVKMLRPQEIPTLVSEGLYDVGITGKDWVGETNADVEAILDLEYGKLD | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
EC: 2.4.2.17
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Length: 92
Sequence Mass (Da): 10519
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A0A955K202 | MDEAGRFSNFYETDSRPPKEYGSFRGDHQPKGNKMKISLNLIQYINQHYNCGVDPYTYGVDEILQRIGAQLGAVEDVKYFGKKYDGVVVARVVSCVKHDNSDHLNVCVVDDGGVVNEVERNKDGYVQVVCGAPNVREGLTVAWIPPGAVVPSTVDKDPFTLTVREIRGKVSNGMLASPAELGISDDHDGILEINVEDVGEDLILPGTPFKQLYGLDDVIIDLENKMFTHRPDCFGTLGVAREIAGIFSDSFISPEWYKNVLVNEQTTELSMSVDNQISELVPRFMMQAVADAEVKPSPMWLQSYLTRVGQKSINNIVDYS... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 884
Sequence Mass (Da): 98687
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A0A955K626 | MTFYFYDLETSGVNPREQRIMQFAGQRTNDKLEPIGDIDNVLIKLTEDVLPDPWAILTHKIPPQQTLAEGLTERDFLAWFQSDIATPDTVFVGYNNIRFDDEFIRYLHYRNFADAYEWHWKDNRSRWDLLDVGRMVRALRPDGIKWPYNSDGQPAAKLEMITSVNKISHQDAHTADADVKATLGFAQLIFEHQPKMFNYLLEMRDKNKIAKLLSEDLPFVYTSGRYSSDHLKTTVVIPVGNHPAQPGTMIVYDLRFDPTELRHLTTEEMAKRIFPPYGSDVPRLPAKALTLNKCPAVAPLTVLDKQSQERLAIDLDQVNN... | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 473
Sequence Mass (Da): 54528
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A0A955FBH7 | MIEVHMDDVPASYANAGVDVHAGDVMSQIWNNEGEKTYGNRTGRLGEVIVYGSGFTSTRAIDLDQIQGQFGLGLLSGVDGVGTKPEIAERATEARRRWLSDEVEERGRDHRGISFDTTAMVTDDLARDGGEPIAIDLLFDASSLNHEDAEAITRELAAGAVEACMAAGVILQNGETAELGDRVGGYEGAFHYNLGGFVIGAVHRDRIITGADVRPGQRIVAIQEDGFRANGISLVRKVLAAQFGSQWHMTRPDLAASALTPSKIYSQAMVEMHGGYDLSREPGAHVSAIAHITGGGIPGKLQRKLAASGHGAVLEDLFAP... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + AD... |
A0A7C6RR77 | ITDNNYIREINKEYRNIDAPTDVISFALEDNMEYNLPMFRVLGDIYISIDKVKSQALEFGHSELREFAFLTIHGLLHLLGYDHMDENEEKIMFSLQEVILNEYGIKREK | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 109
Sequence Mass (Da): 12887
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A0A4Q3C2X8 | MRLQQYPAHHTIAWRPGSSTLIEQSVVKQWYARPTWLWVFLPLVPLFSLLRVLRRCYLQARRQKLPVPVAIIGNISVGGTGKPPSLWL | 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... |
A0A1F8N863 | MRAIQKKPHSSIMVGIGLLKSGSADAFVSAGNTGAVVGGSLLTLGKLNGVSRPAIACFLDILASKPALLLDAGANADCRPEHLVEFARLGSVYSKSLLGIASPRVGLLCNGAEEGKGNRLAQETYTLLKTTAGINFFGNIEGHDIVKKTVDVIVTDGFTGNIVLKTIEGFSDSFLNSVKQIGRVFSSASRLRGRELLRDIGLTSWLKKMDYTEYGGASLLGVNGTVIIAHGRSQARAIKNAIGLAKETIEHATMEKFREEHYEQTGRDSRS | 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-... |
A0A7S8HCU2 | MSRQSRKARRQAADAALPLTPEETAALFAPFTGTGHLALAVSGGPDSTALMLLAARWRAALAEAERPRVTVLSVDHGLRPEASGECRTVAGWADRCGLSHETLRWTGAKPASGIQAAAREARYALMTDWCRAHGASLLATAHTLEDQAETVLMRLARGSGIDGLAAMAAETGRGGLTLARPLLEVARARLRATLEVAGHPWIEDPSNDDETFERVRVRKALPGLAALGLTPEALARTARRARKAADALDAVAADTLSQAAVLWDGGFCTLDREALLRAEPDIAQRMMQALLVAVGGLAHPPAHDALAGLAEWAGGAEAGA... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A917ZFA8 | MAGPTTSDVAGEGRKAGTGNTGGAQDAPRRRPRLTAAIARRRRLLAVLVPLTVLVGGGTWAVYGTSLLEVRDVAVSGTRVLDPAEVRGAAAVPLGGPLADVDTSAVERRLRERLPRIESVEADRSWPHTLRLVVTERRPVAVVRHGSGYSEVDRTGVRFAHVSRAPKGAPLVELKLDEPGSPPSPSLRHFGTQRLLRAAVVVASAMPEAVRGQATSLEVRSYDDIRLTLTGERTVVWGSAELGSEKGKVLTSLLKAVPGARHYDVSAPSAPAAGN | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 275
Sequence Mass (Da): 29023
Location Topology: Single-pass type II membrane protein
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C7QH82 | MTPPDRPASPSRVFARLKRIERRHVAAVLRTETVGGALLIAFALLGLLWANSPWRASYDTVKNTVVGPHLWHLDLSLADWAADFLLAFFFLVAGIELKHELQAGELSNPRAAALPVVSALCGMIVPIGVYLAVSAGHTNAGEGWAVPTATDIAFALAVLAVVGQNLPSALRAFLLTLAVVDDLGAIIIIAIAYTDSIDTGALVIAAVLLLAFYVVQRMRITSLWLNVPLGLAIWIAVHASGVHATVAGVAIGLMLRGRRHGDSDEDHDDELQSPAEKVQWRLQPFSAGFCVPVFAIMSAGVYVGGKTLGSLVSDQIPLAI... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Subcellular Location: Cell inner membrane
Sequence Length: 433
Sequence Mass (Da): 45948
Location Topology: Multi-pass membrane protein
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A0A955GA00 | MTDQLNTPRLPIDTTKNSILTEPLVDSFGRKHTDMRFSITERCNFRCTYCMREDQRFNPSSLDLTPDEILRIASIAHGLGIRAVRITGGEPLMRKDVVSIVKKLKNVGFDELTMTTNASLLSHTSRGVTMAQNLKDAGLDRLNVSCDSLNPERFKKIRRRGTLQGVTNGLQAAYEAGFEEIKMNVVVIRGINDDEILDFAQFARMSSILGRECIVRFIEHMPLGETGDEQTSWTPDKVVPAEEIVNLIDSKWPIKIANHQGDHAPASRWSFDDGFGEIGVIPTMTNRFCGDCNRLRVTSDGTVVSCLFSPKEARFRLRDK... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 379
Sequence Mass (Da): 42070
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A0A0M2U3R9 | MDKLTVPAYAKVNLVLDVLGLRPDGYHEVNMVMQAVAMADLVTVFRRSEGITLSSDRPDLPVGDDNLAFRAARLLLEHTGTSAGLHIHITKRIPVAAGLAGGSTDAAAVLLAANYLLELGLTNARLVQLGAKLGADVPFCLLGGTVRATGIGERLSLLPAAPLLWLVLVKPDFGVSTRDVYRWFDQQPVSRRPDTGQAIRALEDRDAEGLISAMGNVLEPVTATRHPEVAVIIDELVALGARRAVMCGSGPTVFGIAFDRQHAEAMAAAFRPRYKEVFVTHTI | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A0S8FLF0 | MSALLTVEQADEHIRAATANFGVEEIPVSDTAGRILRQPVRAERDLPPFDRVMMDGIALRHAAWADGQRAFRTEGIAAAGSPAMSLVSEDGCIEVMTGAVMPDGTDCVIPVERIDQSDGVAEVHSDYSPEPGQFIHRQGSDHPADTVLLEPGMRLGGPEAAVAAAAGLSVLKVGRMPSIGVISVGDELVEPGDPILPHQVRRSNDYAIEVAIRARRAGSVKRLFIEDDREQMLERIGACLEDADALVLSGGVSMGKFDFVPAVLDTLGIERVFHKVSQRPGRPMWFGRSAAGQPVFALPGNPVSAAVCLSRYVLPSLERG... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 402
Sequence Mass (Da):... |
A0A1G6PDF9 | MDNQSALAVREALWMALQLAGPPLIAMLAVGLVISVFQALTQIQEATLAFLPKLVVLGVVLLLLGPSMVGSMRGYAASLFDRMVAVGGQP | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 90
Sequence Mass (Da): 9421
Location Topology: Multi-pass membrane protein
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A0A2N1W5V5 | MKLIAGLGNKGTEYKGTRHNVGFMFADFLASKLGFSFTEKNKYAAYATKSIRGVSVLFIKPLTYMNLSGEAVKFFADKHKISPEDILICHDDMDLPLFTVKLKNGGGDGGHNGIKSITENLATDKYPRIRFGVGRPEKKSMVVDYVLGPFTDDDTKEFEKKFDNLQDFVHNFASLGYEKSAGRFKDV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 187
Sequence Mass (Da): 20897
|
A0A7W4EAS6 | MRMTQPRRAQNNQLPTFLDHARELQWRLMVVVGFFLLAGALAYPFFNDIVRILLRPLGKAHELVYLTPGGAFAFVVQTCLYVGLIGAFPAIIYHLYRFIQPAVGKASYKRVVGYTAASVLLAIAGVLFGYFVTLPAALQFLTGMNLDHINPMLTVESYISFVMAYLLIGALLFQVPLFMLMINFVRPFPPGGLMKGQKVVLVGAFVIAAVVSPTADPTNQVLLALPMILMYQVGVVWVYWVNRRARLAGRAQPVYRGARQEARETGDEDEDMSEIAAIAQSRAVATRPRMRAAVSSIGKATDARGATVRPRQGGVMRAKK... | Function: 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.
Subcellular Location: Cell membrane
Sequence Length: 423
Sequence Mass (Da): 46477
Location Topology: Multi-pass membrane protein... |
A0A410WSF5 | MTMLLLACLFTLIIHAAETSAYAFRLAGIRTAKLAVALSLAGMIVLISRTSNMVQGLMISGIADKAGQSDPHLALAPFRFVLMSASVGTAIAIVLFPTLVSLSARLIAHFEVTGSIPSLLKATANVHGIKQAGKHLRPPRLQMLSRLRIGGVPKRLVLLNVIVTAIYTVGVLAALYASAYSPDNKSQATMSSALINGIATIIMTLLIDPKVGLLTDRAMHGKASQEAVNKMFGLLMLSRLAGTILAQALLVPATSFILWALTLF | 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: 264
Sequence Mass (Da): 27926
Location Topol... |
K7ABV0 | MVLFTALIGYGLGVSQLIFVEIFCFLFGTLLTAMGANGLNQWWERKRDALMLRTRKRPIPSGRLSSGHALTVTLVWSLTGMLLLYYGVNSLTACLALITLTSYVLIYTPLKPYSTVAILAGAIPGAIPPMMGWTAATNHFGVEAWVLGCLLFLWQIPHFMSLAAIYRQDYAKGGYQLLPDNPEIEGVTRSIIVIFSVALLCVTLLTPFVGLGQKTFFLGAFLFGLALLIVSIRLYQQYSVKNARQVFLASIMYLPALMTLLLIDERFVSHYWSF | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
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