ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A520TU91 | MMIYLFIGLGGALGASLRFYFSSYFSQFIFFGIPLGTILVNVLGCFAIGFFIANQEEGNSLFLNNFLAIGFLGSFTTFSAFTKEALIFYQSDSFFTFSIYIFFTLILCLFSTYLGFKIFYNG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 122
Sequence Mass (Da): 13774
Location Topology: Multi-pass membrane protein
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A0A3M1DXG2 | MTALLVSDLHLDEARPEKLALFLRLLERARACRELYILGDLFQLWLGDDDLRPPHPEILQGLRGLSEVGVRVRVQRGNHDFLMGRGFCRATGARLLPDEARVELAGVPALLMHGDTLCTLDREYQRFRRFTRIRPLQPLFTAMPLAWRLRKAASIRDQAMTRGRNKAPELMDVTREAVAGAMRRHGVRLLVHGHTHLPAVHRFELDGAPARRIVLGDWFGNENVLVCDEGGQRLLPLGEFL | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
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 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A9K3D5G5 | MAISTLVGIPAGVYSTFVIEAKYGFNKTTPLTYVLDTVKGLVLTVLLGGPIFALIIKIFDSVDYAWLYAFGALSVIQVVLMYLAPVLILPMFNSFTPLPEGELRTRIEALASSQQYGISGIYVIDGSKRSTKSNAYFTGLGHTKRIALYDTLIDKHSVDEVVAILAHEIGHCKLGHIRKGIAMSMGSSLMMLYFLSQCTEREGMYQAFGVEGTPLYCGLVLFGFLYAPIGMLLGPLSSWVSRRHEYQADAYAAQATGAPLDLASGLKRLSVDSLANLTPHPLKVWLEYSHPPVLQRISALEAISQQDTRKTQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Proteolytically removes the C-terminal three residues of farnesylated proteins.
EC: 3.4.24.84
Catalytic Activity: The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal r... |
A0A973DLS6 | IWGDIELFAHFVQAPVIAITGSNGKTTVTTLLGEMAKKANVNAAIGGNIGIPVLDIVSDPSIELFILELSSFQLETTYQLNLQGATILNLSDDHLDRYDGFGGYVAAKQRIFLHCATAIVNRQDNLTMPAVSVVKNHLSFGLDAPTGETQYGIKDDALFVGQQLLISTRDIAMLGQHNYLNAMAAIALGTVAGIALKPMLETLKTFSGLEHRCQQISTKTGVRWLNDSKATNVGATLAALEGLAGHQGKLLLIVGGDAKGADVSALQQPFIDHVDTLITIGRDRQLFNDIYPNAISCSDLTSAVLAAKQASEPGDIVLLS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A9K3D291 | VSGSDMAKIEEQLGKDVTERFDFVFSENGLVAFKGQHLIGKESIVSFLGEDSLQEFTNDALLLVARTKLPFKRGTFIEMRTGMVNVCPCGRQVSQAERDSFAEYDKKHRVRQHMVKELDRKWGPKGLGFGIGGQISFDVMPQGWDKTFVLRFLHDYRTIHFFGDKTRPGGNDAEICDHARTEGHSVVSPQDTLAQVKKLFPGV | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic Activity: alpha-D-ma... |
A0A661EF78 | MPKIIVKDVCYNLLQQSLDIIIKKYNTTLQSSNIKIVISNPVDQNLGDYSCNVSLQLAKHLKDSPLNIAHNLIDNLPSHPMIEKIEIGGIGFINFFVSHNAKTDLIESILNLKNDYGRLKIGEGQKILLEFVSANPTGPLHVGHGRGAAFGSSLASVFKFAGFAVECEYYVNDAGRQMDILSISVWLRYLDLCGEKNINFPKNAYQGDYIWDIAATLHREYNDRFSIESNKLPKFDSNSDDIESQMDELIFFCKDFLQTRNFDIVFQTALKTILNDIKKDLSLFGVEYNNWFSEKILFAGNHIDKIIKKLNINKRTYKKD... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 591
Sequence Mass (Da): 67945
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A0A967C012 | MMFQILDPDGAFIGPDPNLSDELLTDMYRHMVLARRFDRKAVALQRQGRMGTYAPLEGEEAAQVASALALGPNDWVYPSYREHGTQLVRGVPISTLLAYWRGLPNVEWDPYRYRVQMDAVPIASHLPHAVGHAYQARRDGTDAVTIAYFGDGATSASDFHAALNASGVWKTPNVFFCRNNLYAISVPLDKQTASIALADKAIAYGINGMRVDGMDPLAVYVATDEAVRRARNGEGPTLIEAITYRFGPHGTADDPRRYRSEEEEQEWRAKDSIPRLRTHLTGLGLWDDVREAELIDGIDRRLDAAVAQIEAIPLPSRDEV... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + ... |
A0A2D5ZZ48 | MSSKSKKIFVLGATGMLGHKMCQVLSGADEFYVYGGLRGRAEAVKALPFFQDTDLVGGLDVNDWGRAKDSIANLKPDVIVNCVGLTTRKIDPAASAQVVELNALLPHRLAHLATDLGARMIHFSTDCVFQGGAGPYAVDHPKDAQDLYGMSKALGEVDAPGCLTIRSSIVGREIRGFTEFFEWIFSQKGQGVSGFTKALYNGLTTKFMAELVRDLILQSPDMRGILQIGSQPASKAQLIQQVSDIFDLGITVNSVDQGKDKTLQTQVAQQDIGFQPPTWAELISDLKRENHLYEGIQS | 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: 298
Sequence Mass (Da): 32378
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A0A6N9BXZ5 | MAHGPRRGDHGRTHHRGHVTALLVLVLVAPLSGSEFLNPETRALQDDPFENPGYLWVDRGAALWSEAGCERCHALSEVAASDFPRYDATSAALIDLSGRVNRCRSLDGAPTWDHDDEPLLALTAFLLNRDRGAAIEPVSDPRAEPFREAGETFYRRRRGQLDLSCSNCHDTLAGMRLRGERISQGHTNGFPTYRLLWGTLASTHRMFRWCNEAVRSEPYPVGSPEYVNLEYFLRHRGQGLLIETPAVRR | Cofactor: Binds 2 heme groups per subunit.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
EC: 2.8.5.2
Subcellular Location: Periplasm
Sequence Length: 249
Sequence Mass (Da): 27971
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A0A9E2VW65 | MKKIFWFALLVMSLAACVSNNVEPPAPLVPFTPGVKVERIWSTSVGSADAILRLGIVAASDSVNVYAADHGGDVYAFSLKSGKRLWRTETKLPLSGGPGAGAGLVVVGASDGTVVALNAADGSQVWKATVNGAVLASPAVSPQAVIVHTSDGHIVALSLAAGQTLWSVSRDVPNLTLRGSGVPLIVGGTVLQGLATGQLLALNLSDGSQRWLATVSAATGSNELARLVDMDGVLAADDSNVFAVNYQGRVADVALDTGQILWARDMSSYTGVSADAAHVYVTDVHSAVWALDKTTGVPAWTQPAMRARDLTVPVPFGDTV... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 380
Sequence Mass (Da): 39087
Location Topology: Lipid-anchor
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A0A8T7BCC7 | DIRDPAESYSAGQFRQDALREIEAVYEAGRIPLLAGGTFLYFRALEYGWADLPEADVKIRSEIDDEGESKGWSVMHAELAIVDPAAADRIHPNDAQRIQRALEVFRITGEPLSNWQQWSKHSCPFVVTKMAIQPQSRENLSERISARFDRMIEQGFLDEVERLFTRGDLTDKLPSIRAVGYRQLWRHLAGDYDLQTAKERAVIATRQLAKRQMTWLRSEPDLAWIQGHSHAERWHSMREVLKQLQVA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A1X3PC08 | MFGRFGSVRAGALGAWVADVTRTLLPESTPVRHRRRVRGASPSSLSDRRSPSFPGSTKVGARENVSEISTKCRETACRGPGYPGPVTETSPASQTTWPHLLDALLGGEDLTAETSAWAMERLMGGELTDAEIAGFLIALRAKGETAEELVGLSSTMMAKAVEISIPGPTLDIVGTGGDRLGTVNISTMSSLVAVGAGARVVKHGNRGASTTAGAADVIEALGVDLAMSPERVAQAATEVGITFLFAQSFHPSMRYVAPARRQLGVRTIFNFLGPLSNPARVDAQALGCAHRGLAPKMAQVLAARGTRGLVFRGQDGRDKI... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A2E0Y9T8 | MFDIGFPELVLIAIVGLLVIGPERLPEALRTLGLWIGRMRRSFTNVKTEIEREIGMDEVRRQLHNEAVMEEMKRIERDVRDSVNAGAAPTPGRAAPERSSAGTPGGEAAASPSLEPAAGSRPAADAAQPSSGPQASPAKDESTGPDDDRRHG | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A8T7BL29 | MAEYFTNKLTGIILAGGKSTRMQGVDKGLTPLNGTPLVEHVIHRLQPQTTTIVINANNHITDYENFGFPIVEDRMPGHPGPLAGIAACMTQAKTEYILCVPCDAPRLPLDLGNRLYQVLTENQAELAYAHDGDRSQPLFALMHRQLLGSINDYLASDQYKVDAWYHQHQYVVCDFSDKSEDFLNINSVEELQKVADQYKISE | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A9D6ZN71 | MSSFLQTAAAFVFALGVLVSVHEYGHFWVARRLGVKILRFSLGFGKPLWLRRFGPDGTEFAVASIPLGGYVRMLDEREGPVAPEERARAFNTQSLSVRAAIVLAGPLANFAFAFVAYWMMYLAGVSGPRPIIGEVEPASIAYEAGLRSGFEITAVDGRETHTWDNMFRSSIRAVLDRRTVELTVQTTDGGSAIVRLGFAGVSLDDVTQGDFFAKVGFRPFRPEIPPVLGKVLAGEPAARAGLLAGDRVVSADGKPIDDWFHWVDYIVKHPEQPIAVVVRRGSRDVAVTVVPRLDEEKGVKRGRIGAELDRAAVPKESVPL... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 455
Sequence Mass (Da): 49477
Location Topology: Multi-pass membrane protein
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A0A2E8KTT1 | MSTFSKIILILILVFIDQISKYWILSFLELGESFNLLPFLDLTLIFNSGIAFGLLDNLGNLGSWLLYLLVSGIIIYFTYLTLKAESXTESLIMLLILSGGLGNVIDRTIYGYVVDFIHFNFNGYSFYVFNFADSLITVGAILYIWFFFIKNKDETITS | 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-, ... |
A0A2D5IED8 | MEASAATAIMSPSEFELIERYFNSVFSQGLSPGISLGIGDDAAVISPAAGQQGCICTDVLVADVHFPAAADPSDIAQRALRVNLSDLAAMGATPVCFTLGLTLPAADEEWLSHFAAGLFAAANRFDCPLVGGDTTRGPLNIAITVYGEVPVGEALRRSGAKEGDSVFVTGSLGKGRTALEALGLGKTGENTDAIEAVKGFRDIKRSDMTPGYKDFLYQCFYQPEPRLTFASAARQYINSAIDLSDGLYADLGHLARASGQAMHVDAGALPFAEAVIALTDSAQRQSAALFGGDDYEICFTAAVDSAPALELIAAESEVVI... | 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... |
A0A962XBZ1 | KPEPKPEPKPEPKPVPKPVPKPVPKPEPKPPRPTTLRQAPTPPAAPEQARTVATSTGAKTRALRIDAKQQYLAELAQRIERRKRYPKAARKRGEQGVVELRFVVQVDGQLTDITVEKSSGSKRLDEAAVRSVVSVSPVSPIPATLGQTTLSIRVPIAFRLRG | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A841L899 | MSSLPNLLTLSRILAVPLLVLLMWGRNPWEWLAAFALYSVAGLTDYLDGYLARAQGTVSKLGQFLDPIADKIMVAAVIIMLIHSGAIHGIATIAALIILLREIIVSGLREFLATLQVSVPVSQLAKWKTAAQMVALGALVLDGAADRLLPWLPALEIGLVSLWLAAALTLVTGYDYLRAGMKHMN | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 185
Sequence Mass (Da): 19941
Location Topology: Multi-pass membrane protein
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A0A952HTM0 | MNPQQDSQSKTEKPTPKKLLDAQKKGQIARSRELSTTVMMISASVGLIVFSGQIGAGIQDLLINNLQLDNNVIGDKELMIDKFASMTVSTLFVLLPFFLLMMISAFAGPLALGGWAFTMSSWQPKLNRMSLLSGFKRMFGAQGFVEMIKSLGKFVVIGLVAFIVLGIHHEKILAMSTLPVIEGMNSGLIVIGQLFLLLSFSLILIAMIDVPYQLVSHFSKLKMSIQEIREENKQTNGNPELKARVRSLQREVSQRRMLVEVAEADVVITNPTHYSVALKYDESKAGAPYVVASGVDFMALRIREVAAGNDVVIFSAPPLA... | Function: Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Subcellular Location: Cell membrane
Sequence Length: 388
Sequence Mass (Da): 42728
Location Topology: Multi-pass membrane protein
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A0A368BYM5 | MPYRMDKILVLQLPNQLNQQASVNTLSIKSLILGSSGYVGSELIRLIEMHPDYELTSVVSESHSCKKVSDVFPHLFLTKKNQIFDNFESYLNNIDAGDNIAIFSAAPHGKSALLISRVLSELSNKASEIRVVDSSADFRFSSKEEFKKIYGFDHPKPDLLKHFVSGAPELININQEKYAAHPGCFATAVSLSIAPLVNSNIVTNEFFINAVTGSTGSGKRPKENTHHPERHSNYFAYKALAHRHAPEIESHIKTRTTQNVKVNFVPCSGPFSRGIYSTCFAKLTQPFSKNEVISLYRDFYSKSIFIRIKNDPPRIKDIVS... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = ... |
A0A368D6W7 | MSLLNGEHDMSHVDGAHGMNRGISAQEAIRRLRDGEVVAIPTETVYGLAASVQHPDALASIYTLKRRPKDNPMILHGGSIEQLLPFVEGWGDAHQACADAFWPGPLTLILRASEHVPSIVTAGLDTVAIRIPNHPVALEILEHVGPLAAPSANLSGSPSATKASHVLDDFGEAVAVVDGDQAAIGLESTVVWAVDGSWRILRPGVIGADEIGQAAHVVVELSPTYEEVAQPAEADQTPLSPGTKYRHYTPKARVMWLDMSQIEAATIAPEQPRLFVVTHTEGRRSQIQALTQKHPSMLHQHADSLDELAKHLYAWFREAD... | 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... |
A0A368C421 | MTYKSDSHIRNPEDFGKVVVIYGGNSNEREISLESGQSVLSSLKKSGIDAFGWDPNQESIKYILNQDIDRAFIALHGANGEDGRIQGLLDFLNIPFTGSGMFSSAIAMSKVLSKKIFLEHNLPTPKFKVIRTLKDLKKATDIFGFPIVLKPNSEGSSLGMSKISKLNELEDAYKAATEFDDVLLAEEFIQGKEITVTILKNKTLPTIRVKTNRTFYDYFAKYKSNKTEYICPGTSDISEEKIYADIALEAFEALHCRGWGRVDFMCEKNSIPKILEINTVPGMTKKSLVPMSAQCKGINFETLCWTILETSF | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 312
Sequence Mass (Da): 34... |
A0A661EFQ0 | MLKSSFFIKSVKMKHWIKSLRIPTLIIAISSVLIGNSYAGLKIDNISITIFILSFLIAIILQIIANFANDYGDFINKTDNKDRTGDIRALQTGDISLQQMKNAIIFMSVLAVFVGLILIYVAFDKDFIKILLFVLLGFISILAALRYTLFNKPYGYRGLGDLAVFIFFGNLAIIGSFYLQTLIVDWLIFLPAWGFGAIAVSILNINNIRDYNQDKKANKKTLVVIYGIDFAKKYQLFLNIIAVLLFALSVVFIKDLLNMFIIIAIGYIFFIKPAIKLYKSQWIFLYNDYLKKQLFYLAIFSIFYSFII | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol... |
A0A962UBB1 | MRKIAISQLFLLVAGSLFWLGASWLIATRLNQAELNAMVESRQAELENKASYLAQNIESYLSHMRHVPQALGRERDVVEVLSLPLVTVTAALPSAEQRKQRWEEDDRLAHIDDYLARLAGYLKASVVYVLDASGKCVVSSNAFHKRSFVGTDYATRDYFRQALENGTGYQFAVGKVSNVPGLFFSSVIKNEGRVLGVAVVKIDVADLAPWISTTNAFLTDEYGVTVLAYDDSLELRAMPGHGVERLPAQKLSARYKRTELAPLTIGPWSEWPIESVRELNGSGQPVLIASRTIHPMLHLYTVQVADFLAGVRQGWVRTFA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 857
Sequence Mass (Da): 94342
Location Topology: Multi-pass membrane protein
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A0A357IAP8 | MRSLPLPRVTKVDIKTCRKKTSSSKKPKSSTDALSSLFIADLHLKADAPALTASAHRLLQQLAPRFENLFILGDLVEYWLGDDADDGSQASVFNALRALSDQGVSIRMMPGNRDFLFGQAFAARIGAELIQDDEIVFEDEDHRLLLLHGDTLCTDDVPYQQLRRMLRDPHWQADFLSKPIAERIAAAAQLREKSRQETHAKSAEIMDVNADSVIAVMEQYGVYDMIHGHTHRPDTHEFQINDHQARRTVLGDWRDEGARIAVLENGQLSLLQWPQDFADLD | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
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 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A368BUD3 | MEWLILSKLKLIKSKVRESVKKALLEDGYKNDLSLKLKNFNKNKIISASVTTRQKGTLSGSSWFEESFKIIDKNAKIEWYVNEGSSFKKDSKIVRIKAKSEAILSGERTALNFLQLMSGIASKASKYSKVLKNSSIELLDTRKTLPNLRYEQKYSTSLGGAKNHRFGLFDAIMLKDNHLKVFGGVSKLKNLKYKNKGDFLEIEIEKLSQIKLALKAKPDILLLDNLSIIEIKKAINIIDNNCLIEISGIKNPDDLKKYRDLKIHYISLGDLTKNIESIDFSLNIL | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 285
Sequence Mass (Da): 32373
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A0A368BYR7 | MSLKRLVRPEILDLPTINVPEALPEMIRLNANESPTSHWNDALNHSLHRYPPIRPYSIVKIIADLFEVQCDQILLSRGSTEAIDIIIRTFCNPNKDQIIISPPTFDMYKFFATSNCIKTIEIPIHGDNEFNINVKDLIKKLTDRTKIIFISSPNNPTGTSVSNDDIKYLLDAVKGRAIVVVDEAYIEFSSTKSLTREINNYNNLIILRTLSKAFSLAGIRCGAMISSSECSELLKKILPPFCFATPVIQFIKSALLSKDLQATKKQIEFLIKERERVKNELEKINCVNKIWKSDGNFLLVKFRNIDTVKNSLIDANVVVG... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 352
Sequence Mass (Da): 39838
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A0A6B1HPK1 | AEMVLVAEELTAPMMAELPIERLRGIVSLKGSRNSHGAILADALGIPTVMGAVNVPIYELENRTVVVDGHYGEVFVNPSSAVRDLYDGFQEEEEEFARELETLRDQPSITRDGHRINLWVNIGLVSEITRSLDRGAEGIGLFRTEVPFAVGDRFPTEEEQRVIYREHMEAFDPRPVTKRTLDIGGDKPLSYFPIEEENPFLGWRGIRITLDHPEIFLAQVRAMIKANDGLECILRIMLPMVSRLEQVEDARALIRRAYQEVREEGHDVKEPLIGVMIEVPGAIYLIREFARAVDFVAVGSNDLTQYMLAVDRNNSRVADL... | Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 434
Sequence Mass (Da): 48584
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A0A2E9NUX1 | MVENTEHRVPRFTEENSSNGLKTIIAMLLCASGVFLILPFTQYISGGGNDKSDIVTVDVSLPPPPPPPPEPPPPEEEIVDEPPPEMSRNVQQLSLSQMSLALNPGIGDALAGAFAFEGFGVEPDTVGDLKIFDVSDLDQPPRRLKTVLPIYPAELRRLRISGNVSLILIINTDGRAEVEKVVKATAREFTQPAIDAVEECLFETPTKDGKPVRARYEINIPFRMQ | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A2D8U2F5 | MKLSSSDIRSKFINYFQSKGHAYINSSPVIPSSDDKTLLFTNAGMVQFKDIFLGLKNSKFKSAVTSQKCMRAGGKHNDLDNVGYTNRHHTFFEMLGNFSFGDYFKERAIFYAWDFLTNELDIPEDKLWITVHKSDNDAKNIWLKKIGIDEKKLSIIDTDDNFWSMGDVGPCGPCTEIFYDYGSKYFGNPPGHGDEGERYVEIWNLVFMQFNRISKDKIIDLPKPSVDTGMGLERISAVMQNEHSNYSTDLFLPIINFITKNVDKKYHGDTSSMKVISDHIRSVSFLISEGIIPSNEGHGYVLRRIIRRMIRHAXKIELQS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6... |
A0A2E4KX10 | MTTLVDSREXSKFNNIARSYWDPEGPMRAXHQINPXRIDFVESYYPLQDAKVLDVGCGGGLATEAXARRGGLVTGIXASPEMLKTAKLHARXXXLKXTYSQSHAEAXATKHACEFDVVTCFEMIEHVPDPMQTLRALSQLVRPGGWLVISTINXTLXAXLGXVLVAEYILSWVPXGTHDYTRFXKPSEVAAGLRPEGLDVESIEGVVYQPLYQQFTRSTSTIDMNYQLAARKSE | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosy... |
A0A8T7BP09 | MKIIRGISTIRAHPPCVLSIGNFDGLHLGHQSIIKQLSSYADEHS | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 45
Sequence Mass (Da): 4942
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A0A8T7DIP7 | MIRWLIGSLIAVLAGTLIALAVLRDNGYILIGYDVWSVEGSLALFILLDVILFAVLYFTVRFFVRLWQTPSTVKTWHHQRQIRLAQKSLTRGLLEMAEGDWKGAEKRLLKHAANAETPLLNYLAAARAAQLQGEHERRDQYLQLAHESMPSADIAVGLTQAELQLAHQQMEQALATLKHLKSIAPKHVYVLKLLSELYQQLGDWQQLRDLLPELKRRKACSPSELEQLESRIHLFSLQQAAGKDLPALENAWKQVPRKKRFQTSLVIEYSRHLVSLNEPDKAIKEINQCLNKNRDKKWDEGVLIAYGNIDGTNPSDQLTV... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 437
Sequence Mass (Da): 49569
Location Topology: Multi-pass membrane protein
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A0A8T7CFJ4 | MQIMFKRLTLISVCLSLGACALSREETAEPPAELVEFSSEFRMEKVWSKGLGGDSSSLRLGLQPASDNARVYAGSRNGDVLALDQASGNVVWRVKSKLPLAAGPGLGQDVLALGSSDGDLIVIDKDSGEIRWQKQLSSEIVATPLVARGLVIVRTVDGFLRGLSADDGKESWQVQFEVPRLSLRGNAAPIMYGTVVIAGFDNGKVAAVSAANGAIAWQATLAQPRGRTELERLVDVDARPVQVGEDLYLAGYQGRVVLVRPASGQLIWSQDMSSFSGMAADWNRLFVTDENSEVVALERKTGIEVWRNKQLRARALTAPA... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 382
Sequence Mass (Da): 41122
Location Topology: Lipid-anchor
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A0A2E5V8Q4 | MKRLWDKDQPIDELILKYTAGNDFHLDERLIKYDIKSSIAHINMLKEMNLVKKDDCKKISEALKIIGKEHEKGEWKIELNQEDGHTALENHLVEKLGSLGGYIHLGRSRNDQVLAALRLYLKDISSIINEELINLVSKINILIDEQGEIEIPGYTHTQRGMPSSVKLWAEGYIAEFLDNAKSINNVISRADKNPLGSAAGYGTPGLNIDRDLTTKKLGFKSTHEPVTAVQLSRGKAEAEMIFELTMILGDLAKLASDIILFYSYEFSFLEIKKSITTGSSIMPQKNNPDVFELVRSAESIGIGALMEVLSISSKLISGYH... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
EC: 4.3.2.1
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Length: 395
Sequence Mass (Da): 44643
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A0A9D7IQX1 | MIGEIAAGALDRSRPLWEIWVVEGLEGGRIAYINKIHHLLADGVASVNYLAHVLYRDPAALATLEIPHFTREEEPSATRLVADALRDLLRDFAHFPTLLRDSARRRKLIEARNRSASVVPAAPYSKEIPKLRFNRALSNLRNYATAQFALDDFRKIRERLGGTINDVALGMIAGAMRRYLLAHDDLPALPLVCAIPVSADREAAAARISGNNLAYFHVRLRTDIADSRARYEATRAETAAAKEVLELLGREAAREWMQYIPPLIFSRRRQRDYRVHAADRMDFPLSGNLIVSNVPGPRETRFTARGDVCEALYSAGPLTE... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 368
Sequence Mass (Da): 41010
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A0A923P0E3 | MINLRDFACPAGTGRQRLQCLLILLGSIALATAVSAQAPDAATQASPTSAAAAAESAPATTPAGAAAASPPTVAAARPAEVRVGDTVVFALQAGHAGRSAALRARAANDALHEVLDAGDDEVRIAHAGGAAVIYVGARPVLQLVPADAALAGDASLEVHADRIAAQIRAALATEHTRSAVAGGIFGVSLAVLFAVLAVFLLRRAWQLGDRAADWLDTSAGQVPALRLGRIELFGRATVRTALSLGVAVGRWIALLGLVYAWLLATFSLFESTRSLTGQLTGALLNPLATLASRIVAAVPLLVILVFALLTLALLLRAVRL... | 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... |
B6K059 | MKAVIQRVTNASVTVNSEVVSSIAKGLCVLVGISREDTIEDVERLTKKITKLRLFEDEQGNMWKKSVEDIKGEILSVSQFTLYAQTKKGTKPDFHRSMKGEDAQVLYQQVLERLRNSLGADKVKDGVFGAMMQVQLVNSGPTTILLDTNE | Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
EC: 3.1.1.96
Subcellular Location: Cytoplasm
Sequence Length: 150
Sequence Mass (Da): 16704
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A0A3M1UVB2 | MAGAEVNQLFAIAAGGALGAVMRFGVSNAVYAWLGRGFPWGTLAVNVLGSLAMGFLYVLMIDRLAVGGEWRAFVLVGLLGAFTTFSTFSIETLTLIQDALYGRALANMLVSVLACVVAAFAGVVLARQVT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 130
Sequence Mass (Da): 13550
Location Topology: Multi-pass membrane protein
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A0A661EMS2 | MSADLLSQSEIDELLHGVGEEELETDNAYPLDGEARPFDFNSQDRIVRGNMPTLELINERFAREFRVSMFGLMRKTIEVSAAGIKVVKFSEYSQSLLVPSSLNLTHVTPLHGTSLFVIDPKLVFALVECFFGGEGRFHTKIEGRDFTNTERRVTGLVLDMIYRDLIKAWSPIAKLDFKLHNTEVNPQFAQIVTPTEVVVVSTFDVELDSGGGKLQICFPWGMLDPLREALDSTTQGDGQQLDNRWYDALAHDIREAEVDLSVVFAETEMTLRALLEVQAGDVIPIEIPPSVTLYGEGVPLFQGRYGVHDGHYALELERRF... | Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.... |
A0A2E5IAP9 | MTEEDISHLRNREITLLMGGWSSEREISLRTGKAVEDSIKSMGLKLRVIDLKSSDEISNVLDSLDLVFLALHGRGGEDGYIQKILERNNVSFTGSNSKSCKISFNKSESKKIWRDLSLPTPDFVEIKKAGTPNSETVPYLSGDEELGTLKESFVVKPAREGSSLGISIVHPGQGSLEDAMRNAIKFDDTLIVEAFIKGEEITVPIIGDKALKPISIKSKNEFYDFDAKYNRTDTEYFETNLNKEELLVVNELSLNAFLSLGCSGWGRVDLILDSKRNFQLLEINTVPGLTETSLVPKAANLEGLSFNNLVLKILNTACFK... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 321
Sequence Mass (Da): 35... |
A0A8T3Q5H0 | MNTAVRSISENRFQPTLPSIQIKRPKLINMVLIGILLLSAFSVIYIKDLNRRLFIQYQALQATHDKLYQDWGKLLLEQSTWSTQARVQKIAQYRLGMNSPSSKEIKILRR | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 110
Sequence Mass (Da): 12845
Location Topolo... |
A0A971X1R0 | MSRLVLYISLSIALHLLAVFPRLAEQFAPDAQAAALGARVEPVALALPKVRMQTAQAKPVVSEVASEAVMEAVIEQPRAPVVEPSQPKSQSKPKPQPQPVSPVAVQQPKPQPTPQAKPEVQAQVSKTFEPLRSKPEAKIEDSVAAQVEAQPDTAAVESPSTQTPTQPDAAPTTAVQATQAESVPAEIISTQPRFARAPAPPVYPAQAKRRQQQGTVWLEVRLNAQGRQLAVQVLRTSGVPSLDKAALAAVRKWQFLPEQHNGVGVPSRVHIPIEFAIAAHR | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A924V6Q7 | MKISLQWLNDYVDVTDYFKKTDELAAILTRAGLEVEEITDQAQALNHVVIGHITLKDKHPNSDKLSLCQVEVAKGVTAQIVCGAQNHKTGDKVVVALPGAVLPGNFAIKKSKIRDMESNGMLCSFKELGVDKPSEGIVILPADAPIGLPYADYAGQSDVTFELKVTPNRADCLSHYGLAREIGCLLNRPVKKIEIFSKFSNQKTTDKIKLEVNSDLCIRYSGRYMSGVKIGPSPEWLKARLESIGMNSINNVVDVTNYVMLEMGQPLHAFDADSLAKSTIQVRQAQPNEKFKTLKEQDLTFKGDELLICDGEKAVALAGV... | 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: 808
Sequence Mass (Da): 89740
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A0A2D9B2W3 | MNKKINHISIIMDGNGRWAVERGLAXSLGHRAGIKSVQTIIDAALVRQIDTLTLFAFSSENWNRPNDEITILMSLFNESITKYMHELNKNNIKVEFIGDIERFNSTLREKIHKLISLTQNNTGLNLNFAVNYGGKWDIANAVNSLIREKGHDINNPITEKDIDDYLTLSNNPPDLLIRTGGDHRLSNFMLWQHAYTELYFTDCLWPNFNEVEFDKAIKYFLNTTRKFGGLVNIDDYKSNV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in ... |
A0A850AIG4 | MAEKRFGDIGNIFPGASDREAQQLRQFCELVEAWNRRTNLISQQDAALLWERHVLPSIIPLRFVEIPPESWVLDIGSGGGFPAIPLKILRPDLQMLLVDSVRKKTLFLQKAISDLKLGKIAAANRRVEELADRAELRESFDLITARAVGAIELLLDWGKPFLKSGGRWLLWKGASDIPELEEIAPRRKLDYRVLSVPESLQSLSPKFKELRWFEISRQ | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 24880
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A0A9E2B2M1 | PHDVILFRSDVMERVRANKTLRIGTCSVRRQINTADFLRWALPACDTAPQLEFLSLRGPVDERVRHIAQDASEPLDAVVIALAGLERLWQDAEGREAIRPFLTDARWMVMPLSEAPAAAAQGALAVESRADNDVCRALLQAIHDPATEQHVQTEQGLLSEHGEAASRCGATVISHAELGYVAYVRGRSGDGSIIRQTRTANAATITHKGARRWSGTVWQQSCRKQPIPGVAERTCKTAAAVFVAHADALTGARPAATPRYWTSGPSSWRRLAEQGIWVEGCADDLGFESVRELLQTPVLQLPALEHWAALTHRDATDSWS... | Pathway: Porphyrin-containing compound metabolism.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 406
Sequence Mass (Da): 44684
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Q60CQ2 | MTEIRWFDDNTSLAPALAAAVAEDVRAALATDPAAILAVSGGRSPVPVFEALREADLDWARVIVTLVDERWVPETDPASNAALVKTHLLQGKAAAARFLPLYTGDASAAAAETRLARSFAELPRPFAALILGMGDDGHTASLFPASPNLEAGLALGGTVENTPPCLAQVGAIAPTERVSLTLPWILDARHIYLQFGGAGKVEVFNAALAGPNRQYPVSFVLAQTRTPVTVFAARS | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
Q60BB6 | MLLAGDVGATKTVLGLFDCWGDRLVSLSEAIFASTDYASLETVVAAFLDGQEERRPEVACFGVPGPVSEGRCEITNLPWVLSERELAAATGVSAVRLLNDVQAMALGMAYRLGEDDWVELNPGAGRPRSGNVAVIAAGTGLGEAILYWDGERYHALPTEGGHSDFAPNGPLEEGLLAFLRDRFCGHVSYERILSGSGLANLYDYLRHAGVAPESEALHAALASAPDRAPIIAEWALERRDALCTAVLDLFAAIYGAEAGNLALKSLALGGVILGGGIAPKILPVLQAGRFMAAFTAKGRLSPLLGRLPVRVAIHPQPALL... | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
EC: 2.7.1.2
Subcellular Location: Cytoplasm
Sequence Length: 330
Sequence Mass (Da): 34575
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A0A2E1Q664 | MKYNNILEAIGRTPLVKINHLAKDLECELYAKCEFLNPGGSVKDRIGYNMVLEAERSGRIKPGDVLIEPTSGNTGIGIALAGAVKGYRVIITLPEKMSQEKQATLAALGAEIIRTPTEAPSHSPESHIGVAQKLEKEIPNAHILDQYSNDANPDAHYHGTGAEILEDLEQKVDMVIMTTGTGGTLTGVARRIKEACPEAIVVGVDPKGSILAGDEEIKSYLVEGIGYDFIPDVLDRSLVDQWIKTEDKESFLMARKIIRHEGLLCGGSSGSAMVGALQAAKSLKKGQRAVVLLSDGIRNYMTKFLDDNWMKNNGFVE | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2.
EC: 4.2.1.22
Catalytic Activity: L-homocysteine + L-serine = H2O + L,L-cystathionine
Sequence Length: 317
Sequence Mass (Da): 34387
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A0A3D1EIH0 | MRLGFYGGTFDPIHNGHIHAALTVHEYLDAPVHLILAARPSHRVPTQSNADHRWRMLNRACDPYPQLIPNDIEMRSQKPSYTYNTLAALRTAFPERTLCWVVGQDAFATLPSWYHWEQLLDLCNIVVLQRPGFKVSEPAAMQTLLADRFVTCFTDQGVGEIVRLNTPMRAISATQVRAKITANEPIAELVCEDVDRYIKAHDLYQKEVAH | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A9K3DDG4 | MAFSLLLSGDGFLIVSLLLICICTHLRRIPKLCNLIINHKHGLRGTLYKASVIGTRLSLVVSVLCVLMGLYMLFV | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 75
Sequence Mass (Da): 8286
Location Topology: Single-pass type I membrane protein
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A0A2D5PRY7 | MKIPTNQFRTGTKILLDGAPCTILNHEFHKPGKGQAVVRIKYRNLLSGNVIEKTFKSNESVELADVAVKEMAFLYKDESKWYFMDNSTYEQIELDEKIMVDAKKWLIGEELCEIVLWNDSAIAINVPKIVSLKIETSEPGVKGDTVSGAQKPAVLETGVSIQVPLFVEEGEVVKVDTRSSEYLGRANDS | PTM: May be beta-lysylated on the epsilon-amino group of Lys-33 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC (if this protein is present). Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety may exten... |
A0A2E2ZEU4 | MEEVXKLAVIGSPISHSLSPKIHKIFAESLGIDISYEALHVEPVDFKESVRSLFQKGYTGLNVTLPLKLLASEFADNQSXESRLCGSANTLWKQGSAIYADSTDGRGLINDFQKQNVELKDKDVILLGSGGSAXAILPSLLKKNPKRISILNRSEDKALALADKFSQSQQRIQVRSXTEKLNFKPDIVINSTSASTLXQDILLPDDIFXEEAFXYDLSYSKDXTPXVEMAISSGVRXCSDGIGMLIEQAALXFEXWTSMKPKTDSXKQXIXS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A1G7LVH1 | MGINERTKSAEAFSKAQQIIPGGVNSPVRALKSVGATPLFVKEAKGAYITDIDDNKIIDFCMSWGVFILGHCNDRVNSAAIRAINTGSSYGIPTENETILAEKVREAIPSMERLRFVNSGTEATMSAIRVARGYTGRDILVKFEGNYHGHADHLLVSAGSGVANISNASSAGVPEGFTKYTAVLPYNDIDALRNYFKTNGDKVAAVILEPVACNMGVVCPSLDFLKAAREVTEQHGSLLIFDEVITGFRLSRGGAQQLFGIKPDMTTVGKIVGGGFPAAAFGGRADIMKVLAPDGPVYQAGTLSGNPVAMAAGIETLTQL... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
EC: 5.4.3.8
Subcellular Location: Cytoplasm
Sequence Length: 425
Sequence Mass (Da): 46201
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A0A2E8XE75 | MEVVILAAGKGTRMFSACPKVLHTIGGKPMLQRVVDTAFSIGASQVHVVIGFGADQIKDYFDDLQGGQNINWLLQEEQLGTGHAVQQAISSIDKEDPDNTVLVLCGDVPLIRASTLTQLLENSDQSSVSLLTLTTEHNHGFGRIVRDGENQVIAIIEEKDASAEQKEITEINSGIMAIPGTRLAGWLERLDNSNEQAEYYLTDIVALAVQDGCKINTLTISDENEVQGINDKTQLAQLETHLQMTNNSELMEKGVTLRDPARVDIRGELDCGQDVEIDVNVLFEGKVTLGNNVLVGANVIIKDSTIGDGSEILPNSNIDG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl c... |
A0A9K3D5Q2 | MFYVVAVINEETGREEPVGFFSKEKAESNLLACIMVLPNHQRCGYGHTLLDVAYHLAHKEGRVGSPEQPLSDLGKALFLSYWKRRVVQFLSTWERPDITIEDIVRGTNITPDDVTEVLVELNLMTSKNNRDVTLQFKRSVIQNLDDALDERYRGRITTIQPSKLEYVPYPQQQRRVQL | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 178
Sequence Mass (Da): 20563
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A0A1G7Q9I2 | MEIIGITGGIGSGKSVVARIFRAMNRPVYDCDSRAKAVMTECAELRRKLSEALGCEVYNSDGMINKPFLASFLFASEENVSLVNSIVHPFVKKDFLDWVQKHNTFNKVYMECAILYESGFDSLVDKVIAVTAPEYLRYERVMRRDGITSEQVRQRMEKQMDDKEKCEKADFIIHNDERNSVIKQILAIS | 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... |
A0A8T7C9P0 | MFLKSGAAAPVAKNSPPGTWIALLSGLVYPLAFAPFGIAPIAILSLAILPILWSGISPRDAAVRGFAWGFGAFLAGLYWLYISLHTFGNAPLWLSLPLMFGLVAVMALYPALAGYLYARFAPSSPGAALLLFFPGSWVLLEWIRGWFASGFPWLAAGYSQTDTVLAGYAPVGGILLVSAAVALSAGVVAGLILGGRRVLPVLVLLAVWSAAAALKPIEFSVPRQQTVRVALLQGAVPQDRKWLPEQYEPTLQRYSGMTRRSADADLVIWPEAAIPALLGYAHEFLDDLWKKARAKDTALLIGIPRRDAASGQFYNSVLAM... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A8T7BGL1 | MLPFASLTSSRQLTPDIISGLFVAIDNMATIVAEQGTSTLLQDKVVALLFFEPSSRTMLSFQSAAQRLKAGTIFAQSASTTSFEKGESLEDLIQIVNGYADIIVMRHSQPGSAEVAAQVSDAPFINAGDGGNEHPTQSIIDSYTIHKHRGRLDNLNVVFGFDSLQSRSIHSLSRLLAQYEGNRFTFTGPQELWPSSELLSELRAAGAQCDCVSEVDYRDNFDVVYVNRLQEERFADTTLFEANRRKYRITRDNIEGCDALLLDPLPRIDEIATEVDALENAVYFKQASYGVPVRMALLALLLGKINL | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Length: 307
Sequence Mass (Da): 33919
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A0A2E5V8F2 | MGVKKDYPYLKKIKIAICAGEISGDNLGSELIKDLKLLFPQAEFYGVAGPKMISQGCKAFYKVDQLSVMGLLEVLRHLPRILWLRFNLINKIKKIKPDLFIGIDAPDFNLPIGYSLKKLDIPVVQYVSPQVWAWRQSRVRKIKDSVDLMLCILPFEQSFYESNKVESLFVGHPIADQIPYEIDYNFDRKEFDINDSQKVLAILPGSRSSEIQYLAEPFIKTAQWLLNRFSNLLVLIALSDEDSLKVLLKNNKNLMSKINADDRFKIIIGKARSVISASDVVLTASGTASLEAALIKKPMVVAYIVSSISYWIFNKLGLEK... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2... |
A0A920R7S2 | MLEVAPLFEQGDYTKGLQSLSTLKNSVDDFFDNVLVMHQDDQVRQNRLALLKQLRNLFLQTADISYLHSS | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 70
Sequence Mass (Da): 8070
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A0A525C9Q8 | METHKSARVKSFIKALEQGAPHPPVRLMLNSLHPAEIAHLIESVPLTHREILWELVNSESGGEVLLHVNDEVRASLIEKMETTEIVAATENMDMDDLADFIKDLPTTVSFAVVNSLDKQDRQRLQSVLSYDEDSAGGLMNTDTITVRPDVALEVVQRYLRMQHKKIPANTDKIIVVDQADRYVGLLNITDLITHDPSQSVSEVLVTSQDGIPANLPAAQVAHLFEDRDLLSAPVIDENGKLLGRITIDDVVDVIRDEADHSIMRMAGLDEEDDMFAPVVVSTKRRAVWLGVNLVTALLASLVISFFDTALKAKYQLAILM... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 448
Sequence Mass (Da): 48230
Location Topology: Multi-pass membrane protein
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A0A972GXC5 | MIAVFGGTFDPVHFAHLKMAQAVRVALGVDELRLLPCGRPPHRVPTEASVEQRRSMLEMALEDQPGLIMDDRELSRPGPSYMVDTLASMRQQYPADPIVLIMGLDALSALHRWHHWQDLFQYAHILVLGRPGYKASENKVLSSFLSSRWSQDLADLSSHPSGRIISLDLGLIDVSSTQIRDKIAHGEDVSTLLPQTVYEYIQAQGLYT | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A3C0Q8X4 | MAVALSMPGVQRGGLSCLFDLLPLCPGATRFPRRVRLTEAADYQRVFKGRCYRLNNSWMTVLAVPNQLQHPRLGLAISRKVARNAVARNRVKRVTRESFRHWQTRLDSLDIVVLGRNGVAAQPGKVLDTALEKLWIKLIEKCAGSSSN | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A963B988 | ERADIQDLFDAWIDALEAEQLELDGKPDPYVLLEVARRLEVEPVRTAVIEDSVIGVTACKRGRFGLIIGFDNGDRREMMLEHGADLVLKDLCSVDVDGAAEDELLPADLVDSKLITNQLAGKRPVLFLDYGGTLAPATDRFEDARISKKTRRILRKTARLMPVTIVSGRDVEEICTQVGLQELFYAGSHGLDIRGHNIHLELPEGDEALQDLDRAMEALTRQLVNLPGVTIGRKRFAIVVHFHPEEADHAEQVAAAIKQVQALLPRLKITGGKEVLELLPDIDWDKGRAMHWLLSELGMDGADVLPIYIGDDVTDEAAFT... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 326
Sequence Mass (Da): 36179
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A0A962RWL4 | MAEALAINPQASLLLLLRQAGVMVALAASVALGLYVALWARTPEYTVLYTDLSERDLSQVVDALQSNAIPYRMDANGGAILVAADKVHDARLKLAAAGLPRSAGMGFEMLEQEQGFGTSQFLEQARYQRAIEGELSRSIAHINNVRAARVHLAVPKQSAFSRTRREPTASVIVDLYNGRRLEPHQVGAIVHMVSASVPSMSPDQVTVIDQQGNLLTDTAGGSDELVLSAKRFEYTRRLEESFVDRIEAILMPLVGPDGVRAQVTADIDFTTTEQTRESFNPDLPAVRSENLIEEERRGGGGPGGVPGALSNEPPAAATAP... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 408
Sequence Mass (Da): 43066
Location Topology: Multi-pass membrane protein
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A0A523KUH5 | MMMSRSQNAGKPLAGLLKGYNTIEPVPDIDIVDITSNSRTARRGSLFIALRGINSQGIDFAIDAVKSGAVAVIYDSEDEYCVRRIPLLGKQVQTSWIGIKSLDRINGEIVSRFYGEPGRYLKIIGITGTDGKTSVTHLITQALTRIGKSVASIGTLGYGIGNKFDTATHTTPDAVTLQSYLHEFHEQKCDYVIMEVSSHSLQQYRVSGCQFDIAVLTNLGRDHLDYHQDMEQYAATKGRLFRDFDLSARVLNIDDAFGRQLANEFKSGGKIRYSALAPKEKQGVEVYLLNSEITEQGLDLDVATPIGEIHASTALMGQFN... | 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... |
A0A523MPT4 | MAGDGPEAAVTRRLFFALWPDEPTRVALVRATRTAVRRAGGRPVAQANLHVTLAFLGNQPVARYAAIVAAASALSPVSVQLELDRFGCWPQPRIFWFGPARCPAELAGLVDGLWTAMAPLGLPRETRPYRPHVTLARKVAVLPELEPPTPLIWKASDFSLIESVTDERGARYTVAARFPAGSPHDPNPV | 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: 189
Sequence Mass (Da): 20506
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A0A843FUB3 | GLTTCCISSQASEEGIGKYFIKYMNLKNYVIGLIICFIIAVALNLGPGIHIGLLGIIGGAFGGALIALLAKKHLKIANGDVLGASNELGRLFSLIAMLVLISINFSALI | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A3M2E8X7 | MPRIDKTGMPPGSPIHVSHNQPLPTAVNIYRFTHDQLDIVRDASSEQVLDLLQTPFHGTTWVQIQGLADTQFLAQLAQTLDIHQLILEDILNCHQRPKLEEYEHLIFAVLRYALWDLETTLNSDSQVSMIYLPHVVVSFEESSTSLFNPVVERLKNARGKLRNHGPDYLFYALMDVVVDSYVYMHDTLEDYIFELEEELLSADTDQATLLKIQNLKRVVLRQRKAMLPVANMVSGLIRGDNSLIKETTLPYFRDIEDHALRVIGNLETARELLDSMLDVYLSLVSQHMNEIMKVLTVFAAIFIPLTFLAGVYGMNFKHMP... | Function: Mediates influx of magnesium ions.
Catalytic Activity: Mg(2+)(in) = Mg(2+)(out)
Subcellular Location: Membrane
Sequence Length: 352
Sequence Mass (Da): 40616
Location Topology: Multi-pass membrane protein
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A0A9K3CW22 | MSEEGVEYVVGIDEAGRGPVIGPMVYGIGWCRSDITERGELKKAGFVDSKTLTAAKRTVLRDRMDKFDNLHYKTRVLSAKELSRRMMAVTRDSLNAISHQAAVELMHHVVQWCNERKARIKAVYVDQVGPVGQYKGLLEREFPGITFVVEAKADFKYNIVGAASIAAKVHRDHLIEAPVLSEQERGWGGTTSWGSGYPADPLCKAWLADHCDPVFGYPECVRFSWKTVDTALEANEAAEVQYAPQRERVGNDRGYLSTCGLSHSSGI | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Seque... |
A0A966X0R1 | MNQGLLIRWKGESVEWLIHDAGQPIQEGQGSIEALSEVLAAMDPPLVDPEAAVLISGQEALITEITVPSKPTRQILDAIPFLVEEQVVGSIDDHFIGLGRREGDQLSVVVLRQEIMRSVIDAFDQASIRVEFIGVDSQLLQHENMVRLLVEEDMVHVIQPHGVGVAMAANLAEQLIPSDLVTDSVPIECLDFSRNGAMVTSLVATSSPEVMVSSASDGTIEPGLLRYWARSGNPLAVNLRQGVFAYRSSRLKMATLIKGGLLVVLTVLGTQLAANLAQAFYLTNQADQLGSEARALYLSVYPASQAPRNMARLWRARLSG... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 406
Sequence Mass (Da): 43824
Location Topology: Single-pass membrane protei... |
A0A967CE98 | MALDTAPTIRNTFGLPVRSQALHEVDFSADLPRTIRDIQRRKLNWCVIGDASNAILPPFFPVVVLRDTNTSIEIDGNYVRAAAGCSWDELVSFTISNGRYGLENLSGIPGRVGAAPIQNIGAYGAQLADTLVELTVFDGLKQRYETVDISELELGYRTSRFKKSGESHLVIVDVLLKLSDQFVPNIAYHGVAQSIGVDPASGSNVTASEVRSAVLKLRAHKLPNPERAGNVGSFFQNPLVSDAEAGRFSKLGLQIWEGSAGTKISAAQLIEQSGLKGQSIGGARVSERHALVLENSGDATYQDVVHLMRHVQDTVLQRFG... | 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: 334
Sequence Mass (Da): 36174
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A0A534BDF8 | MTDVLSAILRALSFVLLFQAAGVAIFVALFGRRLASSRGAVRRLGQAAALAAMVLVAGHYALEAARMTGELSGMWDSSLQGIVWHSPSRAALICRLSGLLLITIGFQGASPRWTIVAVAGAVLAALAFTLTGHTSVNVHRGALATLLMLHLMVVAFWFGALWPLIVASLRETPARASEIIERFTAVATWLVAVILLAGIVMAVLLLPSVSALSEPYGKLLIAKVVGFAVLMGLAAANKWRLGPALVHGSVQTGRWFRRSVAAEYVLIAAVLTITAVMTSFFSPEA | Function: Involved in copper resistance.
Subcellular Location: Cell inner membrane
Sequence Length: 285
Sequence Mass (Da): 30097
Location Topology: Multi-pass membrane protein
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A0A8T6GTE1 | TRATPLSYSNPTPTYETPSCHVGSVRRRRDMRIMTGSPVPEGADCVIRVEHTDAERQPGRVAVFSEGDRGRNVRPAGQDMRAGETVLTRGTTLGAGQLGVLAACGLTSVEVHRRPVAAVLASGDEIAPAERFAEVAAGRAIPDTNGPMLAAAVAEAGGEGVRPGIARDTEESVREHLLEGAAQADLLITIGGASMGEGDLFKRVLDELGYEPDFWRARVRPGSPFGFGHLPVEGRAPVPVFGLPGNPASAFVTFHLFARPFISALAGHRHPFPPVVRARAGVAMGGPGGLAVYPRVHLLPASGGGWTAVLSGHQSSALVA... | 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: 364
Sequence Mass (Da):... |
A0A7C5PVK8 | PALNKIQDELKGLRDIMEAPLMQFAWGETGRVQPLYASLLKQLMTLGLSSRLSKSIARQSANQGLNKHSWLESLKLLAGLVPVDDDDILTSGGIVSLIGPTGVGKTTTIAKLAARFALKHGRRGITLITTDNYRIGAHEQLRTYGRILGVPVHVATDAEELKNLLREADIPSGENERRLTLIDTAGICQKDVRLSEQLTTLNLSGMEIKNYLVLSATGQMNLQDEVIRAFRKLKLSGCVVTKIDEAASLGEIISVLVQHDLPLHFVCDGQKVPDDLHQARGQLLVKEAVKLMRKTNKSPSAEELAYSFGGMVNNAII | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 317
Sequence Mass (Da): 34648
Location Topology: Peripheral membrane protein
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A0A1F3TBC6 | MYKLLVISIDELWLKGKNRPAYFRAIKKHVVDVLTHYQDEVIPIKNEEQRLICTSEKGFNQDAILALQKVPGLHSIQPSRAIDLDLEKIIDEVDLELASMREMPRTFKVITKRTNKRFPHNSMEISRYIGHLILKKLPQYKLVVDVHKPQLVVSLKVSDQHIYIATKTYPGIGGQPFNTSGHLITLLSGGFDSPVASFLMNKRGCRQTYLFFYAYPFVGQNVLDKILKLVGILGQYQNGSKLYVLPFGEFQKELSDHIKPDYRTLFFRKYMLEAAALLKSRLKADAIITGDVLSQVSSQTIGNLAIVDQLTPAMVLRPLI... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarb... |
A0A946UZY7 | MFAASIRTRPEDFEVTEVLGWDLSGDGEHDYLWIEKTGANTEWVARQLARHADVPAKDVGYAGLKDRHAVTTQWFSVPRWHAPDWSSLDVEGVLVLDTGRHSKKLRRGAHKGNAFRIVLRGADIAGHADALAERVQEIGEGGVPNYFGEQRFGRGGGNLRLADDWAAGRRLPRHKRGMAISTIRSFLFNEALSLRVSDGSWNRIRPGDTVNLDGTGSVFVADAVDADLERRCAGMDVHPAGILAGQGCGAGPETWRAALDKARVEPGARSLRLHVSDLEYALEDEAVELRFTLGRGAFATSVLREIANADS | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 311
Sequence Mass (Da): 34001
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A0A9D6WE24 | MRIDPDPDGERRRAILSRLNQHAPSAARERPKAKPRRRRRWRRWLVLPSVVFLALTVAPVALFTTVTPPLTAFMARDWVIAQREGRTDYRLRHDWTPLRGIPAELRAAVIAAEDQKFRRHRGFDFDSIRSAMADYEDGERVRGASTITQQVAKNLFLWPGQSWMRKGIEAWYTVLIETFWGKARILEVYLNVAQFGDGIYGVGAASEVFFHCRPGALNAEQAAMLAAVLPNPIRFRIDAPSDYVRERQHWILGQMRHVGEGM | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
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)-Mur2... |
A0A2E3UWV8 | MKNLGNVYVITAPSGTGKTTINRRLVRENEEIEFSVSYTTRNKRENEVHGKDYWYVSEDKILELINNSEMLEWANVFGHYYGTRLSELENQLLEDKKILLEIDVQGWMKVKKRSSEVKSIFILPPSVEKLRQRLFNRKSESIESFKRRIMTAKSELLYAKYYDSFIINEDLEKTYQKVKDYIKHGKIFSMSKNQAIDHCNKLIDDFSNINLDL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 25193
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A0A523JW25 | MSRGLFITGTDIGVGKTLVTSALLQALGAAGHTTLAMKPVATGCWQTADGLRSEDAEELISAMNQDASYREVNPVALETAAEPIVSAMRNRVNFTTDEIAAQAVSLSRRADWLLIEGPGGVQTPITGKDTTADLALAIGFPVLLVVGLRIGCLNHATLSVELLQQKGLRIAGWIGNEHDGAMSELEPTVHTLEKQIRADCLAIIRWQPRLDPQQLARQLHPAARKISR | 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.... |
A0A9D1PT27 | MNRAKSILWYDLETFGLNPHVDRIAQAGYIRTDLELNIIEEPDVIYNRLTDDYLPQPESCLVTGITPDVVNSRGMREYEFISKLNSEFTRENTTVCGYNNINFDDEAVRSTLYRNLMDPFERESKKGRTRWDIINLVRAARDLRPEGICFDKKNEETGFTSFRLTDLTEENGIEQVGAHDALVDVYATIAIARLIKTKQPRLYSYAYTHRTKYDIWNLIEEDRSKVFLSTMPLFASERGNTHPLMPIWRTSENSSDIYFFDLLSPIPSSLDEIADLRESGIIKIQTNRCPFLCPISVLDKNAEKRLGFTKDEILKKASDI... | 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: 472
Sequence Mass (Da): 55497
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A0A967ZC19 | MPRRSRSSGHWRKQQHADPYVQRAAREHWRSRAVFKLEQIQTKARVLRPGLRCIDLGAAPGGWSQYAAQIVGPKGYVLAVDLAPVAPIEGVDVIQGDFTAPETLTRMIEALGNEKADLVMSDVAPNITGNRAVDQPRAMNLAEEALALCETLLRPGGSFLVKLFQGEGFESFVETTRTQFQKVRLIKPKASRPESREIYLLARNYGI | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subc... |
A0A2E0CA81 | MTEAADNPQQAKNADPQRPETEEAVSFGFEQVSPEEKTRRVGGVFAAVADRYDLMNDLMSLGTHRLFKRMVLQMAGVREGHHVLDLAGGTGDMAALFAPAVGAQGRVVLTDLNRPMMQVGRDRLLDQGISQVEFCQAPAEQLPFADDSFNCACISFGIRNFTDKDQSLAEILRVLKPGAALLVLEFSTPTDPLLETAYRTFQTLWPPVGKLLVGDAQPYQYLVESIRMHPNQKTLKQMFEDAGFVETGFHNLVGGIAAIHRGVKPESTSA | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
EC: 2.1.1.163
Catalytic Ac... |
A0A946UWQ2 | MIDYAALAQCWRDLNLEHWWEPVEALSRARLTTAHHGDYEKWRSVIEALPRVADDPAALKEELLKLAPWRKGPFELGGVTIDSEWRSNLKWDRIAGALALEGCNVLDVGSGNGYYALRMRQAGANTVIGIDPTLLYVMQFLAVNHFVGDTQTFILPLRLHELPDRGHRFDVAFSMGVLYHQRAPIDHLRQLRDTLRPQGQLLLETLYLPGEEAYASTPTDRYARMKNVWLLPTIAELMTWLARSGYRDIELVDQSVTNTDEQRSTAWMSFESLADALDPGNPDRTVEDWPAPRRVIVSATSP | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
EC: 2.5.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+)... |
A0A520TQR1 | MIDKKKSIDFEKSLKELEKIVEELESGELSLEQSLKSFEQGIKLTRQCQSELERAELKVKKLVEENGELKTKPLDDD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A368BUK0 | MANKISLAVLISGNGSNLQAIIDNIKNQKLKADIKIVISNNIDAPGLEKAKASNIKTTCINHKNFKSRELFDDEIIKEIEDQDVDLIVLAGFMRVLSSKFVNKYKRKIINIHPSLLPKYPGLNTHEKVIENNDIEHGVTVHLVEEGLDSGPIIGFAKLKIHENEDEESLKKRIHKLEHFIYPKIISEIQEKKIKIENKIYHEGNIYKHGKEFFI | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
A0A1H9RVK3 | MEQHIVIAVDGPAAAGKTTTSRALSDRFSLSYLESGRAYRTLAHEALSTGINPEDSQAMIGLITGILQRSRSNALFDPARINNSELRTTAVSKAVSAVAKIPDLRKAITSLMHNWAQSRTASIIEGRDIGTVVFPDARIKFFLTARADERAARRHRQEIGSDYQEVLADVVRRDHEDTSRAASPLRPATDSVVIDTTDLSLDQVINTMSTVCRIAGLTEIRHIA | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24480
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A0A2D7G740 | MPRLTYPFPLTSLRVPEDLHWIDLKTGIYLDWFASKINTWQKAHGRHDLPWQQNISAYRVWLSEIMLQQTQVETVKPYFIRFLEKYPEXSELARASTDXVLALWTGLGYYNRARNLHKTSIIIHKDYQGAFPSCLDRLTELPGIGRSTAGAILALSMGKRGVILDGXVKRVLSRFHLIEGYLEERTTTDELWWHADRHTPAIETNVYTQGIMDLGATICKRSAPACSECPLVNRCGAHQHNLAAQIPRRKPKRKKPVKDSLFFIICNEDKEVXVEKRAESGVWAGLWSPXERCKEYSLDXILEELDLHEDSVLNIATESP... | Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatc... |
A0A1X3PBQ6 | MAGTHDDAPRTSSPRRRRKSRRRRDPEGKMPLKEHLRELRNRLIKACLGIVVGAVAGFFLYDTIFALLSAPVIGFDDVDRSTEIAFNTVGQPLDLMIRISLFVGIVISSPVWLYQLWAFIMPGLQKKEKRYALGFIAASVPLFVIGIGLAYVVLPQAIRFFFTLNPEGTSNIIAPDVYFTFVLHLFLAFGVAMVIPVILVGVNMMGLITGRRVLKSWRGTLMFIALISAMAAPGGDAITMFFIAGPLVVLFGVAIVLCLLNDKRREKRVAAREAATEDLITRT | 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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
Subcellular Location: Cell membrane... |
A0A9C9H238 | MKTRRTLCNTLTKPSTSSNRPAPHLANRRSKSRPPVKAPDVQGQPGLVLAHYGQASLVESETGDIIRCITRKNLPRTVCGDRVLWTSSNPREGIITGILDRDSTLVRPDHNNRPRPVAANMDQIVVVIASKPSFEYGMLDRYLAAAELLGVTPAIVVNKCDLLDEESRERLEQRLSLYRDIGYTLLFTSTRTTDGMKALYTALKPHTSILVGQSGVGKSSLVQTLLPDLDIRVGNLSQVTGLGRHTTTVAMLYHLPDGGNLIDSPGVRDFTLCNVSPEDLAHGFREFLPFSGQCRFHNCRHVSEPGCAVSDAVRRNAIHP... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A9D0P4S2 | MGHQKIPLVIINGRLSDKTLNAKNWMKAAYRASLKHVTRVLAKNPTDGAGFIQLGTDPDKVDVLGNLKFARQSGIVEKKSSALPRPYWLAASTHEGEERLLADIQQSLKSPLLLVIAPRHPERSTMIQGQLKAMGILFSVRSKNEPVTAKTQIYLADTLGEMRWLMKFSQCVFMGGSLVPVGGHNLLEPAALGCPIIVGSSVHNVEPEVELLREHQAILEVPNAEALKDMINTLSHDPTGFIPLGQAASQAFHGQQGVLARYLRALGKLQLFSSRQHGF | 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... |
A0A3M0YB08 | MSRVDIVEVIQPRLPLKKAGRDYVACCPFHAEKTPSFTVSPAKQFYHCFGCGAHGTAIGFLMAFDHLSFVEAVEELASQVGLPMPRLNEAAHPHRNLQACLEEACAFYQKMLAQSPRGKRYLAARGIGEAIIERYRIGYAPPGWDTLLRALGKDQERCRQLVEAGLVVEREGKRYDRFRDRIMFPIHDPRGKVVGFGGRVIDEGTPKYLNSPETPLFQKGTLLYGLHQARQAGPSLPHILVVEGYMDVIGLAQHGFPHSVATLGTSVTRSHIQRLLRTAPKVLFCFDADAAGKKAAWRALENVLPELAESHKVGFIFLPE... | 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: 561
Domain: Contains an N-termi... |
A0A2E7GHT4 | MFGLSTGHLLILLVVALLLFGSRRLPELGESLGKGLRAFKKGIEGGSDEPKQIDQEKKSPHDPDHKA | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 67
Sequenc... |
A0A3M0Z1H3 | MAARLAPLEAALEEALPRGAAAARPALARAGAALDRLFDEGVPATVLLPYRALLLDRALRGLWRRHLGGPGEAARAGGAPRAALVAVGGYGRGELHPHSDVDVLVLVEEGALEGPHAPLRAPLEAFLTELFDLGPSIGHSVRSPAQCAEEAAADLSVATNLMEARLLAGPAELFQAMREATAPARLWPSDAFFQAKRREQEARHHRFHDTAYNLEPHLKEGPGGLRDLQTVAWVAHRHFGTAALRELVERGFLTETEHRALVEARAFLWQVRYALHLLAGRREDRLLFDHQPALAARFGYRDGGPNLAVEQFMKRYYRTV... | 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 ... |
A0A2E5M9C6 | MSHWASARFRNRWAGTAWTVALSAERRARLSLSDLAAIRLRSTKVTWAAPRDSASRPRAPLPANRSRQRAPVMSAASQLNNVSRARPSEGRKPPSAEKAIFRPFHLPPIMRTSLPAITHGGPIEKRRQLSANWCGSRYVSEQAQQPEKSGFWGKLRTGLGKTRAQLAEGVGNLLLGEKEIDADVLTELETALLLTDVGVDATTEIMASLTAKVKRRELNDTVALHQALADMLKEMLCPLGRPFTLEGIDPPAVIFFVGVNGVGKTTTIGKLAKRLQGEGHEVMLAAGDTFRAAAVEQLATWGERNGVPVIAQQQGSDSAS... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... |
A0A2E8NG83 | MNKGLLILISAPSGAGKTSLVNEXIDRDXXXIKSVSHTTRAKRPGEXESIDYFFTTESEFNQMVSNNDFIEHAEVFGNFYGTSKNYVEENLDSGFDVILEIDWQGARQIQSVKREAVSIFIAPPTKQELENRLRXRGKDSEETISIRMSQATSDMKKADTYNYVVVNDSFETATSQLLTIISAERLRTSHQIKXNEALAFLLSPK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 23100
|
A0A2E5VBT3 | MDIYLGLGSNLGDRKNNLSKAIYLLEKSGVLILKISPIIETPALLIEDSPSDWDLPFLNLVVFCRVTKDPELFFLDIQKIESQLGRVNNKKWSPRSIDIDILTWGNKIISSKNLRIPHPKIKERNFVLTPLLSLNPKLKIPGIKKNIIDLSTSIENHIPLWMGIINITPDSFSDGGAYKNIDDINNRINRMVENGVNIIDIGGESTRPNAKIISSDEEWERIFPMLQLLKEKRKHNVLYPHISVDTYHPETAIKAIELGVEIINDVSGLTTPEMQDVAKNSKQDWIAMHNLGIPANKDKIIADESLDKINETIDKWLIKN... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
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