ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A537TS30 | MEQPQRACRTRLRDPPRRDCRDRRRGRGAAGRAGLRRAVGARRHRARPLRGAGRRRRVVRRQTRAIARRRVRRARRRRRGAARRLLPRSARRSRVSLVFLLGGARSGKSRHALRLVAESGLDVPFVATAEARDEEMAERIARHRSQRPQTWLTIEEPLQLREAVERVPAAMALVVDCLSLWVANLLEQGAEEDEIVREATVVATEVASREPLSIAISNEVGLGVVPATVLGRRY | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A7X7JDQ3 | MSNPWLIVGVAAGSYLLGSVSPSVFLGRLVKHVDLRRHGSGNPGTTNAFRVLGVRLGIVVLVCDILKGLLPILVCRWLGFGPLASVGAGLAAIVGHNWSIFLRGKGGKGIATTAGVIIGLMPIISGIVVLSFAVMILITRYISVGSLFATLVFVAATLIGRQPWPYIVCSSCAAVMIFYAHRGNLKRLFKRQEPRLVLPWEKKKSAAKTAGNSNSAKATSKQAKPNAHKHAPRKAPKRVAPRGSG | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A8S0H1N9 | MLLQAGKRLGPFELAVAAAQGCTELQVVRRPRVALLSTGDELLEPGTPMRPGCIYNSNRTLLRHWLEALGCEVIDAGILPDRPQHTRLRLEQLQHGADLILTTGGVSAGDADCLGQVLRDSGRPLFWKLAIKPGKPLTVGYFGQVPVIGLPGNPASALVTFGLLARAYLLRLQGYRRWRR | 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: 180
Sequence Mass (Da):... |
A0A7X7ZXW0 | MPEGRARGDGRTDGDIREISFETGFQPSPDGSTLISWGETRVLCSATIENRVPPFIAPKSGGWVTAEYDMLPGSGNRRVKRDRSGAPKGRSQEIQRLIGRSLRQTLDLSRIPDRTITIDCDVLVADGGTRVAAITGGAVALRLALKRMLTRGDIETDPWKGFVGALSIGLVDGRILADLTYEEDSKAEMDMNVVCLSSGLLVELQASAEHRPVHMETVMDMAGQAVSSILGYVIPSQKLAAGD | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. ... |
A0A2S7TZY4 | MRSATSKCKPAKKSSRTKSKNFPTNREMSTPNKLVVGTRGSALALVQAEMTEGLLRKAFPEAEIVRKVITTTGDRRTDVSLAEVAKVEGVFDKGVFIKELEIALENGEIDIAVHSLKDVPTVLEDQFEIVSVLERAPVADLLITKNAGGLEALPQGAKVASSSCRRQKMLKWLRPDIEMVDIRGNVPTRLRKLAENPEIDGIILAEAGLVRLGYNATGEMSTEAGSVFGCAVDPEQFLPAAGQGAVGLEVRKGDECSANFAKAINHAPTMTRITAEREFLRLLNGGCHTPVGVSTQFFGDKLLMEGIVFPEGEAIGDPMQ... | Cofactor: Binds 1 dipyrromethane group covalently.
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: 342
Sequence Mass (Da): 36789
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A0A538N8P4 | MSESTPGTITALGREVRGPMDHLEWFPAPEHCTRVRFSSDELSSVCPITGQPDHSSVVIEYEPGQRCIESKSLKLYLWSFRDRPVFAEALAAEIAAEVNRTVEPRGVKVVVTQHVRGGIVTEATAEL | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
EC: 1.7.1.13
Subcellular Location... |
R7ILQ1 | MTKNPSPSTSVKRRRAPVVRPYLRQSMKQTEAPKRRDFTGVRRFLTRISRGAIWLVIAVLILLLTVALATYSPADPGFSISMHVDQVENWLGRTGAWISDALIYMFGVSSWWLVVTGVFSLLSLALGSRRSDKVREQERGLSWIVSIIGFVCLMFGSCCLERFLELGVYGLLPAGPGGVVGHFFSRPIVHTIGVYPAMAVFLVMVILGASLLFRFSWMDICERIGTVIDTILHWGSIRRAEAEDRRIGEQVRQEKSSETLPVKHEVSIEKAPAAATPETEHEDAAGDADESPAAEAPKRPASRPSAPIPLRTDLPAGPRF... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
A0A2N5KQ27 | MIDFLERVFSPLTNLLGSGLEFFHAQGAPWWLSIALLTIVVRTLLFPLTLKQVKSMRAMQDLKPEMDRLRSKYQDNRQKQQEELMKLYQERQVNPLGGCLPLLVQMPIFITMFYVIRGFDKTHPDFASGGILWFQNLTVADPYYILPVLSAVTMLAASEITAKNLEPQQRWMMRILPVVFTVFLLAFPAGLFMYWITSNLVTLVQNYLIYNYGPGKKAPAPSGDRKANVRNDSHSAKKQGLATDAGNEHKGTQVKQPSTGGRKKKRRK | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A537YH98 | MGLASRGVPPGGHVHLVGIGGAGMSAIARVLRESGYEVSGSDQRESAVLGALRGLGVTVDIGHRRRRVEGAHLVVASAAVPDDNVELLAARAAGIPVIPRGEALALLVQGLRTVAVAGTHGKTTTSGMVATLSQAAGLDPTWLLGADLADRGPGGRLGLGDLAVVEADEAYGSFLWLAPDIALVTNVEEDHLDHYGTMEALTGAFEQFVASSTGTVILCADDPRALALGPAVQAGRLITYGLAGSPDVGAAGVETSAAGSSFALTVSGRRAATVQLRVAGRHNVQNALGAAAAGLALGLEPETVAEGLAGFAGANRRFEY... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 467
Sequence Mass (Da): 48166
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A0A7K1GU49 | MNISSESNQASQPGQPIWHEPGVTRSQRWNKHGLVGATIWLTGLSGSGKSTIATELARELLKTSRLAYVLDADNVRLGLNSDLGYSDDDRTENIRRMAEVACLFADSGTVAIVPIISPFIASREHARKIHKDRQLKFVEVHVATSLEECERRDTKGLYAKVRSGDMTGLSGVDSPYEAPLSPDVVVGLASESLQESVAMIMTKLLVKAGT | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 210
Sequence Mass (Da): 22835
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A0A432JPZ9 | MPTRTRSRCSTPCSTASTVAPPRKAAPGSPRVTRRGVRPDVGETVPVRLTRYHGLGNEFLIAFTDSVPADAPEHARRLCDRSDGIGADGLVFGTPTDPDLANRLTFTLFNSDGGRAEVSGNGLCCFGHAILRSRPGCGGGLDVVVDTAAGPRRIRVAGDPADVKVPATVEMGEAVAGPDTAGLVVDLGGPTAGRMQSVDLGNPHLVVEVDDVDAVDLGSVGPSIEAHFGQVGCNVHMVTVLDRSTLRLRPWERGAGLTEACGSGACAAAAAAHGWGSVDGSVEVRMPGGTAVVTVGDPVVLSVPSVFVDEHEVDDG | 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... |
A0A3A4V6U7 | MGVDNNQSFVATAKLDKLLNQGRGRSMWVFAYSPACCAIEGFMHAGGPRWDFDRYGFVPFASPRHADLMIVGGPITRKMVPVIRRLYQQMPEPKWVIAMGACSCSGGLFKDSYNVVQGVDKILPVEVYVPGCPPRPEGLWDGLLKLRQKIINNEPMRYMNWQPLKPAKKA | Cofactor: Binds 1 [4Fe-4S] cluster.
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 tw... |
A0A8J6YNB0 | MQLTLKGKLILWNAILIGFVGVFLLISFNSFTSYMLPKVMIEEQHQLSPEKDASSSSARKVQIEPIPHPFFQKMDISTTRGIRSLTDQLRLFSLICLFAAILFGSAGVYFLTTRALKPVQVLSNRMKQINIHQLTTPIPMEGAEDEIREMARSFNDMLERLNRVFQRQQSFISNAAHELRTPLSILQTNLEMITRDPNATLEEHKEMLHVFRRNLQRLDELIKHLLLLASEKPIPLEDEINLHSTLKEVLHELMGIAKKNSISIQVNGDPHLVLRGNQVLLRRALSNLIENGILYNRPHGKVEVSYFRRSHEIVIMVTDT... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 392
Sequence Mass (Da): 44510
Location Topology: Multi-pass membrane protein
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Q0A588 | MWGFGRKKKQRRQAEEEARRAAEEAAKAETTPGPEAEPEPEAEPEPETETEAATETEAEAAPVSAEPAEVPDEPRKQGLFARLRAGLSRTRSGLTEGIASLFLGSKTIDDDLLEELETQLLLADVGVEATQRIIDGLTARLRRAELKDTDALFQALKEDMTAILSPCEAPLELPNEPKPFVILMVGINGAGKTTTIGKLARRFGDQGKRVMLAAGDTFRAAAVEQLQAWGERNNTPVIAQHTGADAASVVFDGWQAAKARGSDVLIADTAGRLHTQSNLMEELRKIKRVLGKQDPTAPHETLLVLDAGNGQNALAQAREF... | 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 ... |
A0A662T9Z8 | MSFKISANEFDVQFMKEHGYVRKKCKRCGAYFWTVNEEAEFCGDSPCVDYKFIESPPTRKKYSLKEMRESFLRFFERNGHEIIKPYPVVARWRKDLLVTIASIVDFQPYVTEGIVEPPANPLVISQPCLRFEDLENVGFTFGRHMTIFEMGGAHAFNFPNKPEIYWKNETIGFHHEFATKELGIPEEYITYKEHFWSGGGNAGPDVEGSILGLEVSTLVFMSYKVLNKKLIPLPVKTVDTGYGIERWTWLSTGAYTAFEAIYEDVYDKLVRLADIKIDREILRENSIVSGGYTYDDVKRTHTIRAKVAKRLGMNIDELEA... | 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... |
A0A7N0ZRP3 | MTGYAEIEQEKFNLINSTYKTLEQLENYKNETINFEQQRAISQVRQLAFQQVLQGAIGTLDSCLNNEIHLRTISANVGMFGGMKEIKI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A1F9D7U9 | MAAASQNELSGESLSPMFSGIIRHYDLINHVFTWGMDRRWRNELVEECLKLNPEKVLDIGCGTGDLTIAIARRSRENLHITGYDFSSPMLDAAFKKARKASLDKKISFIHGEAAHMPFPDDSFDCIGISFAFRNMIYKNPLAKRHLAEIFRVLQPGGSCLIAESSQPKNKLMRRLHHLYLRTYVYAMGVLISGNKKAYTYLIESVINFYPPEELEKCLLAAGFRQVFYCPLFFGAAGIYRALK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
A0A6V8DRZ7 | MTEREEVPADAKLPTENGDFRIRVFHDTISGLDHVALTLGEMGGPSPVLVRVHSECLTGDVFGSLRCDCGPQLNSAIRQIQEVGWGCIVYLRQEGRGIGLHAKIQAYNLQDKGADTVEANLLLGHPVDARDYSIASEIIRAVGIHTVCLLTNNPDKVGQLVSNGTNVSERMPLIEGVVDENRDYLSIKVDKMGHDIPEDKLGS | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
EC: 3.5.4.25
Catalytic Activity... |
A0A7X8UHV9 | MLIAAEARDAVKARGRFTLALAGGSTPLSTYRLLAAAPFVDLIPWRDTWVFWGDERCVGPNHPRSNEGMAREAFLDRVPLPRENIHPVRCEGGVKGSDAAVGMGAADEVRRSAARYEDLLRNIFASPSVGAERGAEGVDSARNGPAGFGFDVILLGLGEDGHTASLFPGSEALHVGDRWVVAVSGGTDAAGIKVAGVDAGRAEVAAEREMWRVTLTPEFINRASLAVFLVTGAAKAEVVRQVLEEPADGDRFPACLIHPANGTVRWHLDQEAAALLTAGPVSGGIYT | 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... |
A0A538B6U5 | MVVPYREPVRAIAYFSPEFGVSEDLPQYSGGLGVLAGDHLKGAADMGLPLVGVGLFYDHGYFHQKLDDRGWQQEEFPQLDPTALPLTPVDGRVPLELAGEQVDADVWRYDVGSVPLYLLHVDGVTDRLYGGDIEHRLRQEIVLGVGGVRLLAELGIEAEVFHSNEGHAGFLMLERIRRAIVGDGLSFDEAVDRVRPGGIFTTHTPVPAGIDRFSRELMERYFGAWAAECGVDIDRLMALGHLPDEAPDAAFNMAVLGLRLAGRANAVSELHAHVSREMFASLDVRIDAITNGVHVPTWAAQQPSAEMDNEALWAARAAGR... | Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosy... |
A0A2E4AX46 | MNKPKVLFLGTAPIAVPALRVCAQLQEIELVGVVSQPPSRRGRGRKLMPSAVHQAAQELSCDVVTPDRFRGEEGDTILNRFAPDACLVMAYGQIIKADHLARCSNRWFNLHGSLLPRWRGAAPIERCLEAGDAVTGVQLMRMEVGLDTGPVFAERRIETVGHNAQSLSVALGNEAAKLTQSHLVQAIKGQLEPHPQNDDLAVYAHRVLRQEGHIDFRGKAEVWACKSRAFDPRLGLRCRLIQSNRVLGIKIWSAQVETSLTADKPGKILKCDASSLWVSCEEGVLNITSLQVDGKKRLSWSQARSGLSLTTSDYFDQ | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A6A8MUD4 | MTISSKTSLRVGRLLKAHGLKGAIKLELYTDAPNERFVPGATFNLQVPETSPWFGKTVTVKELRWYNAQPVLFLEGIEDRNQAETLIKAIMLVNQDLDELPTEPDAWYDQQLVGLAVLRDGVEVGSIIRVEHYPAQDMLIVGTKDEKEVMVPFVKAFVSTVDIEAKTITVTPPAGLFEEIEE | 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 ... |
A0A522TTQ0 | MQPTKGIDFSDAALGSRRGIMGILNVTPDSFSDGGRFFDTEAAIERGHQLAIMGADIIDVGGESSRPGAVPVPVEEELRRVIPVIAELSNSYRVSVDTFKPEVAARAAEAGATLINDISGSLAQVAADHEVGWVAMHMQGSPQTMQRFPHYEDVVTEVFDYLQRKIDWAGNLGVSEIWIDPGIGFGKNLQHNLSLLQRLDKLTELGVPILVGTSRKAFLGKIAKASTGFEVPPIQRTEASVSSCAWCFLNGATMMRVHDVAETRELLTLLSWRQDKLSKVNR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
A0A7W0PGZ1 | MTALYRKYRPQGFDDVVGQEAVVRTLTNAIEHDQVRQAYLFAGPRGTGKTSMARILPKALNCAGTPGPSPSPDKICHVCTAIANGTSLDVVEMDAASQRGIDDIREIRERVVLQPVEGRFKVYILDEAHQLTDAAWNALLKLIEEPPPHLLFVFCTTDLGKVIPTVRSRCQTFVFQRPRLPELVTLLRFSSTSRASSVSWSREMKRSSSGWSSSSSMPASATPASSTTASRRPMTS | 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: 236
Seq... |
A0A6I3DIJ4 | MSHRRSTSPLLGVLAVLAALFVISPLLSVVIRVPWREFWSTLTSNAVRESLYISLQTSFVAAVLAAILGIPLSWWLARTSNRLARIIRTVCIAPMVLPPVVAGIALLAAFGRRGVVGEQLYNWWGISLPFTKTAVVLAQVFVAMPFLILAVEAAFRQANEGLEDAARTMGASPLRIFFIVVVPSVRPALVAGLVLAWARSFGEFGASITFAGSFPGRTQTLPMSVYEIATYDYRQALVVSVFMMIVSVGVLAVMRDRWATGATR | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 28698
Location Topology: Multi-pass membrane protein
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A0A1H4IM26 | MEVLKFGGSSVSSEVSLKNMLKIVNNYDLENEPLIIVVSALKGVTNELVALTKLLKDGDQEYAKVIRTIFEKHKEFINIIFKEEQSELLKKIKLVENDLLESVSNIIKNGVTSDKDYDKVLSFGELFSAQIITAFLNKNRLNFCFKDSRDLIITNNVHMKAKVNWDLTRTVVNSFFSGNKNSYVVSGFIARSIYGDTTTLGRGGSDYTATVLGAILNAEKVTKWTDVNGIMTADPNKVLEASSLENITFSELKNLSKFGSNVLVHPNSIDELSKHNIPFLIRNTFDRDFKGTQVINENSSNKKALSLHESCCLVGFNNTA... | 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: 447
Sequence Mass (Da): 50785
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A0A7N0VK87 | MEAPLERKGRSRTRSRSRSRAERALSPLGRLLLHPNCYTLIHLTITTADPIHIPRLKAHLSTSIFATHPRFTTVPDTGSNHWPDPDTAAVIDPDRHVITVNGPVTSVNDYLAELASVCAPLPTDKPLWEIHVLPEPHSNCAIFVIHHALGDGACVMSLLESFCSPTNEPQITPKQDIVIQIRERGRTAAEVVKTVWFTMVSTVKVLTLFLGEKGVKIVAKTGVNLHPRNKFAIAAATFSLEDMKMVKNAISPPATINDVFIGIISCGLSRYVHLLHSQQDLKGLKFSGFAAVNMRPGKKNPAITDLKGWGNKLGCYFNRI... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Subcellular Location: Cell membrane
Sequence Length: 468
Sequence Mass (Da): 51762
Location Topology: Single-pass membrane protein
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A0A0H4VA00 | MTDNLRGLDLIRDVDVSLTVELGRTRLALRDVLELVEDSIVPLDRQIDELLDIYVNGKPIAKGEVITEGGRFALRIVEMISERRSGEDRRAEERSAPLAENA | Function: FliN is one of three proteins (FliG, FliN, FliM) that form 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.
... |
D3UHY6 | MKLGIFDSGAGGLSVLEHVLRAEIFDSIIYYGDTARLPYGTKHPDSIICFCLEALEFLLVQNVDIIIVACNTASAHALDAMQKAAPKIPIIGVIEPGILAIKNRLKNLDAKILVLGTKATIQSAQYQRHLEKLGYSNITAIPTSLFVSLVEEGIFEGPLVEECLRYYFGGIDFVPDAIILGCTHFPLLQKPIAAYFQNKSLLIHAGEAIVQYITQNSHLLFESKKSRSLLSTKAGIVGDLVDGAHKLDNKTCNKAAQIKTPHARNLNARANNLPRCNHTTLQFYASSDEKGLKNTAQNWLSSAKNFTIL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 309
Sequence Mass (Da): 33848
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A0A803XTU9 | HDIVGLHSSNYNDLYQWSVESFADFWAEFWKYSNIVCSRLYDEVVDTSKSIADVPEWFKGSRLNYAENLLKHKDNDKIALYAAKEGKEEILKVTFEELRQAVALYAAAMRKMGVKIGDRVVGYLPNSIHAVEAMLAAASIGAIWSSTSPDFGINGVLDRFSQIQPKLIFSVEAVVYNGKEHNHLEKLLSVVKGLPDLKKVVVIPYVSSRETIDISKIPNSVFLEDFLATGKGDQAPQLEFEQLPFSHPLFIMYSSGTTGAPKCMVHSAGGTLIQHLKEHILHGNTTSGDIIMYYTTTGWMMWNWLVTALATGASVVLYDG... | 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: 504
Sequence Mass (Da): 55991
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A0A7K0VAL2 | DAGFDMDLGGKDIISVQYQNANNSVRVSDEFMRAYESGEDFGLVARATGEVIERTDARKLFRKMAEAAWACADPGIQYDDTINDWHTNPETGRINASNPCSEYMSLDNSSCNLASLNLMKFLKSDGSFDAKTFGRAAEMIITAMDISICFADFPTEAIGETTRAYRQLGIGYANLGALLMASGLAYDSEGGRALAGAITSLMSGITYKRSAELAGIVGPYEGFARNSSAHARVMRKHASASSSAKSMTTLDIDVWTEANKAWDACLSTGDKNGWRNAQISVLAPTGTIGLMMDCDTTGIEPDFSLVKFKKLVGGGSMQIV... | Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleos... |
A0A7V9PZG5 | MTRRRLGDVDPNLIRSALRDLVPYEPGKPVEEVQRELGVERVIKLASNEGPYGPFPAALDAIARASLELNRYPDGGAFRLCRELAERHDVRFEEVAVCAGADAVIGYLALATLDPGDEIVTGWPSFPSYVLDSLKQGAIPVRVPLRDHRFDLEAMLAAITPRTKLVFIAAPNNPTGTTNTRAELDAYFSAVPEHVLTVLDQAYFEYISDPDYPDAIEEYAKAGRRVLVLRTFSKIYGLAGMRVGYGIGPAEIVTAIRKVRRAFDVASVGQEAALASLDGAEEIARRRDANRAAMTLLEEALRRVRLDPVEPAVANFVYVE... | 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: 374
Sequence Mass (Da): 40732
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A0A7V9NUB0 | MPELPEVETVRRDLVPFLTGRTVHAVSVSRDRAVRRQPHPDFIAALRGRRLTDVRRHGKFLIVDLDSDDALVVHLRMSGQLRVASPRDDLAKHTHVVIDLDNESQLRFLDPRTFGEMFVDEVDAGRRPLALRGLGPDAVNDKLSASAFHQMILGGRTTSTVKAALLDQTTLAGVGNLYADEALFAAGVHPKRLAASIMGAEAAAILKALRRILLAAIKARGSSFPDEGYVDAYGKPGGFALRHQVYGRAGQACPRCGNAIEKTVVAQRGTHFCRRCQA | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
A0A7W0P3D6 | SIVIVAIAAGMFLVAGVSGRHLAALVVICLVLIAAAFQLGVIKEYQLDRIRAFIDRENTPADVRYNLDQAEIAVGSGGLFGQGYLHGRQTTLDYVPEQHTDFIFTVAGEEFGFVGAVFVLTLFALLLWRSIRIAFLSKDPFGTYLATGVAIMFAVQMFVNIGMVIGIMPITGIPLPFLSYGGSSMLASCIGVGILLNVHMRRFK | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-... |
A0A538GJS0 | MSLLRRRPVRRLGRPHRPALRGLGHARRVDPHACRSLPARDDRPARLVSPRFEAPRGTHDVLPAEQPLWQRVIAELESLCALYGYRRIQTPVFEDTELFARTSGAGSDVVQKEMYSFEDRAGRSLTLRPEGTAPIVRAYLEHGLHREPQPQKLFTIATMYRYAAPQKGRYREHYQASVEAIGSNDPAVDAELIQFYNELLRRLGVTHYRLELNSIGDRNCRPAYLERLNAWLDEHEDVLDDEARQKRATTPLRVFDVKSERVQTALVDAPKIGESLCEACREHFDAVRRYLDAYGVAYELTPTLVRGLDYYTRTTWQFEG... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 460
Sequence Mass (Da): 51273
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A0A7W1I929 | MVTAIVIGVHVSVAALLVLLILLHSGRGGGLSDMFGGSMGSA | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 42
Sequence Mass (Da): 4108
Location Topology: Multi-pass membrane protein
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A0A926DAX5 | MALLLFGIMILVHEFGHFITAKKAGIRVDEFAIGFGPSIIKWKRRETQYSLKLLPVGGYVKLGGEDEDTFDGTGFNEKPIWKRMLVLFAGAFMNLLSAFVVAVLLVCLTPALASNTVAQFDMEQSLPEESGLRVGDEIVKVNGQTIHIASDLPVALLADDDGVVDMQVRRNGQVVLLEGVSFRTQGEGVEREVFLDLKFQRAAKTPITVLRHSFFRCVSITKSIWNSLLDLAQGKIGVEALSGVVGTTQAMGQIIRAGLEPMLMIFIFISINLGIFNLLPIPALDGGRIVFLIVEAIRGKPVKREIEGIVNAIGFVLLIA... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 336
Sequence Mass (Da): 36900
Location Topology: Multi-pass membrane protein
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A0A6L5FW16 | MRVLFLGTPSWAVPSLEGLLEAGAEVAAVVTNPDRPSGRGMELKPPPVKETAVAAGLEVLQPAGARSPEFFERITAIAPDVAVVVAYGSILPKPVLDAVPHGFVNVHFSLLPEYRGAAPVQRAVMDGKKETGVSIMVLTEGMDEGPVVAAAATEIGASETAGQLGERLAGIGATLLAETLPAYVDGTIDPVPQDDSLATYAPKISTDEVRIDWSRPASEIHDLVRGLNPAPGAWSTFRDARVKVHATTPAAGSDLGPGEIDGDAELLVGTGDGNLRLDEVQPAGKKRMDGSEMKRGMRPEPGERLQ | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A1M6RUW9 | MFYPLMIDLNDKIVCVVGAGGVALRKTTKFLEYGATVKVIGREIKEEFSELKSKYEGRLQILKGDFKEEYLQGVFMAEIATNDCNINERVATMCKDRNILCSVADNIKKCDYIVPSTVKRGSLIFSISTLGKSPSLCAKVRKELEEKYPESMADFVELLGQGRELVLNKIQNAEERRSILNKMVYMDFEELKKVVDQLKG | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 200
Sequence Mass (Da): 22697
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A0A0F2J685 | MIIIKTSDEIKKMAQASRIVSIVLKELENYIKPGITTKDIESFADGIVAKEGGKSAFKNYRGYPANLCASVNNEIVHGIPSKKKILKEGDIIGIDLGVVYKGYIGDAAKTYPVGKIAEKASRLIKITKESLLRGIEMARPNKRVSDISNAIQTYVEANGYSVVRNFVGHGVGKDLHEEPQIPNFGLPNKGPRLKEGMALAIEPMVNEGGYDVNILNDGWTAVTADGSLSAHFEHTVIVTKNDPLILTKHD | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A0A2U2AKD8 | MGNIRKAAAVGQSVWFDNIERKMLGHDGELARMIKKEGLLGVTSNPAIFEKAIAGGEAYLPIIQDPNNHELSARELFFKLAIEDIQAACDLFLPTYEESRYRDGYVSLEVSPDLAHDANGTIIEAKALWEEIDRPNLMIKVPATKAGLIAIEALIAEGINVNVTLIFSVKRYSEVLEAFFKGLEARVKVGLPILQIASVASFFISRIDAVIDPQVATKAPHLKGHIAIDNAKMAYQHFLREMEHERVKALLKAGMQPQRLLWASTGVKDPSYSETMYVHHLMGKETVNTMPPKTYSAFLEESITPYPQLESDLEVAKSRL... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A0N1B4A3 | MHPLTQFVLVGRANTPGLGDTLTAIGEWLQGQGGQVCIDADSAASLDVCHLPKIALEDAPGRAQAAIVVGGDGTLLGAARVLAPLGVPLIGINHGRLGFMTDVPLRDWQPALGSLLGGNYSLEARSMFDCQVRRENAGIWSALALNDVVVQRGAAGGMLEFVVRIDGDLVYQQRADALIVSTPTGSTAYAMSAGGPMLHPSLAGITLVPVAPQSLSNRPIVLPADVTLDIEVVAGKEMAAHCDMQTFSTLELGDVVRVTPSSHRLQLLHPPGYDYFATLRRKLHWNLMPS | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A376C5X7 | MPFPLKAKPDFVPRVLSIAGTDPTGGAGLHADLKSIAAAGGYGMGVVTALVSQNTVGVRAVHTPPVDFLVEQLAAVTEDVTIDAVKIGMLGSRELTQAVTSWVQETKPAVVVLDPVMVATSGDRLLDEDAIDAMRDLVAEATVITPNVPELALLSDAPEASDFTELIEQALEFAGKNDVIVIAKTGHLSDEEAGNAVASPDGQVFFSSSPRIHTENTHGTGCSLSAALATRIGGGSAINDALRWTTRWLSESIRFADNLNVGQGHGPIDHGHRARRLEKVALRRMQPVHLNSSFSPETIEGTDTEQTPKELESFFGHSLQ... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A0A662DJH7 | MPEVSSFVSLRPGSRFDALYRTARRRRLGAITVFQAPSDTVLPSVGVVAGRRVGNAVQRNRAKRRLREAAHRVELRSNTAYVVVASPDVLGVEFGELVNWLSAAIVVEDGDRDKEAL | 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... |
A0A7K0RFT6 | MSATATPSPAAQSGESRPPRVAMVGAGQLARMTHRAAIDLGVELTVLAGSPQDAAVRAGARPVFGSSARAEDLRELAEGADVLTFDHEQVPPELLSELAAEGLPLRPGPAAKLLAQDKLHARRELEARGFPVPAFTLATSAAQIDDFAREHGWPLVAKAPRGGYDGRGVTVVGTPADALELLEDEPGGMLLEPLLPIERELAVVVARSVDGEARAYPVAESVQYEAMCREILVPAPITEDLAGQAQELALALTDVPGAVGVIAVELFVVDGGLVINELALRPHNSGHFTIEGADTSQFEQHLRGVLGWPLGSTQLTAPAV... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimid... |
A0A2E1CE51 | MSSKRCLLVLFGGRSAEHNVSCVSARHVIEAADPELYEVVPIGIDKSGNWHLAEKAIEELKTNQLKEKLEPVGPIWNPIVELPKLSSEKNLIVFPLLHGPLGEDGTIQGLLEIIDVPYIGSGVLGSALAMDKIATKEILTHHKIPQALYRNVHSKQFEELDSEGMESLFSMLLKELGSIVFVKPANLGSSIGVSRAHDHDSLKEAIEKAFTYDEWIVVEEAIEGREIELSVLGDLVPQVSPPGEIKPMGDFYDYAEKYENDSAELVDEPNIEANLVVNLQQMAARSFLALRCSGMARVDFFLHPERGPILNEVNTIPGFT... | 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: 360
Sequence Mass (Da): 40... |
A0A971WHZ1 | MREVISLQELKRIAQVSKLELSEEELQGFFEDINNVVSRFEKLNDLDLQDISPTSHLSWSEPPFSSDEPRAGEGGEEVLKGAPQVANGYFVVPRVVDKEEKENEDRRV | 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 ... |
A0A524L373 | FDLEGINSENITYGHRLLAPQKIKISSTQEYFRKIEKNYVIIDPQIRENIIRTDIKRIIKGIHGEEIINEKLLKELVYLVEYPNAILGKYDKKYLKLPKDVLTVVMEKHQKYFPVFKNKDELLPLFIVIINNSKEYASKIKEGNENVLRARLEDAKFFYQEDQKTPLEKKVDKLKNVIFQENLGSLFDKTKRLESLCEYIADVIQIEQKEKQDLLRSANLCKADLVTEMVKEFPELQGIMGKEYAVLSNERKEVAEAIFEHYLPRFSGDILPGTKNGMTLAISDKVDNIVGCFLSGLTPTGSQDPYGLRRQTRGKIAIIL... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 528
Sequence Mass (Da): 61218
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A0A7X7E9Q9 | MITERVQKVLAAWAAEEGWDEMPACILERPADETHGDYATPVCMQMAKPARRAPRVLAEELRGRLLADPAVARAVESIEVAGPGFLNFTLSRAAYREAMLEMLAQGDEIGRGIARPSPRVNLEFVSVNPNGPLHVGHGRYAAYGDALRRLMAFSGMNVATEFYINDYGRQMDRFGRSIAARYAQSFGLDLPVPDDGYQGAYVGDIAAAARAEIGEQYLEALGKAAGERADGGTTATAAGDTAAAAPAEPDDDADDDGSAEGPSDWPDDPAVKEAMSFFRAWGCRAMLDEMREELAGFGVLFDVWFSETTLHESGRLERVV... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 598
Sequence Mass (Da): 65719
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A0A4P5RWA7 | MAIYLAWDFWAVAKGSWYFDPEQLMGFYIFGQLPIEEVLFFVIVPLMVVLTYLALIKLSKPSSKDENSNDLR | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 8380
Location Topology: Multi-pass membrane protein
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A0A537XE27 | MSAPPARGEPRSRAKGAALVFTGVLGALVAVVVLLVIVALVTGVVRAFRQPSESMAPTIKRNQHLITTGLGFPFSSTVHRGDIVVLHPSVGLDRPEQACAISREPADGHPCARALTQQSSSKVIKRVVAVGGDRIRVVAGRVYIDGVASKEPYARTAAGCLGCELPREITVPPGQVFVMGDNRPSSDDSRFWGPVPMGWVIGRKLLVY | 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: 208
Sequence Mass (Da): 22069
Location Topology: Single-pass type II membrane protein
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A0A089LSU6 | MLWNLKIRGKIAVGYFMIVLLLGLFLLIVQGRIKELEKETELLSGHDMHVNELIDKIEKNVLDMETGQRGFALTGNESYLVPYNEGNEDWQENFADLKGMITDATQLENLENIRDNIKLWIEEAGQPVVQNKQQGHDDEVASYFQADTGKAIVDQIRSQSDRFREIEAGKTAERVVELKDRNQELFLTMYVLWTLVALASIIASTMISGGIVRAMKDVIAMIQGISEGRSLKTRLNVSTKDEINDLVETTNRLLDKVEKEQIASERITGMSLKLQEKTDIYSLCDTFLYRLATMLEFQFGAIYVARENEDELTKISAYAG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 899
Sequence Mass (Da): 101196
Location Topology: Multi-pass membrane protein
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A0A3P8WLF8 | MNSFFSLLSVHCATQTVTHGTTSLPGQKLNPENFLPKVHAFSRTLMFASANLTGLASISFPKATTCKCGLSSLPCTDYSDTDKCAAVYFISYCSLTAPGDCAAYLHLGHRRPNMANSGLLPCIYLAFVNSIFFSLALPTVFKRNPMNDRPVFGILTQIVTDDVLKPFGKTFIPASYVKYMESAGSRVMPIRLTHTTEEYEDIFRKINGLLFIGGAVDIETSEFARVAKIFYNLALKANDKGDFFPIWGTCLGMQLLTVLVCGENLLEKTTAENIALPLNLTTEAYSSRMFRDFPEDFMKILTQEPLTGNFHHYGLTVETF... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 434
Sequence Mass (Da): 48838
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A0A2E7UIS1 | MISIEVIKKSRDFLKIISIGRKLSLLGVVIYYSRDSNSENLKIGISIKKKVGSAVVRNKLKRQIKALSRNNAISLSGIVMIMIIKENKLNLNYEFLSRIFDSFINKVKDIRETNEC | 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... |
G3USI5 | SKWDLPVFTLPFNIAVTLYLAATGHYNPFFPTTLIKPSFTTKPQQTHADHIIPKQIKAPSWTLLQSIPVGVGQVYGCENPWTGGIFLVALLISSPLICLHAAIGSTVGMFAALSIATPFDSIYLGLHNYNCALACIAIGGMFYALTWQTHLLALACGMYLIR | Catalytic Activity: urea(in) = urea(out)
Subcellular Location: Cell membrane
Sequence Length: 162
Sequence Mass (Da): 17598
Location Topology: Multi-pass membrane protein
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A0A522TUQ2 | MSSYSEAEAQAYSGSLKVAENDAYVLVASRYNDFITRELIDGVTNGLKFYGASEKNIELVRVPGAMEIPLAAKWLAATGRYCAIICLGSVIRGATTHYEVVVNACSEGVARVGLESGVPTIFGVLTTENIEQAIERSEMTLGNKGHEFAATAIEMVALKRSI | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This ... |
A0A538BPA9 | MVGLVLVSHSHEVAEGVAALARQMGGADLPIATAGGLEATGEEHPVGTDAVRILAALEQVWSEDGVLVLMDLGSAVLSAEMALEFLDPDRRGKVRLSGAPFVEGAVSAAVAAKLGRPLDEVAEEALGGLAGKTAHLGVGSQGTEAGSLPASDEPAGPEVRLPIVIDLPHGLHARPAARLVRTAGAFDADMRVTNVTGPGDHRADGTRERPGRRGSDRRHPRLARDRRRTRAPPPRSRPPGPAWGHGDAGGRALASGRGDRRGSR | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
A0A2E5EWQ6 | MSVGSIAMGGALGALLRVYISHWLIKVTSVGFPWGTFGVNMLGCLLIGACWAHFQDVARSELWVLFIMMGFLGAFTTFSTFGLEMLRLWQTQQVLVAILYLLSSNILGLMAVGLGYWARQLF | 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): 13470
Location Topology: Multi-pass membrane protein
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F3LID1 | MVNKWFAAILGFLVPPLAFLYLAKLRVAALYFVLLVTSGISDFYLAPAIGFSFLALLLSVLATIHAFILAKTVEYKEERKWYSNWWGALSIPISMFALIFLTRSFVAEPFSIPSESMSPSLEAGDYVAVKKWGYGLYGSFGITLISQKVENRTPLSRGEIAVVIPPHDPRPFVERVIGVSGDVIEFRDKQLIINGNPIETKTLENGIVNEVFGENISTVKYINDNSRLRSGIWTVPDGYYFVMGDNRDNSADSRVWGMVPAENVVGRVFTKW | 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: 272
Sequence Mass (Da): 30433
Location Topology: Multi-pass membrane protein
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A0A8S0HD97 | MPEYVNWLRHASPYINAHRDCTFVVMLPGDGVEHPNFGNIVHDLVLLHSLGVRLVLVHGSRPQIEARLAARGLTPHYHHGLRITDAATLECVIDAVGQLRIAIEARLSMDMASSPMQGSRLRVASGNLVTARPIGVLEGVDYHHTGEVRRVDRKGINRLLDERSIVLLSPLGYSPTGETFNLACEDVATRAAIDLGADKLLLFGADPGLLDENGKLVRELRPQQVPAHLQRLGATIRPSCWMPPPRRAAAGSDAAISSATPRTAPC | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 266
Sequence Mass (Da): 28887
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A0A2S7TYK9 | MRLPRKFSISHRSEFARVREHGKSRPGRYLVVSVLRSDELDHFKYGLITTKKVGKAHQRNYFRRVFRSIMQNHGELICDDYYIVTIARWRASEASYEELEREWLKLARKLGVLKTELS | 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... |
A0A7C5DVQ3 | MKDFYPREVKLKRKIERELKFLFESWGYEEIEPPTIEYYATLEKALGEDLKERTFKFINRSGELVCLRPEFTTSVARMLSSRNKKPGLNFRIYYDGKIFRYPSSSFRTESELTQMGIENIGTSSPQDDAEVIALALLSLERAGIGDFEIDIGHAGFFKVLLKRLELSPSRENFVKHLLKKRDFVALKTLVREMTFAGAPLRDLFVELPFLRGRWELVKELEARFAEEKEVLKTLERIEEVLAVLEDYGLSKRVFLNLGVIRDFDYYTGVVFEGFSPQAGHPLLAGGRYDELFPVFGKNVPACGFALFVERLMEVIEKESP... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
A0A7X6NZY5 | MTLALLAAGVFDGFYSVIAGLLNLLYSLTNSYGGAIILLTIIVMIITAPLTLKSTRSMLEMQRHQPEMRRLQAQYKDDRERLNQEMMAFYKENNINPMSGCVPMLIQAPIFIMLYGALRGVGNRDGGAASAIGRVAGELVTNRPFNAWKLTDQVFNPDHLDAGAQLYRDFHTRNEMNFFGVDLAITPIDSLKLGVVTALPFIVLIVLMFVTQLIQNRQIQGRNKNSEVNPQQQMIMKIMPFMLPIFSLALPAGLSLYYFVQGLCRIGLQAYITKQVYEPHHARVAQDTATKKNVVETTGTKKQNTKGVSAPKGSSPKSAQ... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A803XXR7 | FSAFDLSPEDVRVVILGQDPYHGDGQAMGLSFSVPEGVKPPPSLLNIFKEIEREGGRPAAGRTGDLTAWSKQGVLLLNSVLTVAAGQAASHRGWGWELLTDAAIKVLSRGNKPIVFMLWGKDAIAKRSLIDEGKHLVLVSVHPSPLSAYRGFLGNDHFKKANEFMMRHGFAPIDW | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular L... |
A0A7K1C1V6 | MGINIFKDCFGQHERRCELASETELIAALSTIFTVADPKLIVGIGDDGAVIKASTQNLVAATDMAVEGVHFNRRWSNLHDIGAKIAAANLADIFAMGGDPRYLLVSAGLTKDFGIAEIQELAQGIKSEADLVGAAIIGGDISRAEQLVISITALGEVENPIKRAGAKVGDAVIISGLPGKSALGLHQLGKGESNSPYIRAHLKPEVNYQLARKFRNVSAMCDVSDGLLSELNHIATSSEVGIEVDVKAIESIPGFPELSAAAGSNIWEFVLTGGEDHIFVATTSGEIPVGAYTIGRVVAGSEVKVPGIANFSGKGFRHF | 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... |
A0A3A5VK96 | MVVQGRQWRHRQAPLRAFEADWMSKVGLLQFDPTVGDLEQNVLRLSSLATQAKEAGATVGISTELAVCGYPPRDLLMERDFVERSMTAALNMSAPLPVLIGTPIPAEDDRTLPTNGVVRSGPDATSITNDEHGRIVAEKQLLPTYDVFDEARYFAAKNRSGLARSFGGFTLGVTVCEDAWQSAGMTPSSYAQDPIEHIAEWTRQGVDIHATVNLSASPFHTEKFTTRLAVARHAAAVLNHPFLLANQVGGNDDLLFDGRSLVVWPDGRAVVAPSWQEGVLIVDLNDANACTWVGSHANDALSIGSATLMVLEPGDDGSSF... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
EC: 6.3.5.1
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) ... |
A0A803YQ18 | YPFKVSRNNQPHRHYGVTSPISLAPPKDIDYIHTQKLVEVMESFGVFEDEEELNHRLVVLCKLNNLVKEWIFELGESKNLPPSVVENVGGRIFTFGSYRLGVHTKGADIDALCVAPRHVERSDFFQSFFEKLKHQEEIKNLRVSKLFLVDGYFFIELDLLQYFQIICLLFWVLSLRFSSSDACGQLYIKLIGADVSVCKYTTLLLCKITSRMLHVLHIELNS | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 222
Sequence Mass (Da): 25644
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A0A7C2HWN0 | MEGKTKIVATLGPSCRDEDLIQSMIRAGMSVARINASHADSNVIREEMASLREASRKAGREVGAILDLMGPKLRVGEIANNGAVLAEGQDFILTSRQIIGDSRSVSVSNPEIISALKRGNTVLLDDGSLRLEVEEISGSDVLCKVRNGGILRSRKGINLPGVELDLEPLTEKDRRDLGLGLEIGVDCVALSFVRSSRDIAELRRYLRAMGSDMPIMAKIEKREAVADIEAVVREADAVMVARGDLGVEMDLEDIPLLQKRIIAVAARQGKPVITATQMLQSMISSPTPTRAEVTDVANAIFDGSDGVMLSGETAVGRHPV... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 379
Sequence Mass (Da): 41135
|
E3I6E3 | MAQEERDVSLTGLTEGEAKEFHSIFVASFIGFTIVAIIAHVLSWNWRPWARPLADLGDGVQTAALTIVQYLA | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Subcellular Location: Cell inner membrane
Sequence Length: 72
Sequence Mass (Da): 7930
Location Topology: Single-pass type II membrane protein
|
A0A7C3YDF5 | MRLADGDEVIPDYHIHTGFCGHAEGDPREVVERAIALGMPEVGFSEHLPLPPGFPPAQRYADLAMARDDLDRYVSLVHDLAREYRGDIRVLCGAEADYIEAALDHTAGLLAQYPFDYVIGSVHFLGDGLAYDHGDERQRLVAYGVDRVYLESLGLAARAAASGLFQVIGHLDLAKKFGHRPTDAEAVAAAAAAALRAAAAAGVAIELNTAGWRKPVGEAYPAPDLLAAAAALGVRLTFGSDAHRPDEVGAGFDRAARLARECGYERAASPLGGEWPLPAPAGAAGAADPGEDA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 293
Sequence Mass (Da): 30797
|
A0A523UZX3 | MEGAKKSFFLNKIGHSGTLDPMACGLMIVLINKATKLSNQFLRLPKEYIATIRFGIETDTLDIKGNIISEKDIGSLSIERINEALEGFRGEIKQVPPMYSALKHNGRPLYKIARSGKSVKRKPRDVEISGIEVRSFDGCVLTVNVKCSSGTYIRSLADDIGKVLGTGAVLSALKRKKIGSFSLKQSIKLEELLDITKLDILSGDKSSLISIEGLLGKNPSIYLREEYGKAIINGKRIELEMIDTGKTDMEKLSRVYKSDSPGFDSMVLIRSFSDELLAVHRMIKEKIFTCGESFKQEFTKSIVIF | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 305
Sequence Mass (Da): 33881
|
A0A1R4EQV9 | MDFFGMLMWPIKWVLEAVLVGFHWLFEWFGMDPASGLVWVLSIASLVLVVRTAMIPLTVKQIKSSRKALEVAPEVKKIQDKYKGKKDSLSREAMNREVMEVYKKAGTNPLASCLPLLVQMPVFLGLVQVLNTANQGVAGVGAMSEVLARQFRASTLFEAVPLHMSLEVGVSEWNWPVIITAVSMTIFMVGAQFYTQLQIMTKNQTPQMKESPMYKQQRMMLYIIPFFLLITAWIFPLATMFYWLVSNVYTLVQQLIIINRMPNPGSEAALAREAKMARKRQRMGLPAVEGEEKQDEEDTVIENLQRKQPRKKGPRSNR | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A7W0ZA57 | MSKLLLVPLEDIVVFPNMSVTLTVDVGPEDRVLLVPRHENDYAGIGTVAEVTDRVRLPGGGRAVALTGLHRGVAGAAESDARGRLRVEVEERPDAEEADGRTRELEREYRATVEEILELRGDDGRISAFVRSITEPGALADTVGYSPDFTFEQKVEVLETIDVNERLELGIRLQKERLAEMQVRRRIREDVESGAQRQQREYILRKQMESIRKELGDDDASLVDEYRRKLDEAELPEAVSEQAERELGRLERQGDNSPEASMIRNYLDTLLGVPWGKRSEERLDPLHTREVLDADHAGLEDVKDRIVEYIAVRKLREERG... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A0A6I3CNJ0 | NLAEAHTDFIFSVIGEELGLLGTLTVIFLFAILIYAIFRVAITTKDIFQKYVVTGIGCWLILQVLVNLMTDVGIVPVIGVTLPFISYGGSSLIANCLALSFVLNVASREPQFKAARVARKAVK | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-... |
A0A8J7CF58 | MYKSFLIDLDGTLYRGEELIQDAPSFLAWLRDEGFSFAILTNNSTRTPQQVAEKLLRMGFYVTAEEIFTSSLATAEYLKTKHAGKRIYPIGEEGLIEALQKAGYSLVDGENPQDVEVVVSGLDREVTYEKLARGALAIRAGAAFIATNGDKALPTERGFLPGAGSLAGLLSITTGVDPTVVGKPSKIIVEMALNRFGFKQKESLIIGDNLHTDILAGKNGGLDTLLLFTGVTTREEAETSTIRPTYSFSSLTEVRQWLMRKG | Cofactor: Divalent metal ions. Mg(2+) is the most effective.
Function: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro.
EC: 3.1.3.-
Sequence Length: 262
Sequence Mass (Da): 28561
|
G2G3K9 | MTLTPGPAAFDRAFRTARAARRAAFAAYYPVGFPTVEQSLVNLQALAQHADVVEVGLPFSDPVLDGPTIQQATRQALDAGFRMKDLFTAVRAIRTATRAAVLVMTYWQPVADQADRFAAELAEAGAAGALIPDLPLEEAGPWLAAARRHGLHAVPLAPPTASDERLARICAAASGMIYAPATSGVTGHTGPLAPDLPAFVDRLRAYTRLPISVGIGISNAEQAHQAAEYADGVVVGSALLRHIQANPGPDGIRAALTLARDLALGVRRLPGAA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-s... |
G2GE79 | MSSLALYRRYRPESFAEVIGQEHVTDPLQQALRNNRVNHAYLFSGPRGCGKTTSARILARCLNCEQGPTPTPCGTCQSCQDLARNGPGSIDVIEIDAASHGGVDDARELREKAFFGPAGSRYKIYIIDEAHMVTSAGFNALLKVVEEPPEHLKFIFATTEPEKVIGTIRSRTHHYPFRLVPPGTLRDYLADVCGREEIPVEDGVLPLVVRAGQGSVRDSMSVMDQLLAGAKEEGVTYAMATSLLGYTDGSLLDSVVESFATGDGAAAFEVVDCVIEGGNDPRRFVADLLERLRDLVILAAVPDAAEKGLFDAPADVLERM... | 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: 466
Seq... |
F3BDB4 | MLIICCLSIVGIAILDLWIKSRVEKKIKRGEEIPVCRGKILLRHVHNEGMALNMLDRYPKAVKWISIVMTGIVAVYALCLFGKHKNGLEKISLSFLIGGAVSNLYDRIKRKYVVDYIGFKTKWKKLTDITFNIGDFSIFAGAIGFILSGFKK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
EC: 3.4.23.36
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) an... |
A5D505 | MTCEFISGGVTAAAGFLAGTACAAIKKKDKRDIAVVYSTVPAAAAGVFTLNLVKAAPVLVSMKRVAGGRAQAVVVNSGNANACNGEQGMRDALAMAAEAAGVLGIPEEYVLVASTGVIGQKMPMDRVLPGIREAAGRVSAGGGHLAAQAIMTTDTYPKEAAVRLELGGKTVTVGGMAKGSGMIHPNMATLLCFFTTDAAISPACLGQALKYAVDRSFNMITVDGDTSTNDMAVILANGLAGNEPIEGGGPDYEAFRDALGEVCTRLAVAVARDGEGATRLIQVEVLNAATEEDARLAARAVAGSSLVKAAVFGRDANWGR... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A367I4H9 | MTKLILIRHGQSVWNAANRFTGWTDVELSPKGEDEAAAAGEELAEVRFDVVHTSALMRAQRTAEIVMKHNRASGNPNSVPTHRDERLNERHYGDLQGLSKAETAEIHGAEQVHIWRRSFDIPPPGGESLEMTAERTIPYFLEEIIPDLEAGKNVLVAAHGNSLRSIVMRIEEISPEDITSLEIPTGVPMHYEFTNGEISRID | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.11
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 202
Sequence Mass (Da): 22557
|
A0A971WHW6 | MIAIVDYEIGNLYSIFKALERLGEEVVVTNQAQEIREAEAVVLPGVGSFEKAMENLEKKEIKEVIKENQEDGKPFLGINLGLQLLFEKSQEAPRKKGLSLLPGEVVKLPPTNKIPHMGWNRVYFKKNSPLTRDIPQGRFFYFAHSFYVLPEEPQAVVGICNYNVVIPAIVNHDNVWGFQFHPEKSSVWGMKVLENWVRSWKK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A2M7JLL1 | MMNEGRLEDVMTATVLPWAAEMGVELDTEQLRRLEIHLDTLWQWNKRMNLTGLSSRDLVVRDLLLDSIAAVRFFPSQGRYLDIGSGGGFPAIPIKILRPALEAYLLDSVQKKVHFLKEAVRLIGLSGCMVIRGRVEKLPTPLLTASYDRVTARAVAKMPQAITWSAPMVKAGGVLVCFQGAECDSEILSARDTIEANGLCLEKVFEYRIPGKPSPRSIVILKKET | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 24979
|
A0A4D6XZ00 | MTYVLFLKIIFNFFNNLNKIGYFMKFSESWFREWIDPKINTSTLCNQLTEIGFEANIYNPLFFNTFHNIITGKIINELKIKKKSKLNFFTVDIGSNKSIIVYGILDTTSIGKIVAIATEKSILPNKLVIKKTLITKNIYSEGKICTFLDLGINISQKEVIEISSKYPLGLDIKEFFSHFFPIINISSTPNRSYGLSLLTLAKEIAVVNNLKLPFIKIKHTTKNQKNKINIKIEENLQHLVTYCGRKIKNINLKKETPYWLKERLRFAEILPGKNILDNIINYVYIELGQPVHIIDSSLIKNELFIRHPKEKEIKNLYTKK... | 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: 824
Sequence Mass (Da): 96165
|
A0A7K0PBV0 | MSIIDDIVDRTKVEVKKRRKELPEKELRKRLEGREDGRPFAEALASQPGVSVIAEHKRRAPSASEPLREGAVLSDIVSAYERAGATALSVLTDGPFFGGDLEDLAAARAASRLPILRKDFIVHPYQVVETAVSGADAMLLIVAALEDDKLLKLYREAHELDLDVLVEVHDEEELERALEIVDADLIGINNRNLKDLTVDLDTTFELLSQIPAGKIVVSESGISHRDQLEELERVGVDAVLVGSHLMRQPDVEAGVRELLGTD | 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: 262
Sequence Mass (Da): 28808
|
T0APJ0 | MRLSIYRYNPESDAAPRMQDYDIALGGHDKKLLDVLMRIRETDDSLSFRRSCREGVCGSDAMNINGRNGLACITAVSDLKEPVVLRPLPGFPVIRDLIVDMTQFFTHYNSIKPYLINDQIPPERERLQSPEQRERLNGLYECILCACCSAFCPSYWWNPSKFVGPAGLLQAYRFITDSRDTATRERLAYLDDVYRLYRCRTIMNCTEVCPKGLSPSHAIEQIRVALLRESS | Cofactor: Binds 1 [2Fe-2S] cluster.
EC: 1.3.5.1
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Sequence Length: 231
Sequence Mass (Da): 26483
|
A0A5C7P688 | MLAAAEDADLDRAARLLADGGVVALPTETVYGLAADATTPAAVGRVFAVKGRPSDHPLIVHLADAAEADRWAAQIHPRLRELAAEHWPGPLTIVVPKQLWVSAGITGGQETVALRVPDQGATRSVIQRLGELTGRAPGVVAPSANRFGAVSPTAAEHVLASLGAFLGAGDAVLDAGECPVGVESTIVAWDVGAGAPRVLRPGAVTVPDAVPSAAGRPGPSQEVPRVPGALAAHYSPRARVLLVGADGALPSLDRAGLVALAGVATPPGWLRLAAPGDAAAYARVLYAALRSADDAGRAVVVAVPPAVGPLAPAVLDRLQR... | 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... |
A0A7W1QQ71 | MGERIAVLVSGNGTNLQALLDDPFCGPRISLVLADRAGIRALERAEARGVETLVIEPSSFADRGSFDEAVAGALQRHGADVVVTAGYMRLLGPAVLDVYGGRWLNTHPALLPSFPGMHGVRDALEHGVKVTGVSVFLVDEGIDTGPIVLQEAVEVREDDDWRSLESKILEVEHRLLPAAVRALVEGRLVVEGRHVSIGGGDR | 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... |
Q9KDQ7 | MKRGRDIQILLLWLMLITIGFALVASALLKAPYYTKDYFDSNEFAEEMDDFWGYFYLYEIIETNKAELLANLEVTEDEINEHRYRYGTLAEQVANIHAQYEEQIQLARLEENEDLAQFYENERDEKIKDITLNFESDEHVKKKILKEKEARFDELFQRLERDRTLYDNYKQSIYYVLKDRNTEKTFWNLSSDQTWEEMKEDERFLYETSVKGTEDDHPVMPETYRFEHHFYDFLHGDYVMDDEYVDMDYYLEALTGDLSYPILEGKLAIASEREGNRFVSNYEYYQSQQQRMIYEGGIGFVLLLAGLWFSLKKAPIRALR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 750
Sequence Mass (Da): 87284
Location Topology: Multi-pass membrane protein
|
A0A803XXL7 | MRVVEHASSSSQFFFSFQITERIIVLFVVINSQEEVQGKYIVCVLFFLWNLLDVVRYTYNMLARMEIHYLPLTWLNFSLCILLYPLSVLAKAFAICVSLPYFETFGTYSVKLPFPFAFSVYFPYVLKMYLLVLFTGMCFIIRNLFSERKAHLETGNSKKKRS | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
A0A358SJI4 | MHWLGNIAGRLYRGEVSFDFVGRQKLWYMISGVILLVSVVALLVRGLDYSVDFKGGSEFEFSAPGASTSQILSTVVAAGGGADASIQSVKPPGKAPLWEVQTNRIPQTTAQHVADALAAKYHLSPNAISVTFIGPSWGSQISQKALKGLIAFLIVIVIYLSIAFEWRMASAALVALVHDIVITIGVYALTGFQVSPATVIGLLTILGYSLYDTVVVFDKVRENTAGILGTRRTTYSQAANLALNQTLVRSINTSLIALLPVTAILVVSVTLLGNGELKDLSLVLFIGMLSGTYSSICIATPVLADLKERQPQYKQLARQV... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 420
Sequence Mass (Da): 43951
Location... |
K0P5N2 | MEKDYYNILGVERNATAEDIKKAYRKIAMQYHPDKNPGNKAAEEKFKAATEAYDVLSNPEKKHQYDQFGTSGYQGGSRSYDDDIFEGDLNDLFQDSPFGSFFNSGRRTRRTANRGEDLRIRIKLNLEEVALGTEKKIKVKRYTSCAACGGNGAENGLSVEKCVPCKGQGVVRKTTQTMLGNMLTEAICSHCTGTGSRIKTYCSDCQGEGRKFIEDLITFKVPKGVKKDMELTLRGKGNAPLRGGTSGSLIVQIDEEENDLLKRKGNNICYTLHVSFIDVTLGCEMEVPTIYGKVRLKIPPGTSSSEVFKLKGKGITDING... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
S7PZ54 | MRHAGTPIAIVTAYDFPTGRACDLYGADMTLCGDSLGQVCLGYDSTTRLTMDEMVHHCRAVSRGSKNPFLIADMPFGAYYTSPEDALRNAIRLVQDGGAEGVKMEGGEELAPTVRKLTSVGIPVIVHMGLTPQRHTSLSGYRVQGKDAQSALSVLRTALTLESAGAFSILLEAIPHLLATHITNRLSVPTIGIGAGPGTNGQVLVWDDLMGTWHGHKAKFARRFADGQAEEKKGVTCFVIAVKERSFPDLTSESYEMAQSEWERFLEAEKS | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
EC: 2.1.2.11
Catalytic Activity... |
A0A3P8WZ63 | IFRPFDIFILLAIFANCVAMGVTKPYPDDDSNPTNHQLEQVEYVFLVIFTIETFTKILAYGLVMHPSAYIRSGWNLLDFVIVIVLFSVIAEAMTDHKPGEAHHAAGKPGGLDVKALRAFRVLRPLRLVSGVPLQIVLNSIMKAMVPLLHIGMLVMFVIIIYAIIGLELFIGRMHKTCYYTSTLMVEDDPSPCAFAGSGRFCVDNGTECRGKWEGPNGGITNFDNVFFAILTVFQCITMEGWTDVLYWMNDAIGFEIPWIYFVSLVIFGSFFIINLVLGVLSREFSKEREKAVARGELQKAQESKQMEEDMVGYMDWLIEA... | Function: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death.
Subcellular Locat... |
A0A369R489 | MQPQAAGPQGDGAPPAGAILAGGAGRRMGGTVKAGLRLGGETLLARAARRLAPQVPALAVCAGPDPARLAGLLPPGAASLADPLPGYEGPLAALSAALDWAEAEGHADLLTVAVDTPFFPADLATRLAAGRGAAAAALAEDGNGLHPTFGLWRSALAAPLRAALAGGARRMTGFADRSGAVRVRFPGDDTFFNVNAPDDLALAEARL | 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... |
A0A6G0A1S0 | MNIAWFHCFSGIAGDMALGALLDAGADLDEVRSLIERLPVGGWELAVEPVMRGGIGGVKVSVLTEPTTVVRTFAHIEGLIEEARLPERVRLRAIGTFKALAEAEGRLHRWPVEQVHFHEVGALDSIVDIVGACAALEVLHVERICCSPIVNGRGMIKSAHGLIPNPPPAVVALLEGAPTVGVEVDAELTTPTGAALMAANVHEWGPLPAMRVQASGFGAGSRELADQPNLTQVVLGEEVAELAAGQPVVLLEVNVDDATGEVLADSISELLEAGAHDAWVTPIVMKKGRPAHTVSALADLALAAQVAATLRTSTGSLGVR... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A5C7PES6 | MADAQDDGQSGSGLRFRLFGMPVRVPLSGLAGVALVAWLWTPTFSVAGSGVWAAIVFALGLYASILAHELAHGLTARGLGHGVRGITLWILGGFTVYERAGLTAMREGLIAASGPLTTLGVAGLCELGANLLLGQVPGVVVVVLKALAWTNLLLGILNLLPGLPLDGGGIVRAAVWGLTGSEYRGTVVAAWFGRIIALVCVGVPLGLALGGRLDLVNVLVACVFGVFVWVGATASLRAATFEAKIPGLQAGALARRAVPARGPESLALAEQRMTQAQAGAIVVVDDDGRPTGVVDATAAAATPADRRPWVTVGALATPLP... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 368
Sequence Mass (Da): 37054
Location Topology: Multi-pass membrane protein
|
A0A538IL77 | MLAEIGPLEIVGIVLLVIILFGAKKLPEIGKGLGKGLREFRDATKGLTDDEKSQPEDKPAVPPAKDDRGAGPAAGA | 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: 76
Sequenc... |
G2G614 | MARPGAATLRSWAAASSGGLLLYASFPPVGWWFLAPLGPALLILAVRGRRARSAFAAGGIFGIAFLAPLIVWLANLGLVPWLTLTAIQAIVFALAAMPLPRLIALPGWPLYTAAWWVALEAVRGRAPLGGFPWGRLAFGQADAPYADWAAVGGGPALSFAVAFLGSLLVYGLTEWRGGRRHISAAVCLGMATLIATPLALPAPGTSGPSAVVAVVQGNVERERTLQEQARVRNVAQNHARETKALADAVRRGEVPRPDVVLWPENSLDGDPGRDPELGSLVADSVRELDSPLLIGAMLEAPRARAYNAGQLWLPGQGPVS... | 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... |
A0A7X7JCP6 | MAKNTATKVGSKSRTGLGAAVSRARSQQAVAKSGQAQAPRGNRLRRYLREVKVEMGKVTWPNRTEVGQATSVVIVAVVIASAYIGVLDVIWSNIVRLVRLG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 101
Sequence Mass (Da): 10832
Location Topology: Single-pass membrane protein
|
A0A432HUH6 | MYTLEIREDTIRIPAEYIREGHSLSQHVDQLAHSAFEGRFDDDGNFILVTFDHEMLGRGRIIHGDGAIYQRVRFKALLFHMDSNEVVDGAVSEVHEFGAFVQIGPVEALLHKSQILDEQVNINMGQGRIEGARSGRFLELGSPVRARIVTISLNPHDPRSSKIGLTCKQTGLGAHDWLTEDREE | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 184
Domain: Forms 2 dom... |
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