ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2E4W1W8 | MNECFVVIAGGGTAGHVHPGLAVANALARGGYRKEEILFVGSDRGIEQDLVPSEGFELITISGTGISRRNPLAALRAIYLLIRGTMEALRLLNKRKPQVVLALGGFACFPCALASLVLKIPVVAHEQNAVPGLANKVISRWARHSAVSYKDTSLRNAVYTGNPVRQSIIDARRIEPACIREKLKVPSENLFVVVTGGSLGAKKINLALRDAIPLLDKGMGLTVYHIIGRRDWEELFRSEEELRNYVDYRPIEFEYDMPSILRSADLIISRAGGSITAEIAALDLPSVLVPLPNAPGDHQTANAKSMVDLGSARILTDENC... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A523V2J3 | MNKDKVRELFDSISGKYDITNSIISLGLESIWRRQFLRKINSSDNRILDICCGTGTSTYQIWLKNRNAMVTGIDFSDGMIDIAKSKYRENINLLFYSSDASNLDFADNAFDCITIVFGIRNIFKREKALKEFYRVIKKSGRIIILEFNYIEKGFFGYLFKFYLSRIMPFVGGFITGDRWAYRYLAGTIKEFPELKKFKRLMENAGWESVQHLPLTMNICNVYTGYKI | 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... |
A0A537YD62 | MLPSRPPGLTATPSRRSCWPTSRPGSSGRGTVPDTRGRTSRHTWPPSAPSIAGCTRKRWPGSRGTLCPECTYHFRLPARERLKQLVDRESFHELSATIEAADVLGFVDSRPYPARLEEARRKTGNREAALYGPATIGERPLVVVALDFPFMGGSMGGAVGEIVVRAAELALSSRVPLLAISASGGARMQEGCISLMQLAKTSQAIARLHEEGILCLCLNTDPTFGGVTASFAMLGDILIAEPSSHIGFAGPQVIAQTIHQELPAGFQTAEFLLQHGMLDLVEPRENLRNVIGKMLRFHGVRDARGLPTAEAQAPLTDPRQ... | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase ... |
E3HZ27 | MNIVIVESAAKAKTINKYLGADYKVIASYGHVRDLPAKDGSVLPDNDFEMTWEVEADSNRIVNEIAKAVKGADRLILATDPDREGEAISWHLLKILEQKRALNGVSVERVAFNAVTKDAILTAMKNPRKIDEPLVDAYLARRALDYLVGFTLSPVLWRKLPGARSAGRVQSVALRLVVDREAEIEAFRTREYWTVEAALKNGGGDAFTARLVARAGKKLDKFDIPNEALAHAYRDAIKGQSYRVDSVDAKDHKRNPAPPFTTSSLQQEASRKLGLSPRQTMQIAQKLYEGIDIGGETVGLITYMRTDGVQIVGEAIAQAR... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A7V3CRA0 | MDALLTLRIVAALVAAYFIGAIPWALIVGKRFYGIDPRTVGSGNLGATNVFRALGARAGAATLLLDAAKGAVAVVVAWLLVPEAMYPVAHGWAGVSAMLAAVMGHSYSPYIGFKGGKGVATSAGALFVLTPLAALLELLIFIGVVSVSRMVSLGSIIIAVIYPPLVFWLYPDDTPVQVVVTVLAVLVLWRHRSNMVRIVRGEENRISWSRKGSATKGKDVS | 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... |
A0A538A5L6 | MAGARRARLWRRARPDRVSHGRRDGRRPRHHRGLAPQPRLRPVKVSEIREAYLSFFEQRGHLRVPSGSLIPAPEDTSTLLTIAGMQPFKPYFRGDEQPPSNRLTSCQKVFRTPDIDEVGNTLRHLTFFEMLGNWSFGDYFKDQSIAWGLELSIEVFGLERESIWATVFGGDDELGLGPDEESIEIWKRRGIPEERIVLLPRSENFWQAGETGPCGPCSEMYLDRGPEFGGADERPGDDTDRFLEYWNHVFMSYELHEDGSLTKLPANNVDTGMGLERMAVVLQGVESVFQTDSFQPLIDLAQEMSGRSYGDDHATTRAMR... | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Al... |
A0A380P1F3 | MKCKKTAEIADLVHAQDKQLEAEVGTIGGEEDGVIADGEIASLDDTLKMAETGVDSLAVGIGNIHGKYPADWKGLHLDHLKAITDMLSEKLGRDLPLVLHGGSGIPDDQIQEAIKLGIAKVNVNTKGQLAFHTAIRDFVLSDKDLQGKNYDPRKFLQPGSEAIQAMCEDRIKVFGSQIKHNGRACTHVYTLFVSKASCIS | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 200
Sequence Mass (Da): 21605
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A0A4D6XRE2 | MKKKTTLPIIIGNWKLNGTKNKLNSFFKFIKDKSLKIKKNLTILALPNIYLNYAQELVSKLNINCKISAQNIDIHKQGPYTGETSVNMLSDINIKYTIIGHAERRYYHSENNDIIAKKFILSKQKGIIPILCLGENQLEKDCGKTEEIILSQLNAIASIDKQNKTIFNNSIIAYEPIWSIGSKKSADPDLIQQLHTFIKNYVIKFQNFNIDNFYIIYGGSVNEENVNEFLNKKNVDGCLIGNASLNKKIFNNILVKSNKIDK | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A3D3DDQ7 | MVNWGISQLVNYHISKVRIKYMFYYVARAIGWLLLKIFWRMEVIGVENIPERGGVIIASNHVSYLDPIVLGVSTKRKIYFIAKKEVFNNIFGSIILRGLNAFPVDRKKVDMFAFKKTISILEGGGALGIFPEGTRSLNGELQELKSGVVKIAMKAGVPIIPVGIIGTHKIYPHGKIFPTLFKNKITVYFGAPQYFDKHNIKDKTYQKEALNIISQKIKELTVIDHN | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 226
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A4D6XVJ6 | MENSFLFTHEVKNHKFLKKINSFVCRRRKIKERHELEIKKYWSLIGMMYTKNFVNLNKFFINEYPLVLEIGFGTGISLVETARRKKNNNYLGIEVYFPGILQCARIIYSLGLKNLRIIYYDATEVFENMIEDFSIERIQIFFPDPWPKNKHKKRRLLNRQFIILLLQKLKRGGDLCISTDCKDYSDDIVKTLSSIKNYLNITILYDSSNKLFFCPTTVFEKKSKLLGKINFYILCKKL | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 238
S... |
A0A3A4WME0 | MEFYSEKIRVGGKEITVETGHLARQADAAVTMRCGDTIVLVTAVASNEPRDVDFFPLTIDVEEKMYAAGKIPGGFIKREGRPSEKSILTARLIDRPLRPSFAEGFRNETQVIATVLSVDQMNPPDVLALVGASTALTISDIPFEGPIGGVRVGRVDGEWLINPTFQELERSDIDLVVAGTRDAILMVEAGASEVPEEEILEGFEIAQAANRELVEFQERLREIAGVPKREVVLAEPDTELEGRVRAAAAERLSEALRNADKLAREAAVAAVRQDVVTALAGEEGPSQADITKILYKLEKELMRRMILKEGIRVDGRKTDE... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
EC: 2.7.7.8
Subcellular Location: Cytoplasm
Sequence Length: 721
Sequence Mass (Da): 78... |
A0A7K1D7C6 | MSDNSILVIKGALKDYAWGKVNGLQNWVAKTDQPQAELWFGDHPSGKSINKKTNKELSTNANFPLLIKLLCANEPLSIQVHPDKQTAESGMSDFEDSEKILSDDNGKDEMLFALEEFQAFAGVESKAKRDVVFKILFEKTNAKELQEVLATDTFFDAADIIFEIDKTKISQINKEVVDCVKKANYPAKAISTFEKIVIKYPNDPGVLVCLLMQFHVLEKGHAIHVSPGTPHSYVQGLAVEVMTTSDNVLRMGLTNKYVNIDAALSLVEEKQIQVLSLPTNDGVHVYKPESDFELVAVDNATYQSRDTKFAGVLNLEGETK... | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 357
Sequence Mass (Da): 39356
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A0A2G8LA43 | MATSSVDKLKEAEQRHGLSGPGTIYPSVPAYEELQVMSTPNQQSSGCCGAPHWKEPPQSSYSEIEDYYELKQHVSVDFQATFRAPESRGAVEAVTKFNRLVFHWTKRCLYFLFTCLLGPVMALSFGMLFGIMDFLFIWMMNPITRIVHVLTRFISDVHRPLIRVSLDPIFESIGQTLRIRNSGKFTERKYKLDVTGINFNGAGATVPMLEDA | Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Location: Cell membrane
Sequence Length: 212
Sequence Mass (Da): 23992
Location Topology: Peripheral membrane protein
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A0A1V5G0G4 | MDATIAILLGGLDLMQWIERVLWVSLRTGGLLMLSPFLGTQAVPKRVRLILALALSLAFAPLIPAPALSAALDAATFLAVARELAIGAALGFLLRIAVEATAMAGELVAQGMGLSFAQMIDPMRGTQSGVMTQWFMIIAGLLFFALDTHIALLRVLIGSFQALPPAATPASMSNLLDTVPAFSGIIFATGVSLALPAIIAMLALNIAFGVMSRTAPSLNPIAIGLPAALLAGLVLLIGLVPYLLEPIRALFESALLTASQMVR | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 263
Sequence Mass (Da): 27394
Location Topology: Multi-pass membrane protein
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A0A7K1DYE7 | MRASFSSAEPQSPIRGVGRVLVACYGILALAALGRSVFQIITKFDSAPLAYVLSAVAAAVYVLITVLLLVDRPWARVTTWIAISIELVGVLVVGAVSLVDPGLFPSDTVWSVFGRGYLFIPLVLPVIGLWWLARTRVRASVVTIGKFDGLHIGHMELIRESVEIAQDERLRSVVVTFDRNPQEVLAPSDAPVKIAATTARNRKLRAAGVDHVEELRFNESLANLTPEDFVDAVLVKRLHARVVVVGSDFKFGHNASGTVETLRALGAQRGVRIVVAEDVLVDSRRVSSTWIREALEAGDIELAARLLGAFPVVLGEVVHG... | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.1.26
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 437
Sequence Mass (Da): 47557
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A0A3P8WVL3 | MKVFVTSVFVCVLISRINCDGNSVDWCYHLPTCDDSTWPDIATDYCAGSRQSPINIDKSAAAPDSSLSPFNFVNFNSKSSLKSIKNTGKTVKVSFDSGVKISGGGLSEEYDSLQFHLHWGNGASTPGSEHTVDGKRYPMELHIVNMKSSYNGDISLGLADSTGLAALGFFIQGSSAPANQPRSWRNLASYLSKITKGGDSVEMRPGISLDDLLEGVDRTKYYRYLGSLTTPSCNEAVVWTVFKEPIEISEELIELFSNTLHVSDSSSPFMRNVYRNIQQDQPVTTQP | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 287
Sequence Mass (Da): 31451
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A0A523VG96 | MIEPKEALDIILNNVKSLPAKKVFLEKGLGHVLVNDIKAKIEVPLFDNSAMDGFAIHKQDLGTKNCLKVIGEVKAGQKTSKVASKGKAISIMTGAPVPKGAAAVIPIENVDEDKKKKTIDIKSAANDRDNIRNKGEDIKKGSVLIKKGTILKPIHIALAASVGVSEVKVFEKPKVSIVVTGNELKRPGTILKAGELYDSNSFLLKSLLLKNNFDVAYVAKTKDNLDKTIRTIRKAIEKADVVLTTGGISVGKYDFVSLALEKIGAKRFFNKVKQKPGKPLSFFTYQNKAIISLPGNPVAVATCFEIYAKPMLKKMSGTND... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 402
Sequence Mass (Da):... |
A0A0S8B239 | MRVARFFVDPPLETGARLALPERAAHHAARVLRLRVGDPLTLFDGRGGEYAATLVERTREEISVEVGAWHEVEREAPLGIVLAQGISSAERMDLTVQKAVELGVAAIQPLDCEKSVVRLDARRAESRRAHWQRVVVAACEQCGRNRLPEVRPPLRVSALCESTPAAPAKWLLAPEAPTRLRDVAHAIGKGLVMAAGPEAGFSAAETRALLDAGYMPVRLGPRILRTETAALAALAALNAIAGDG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A523VKB5 | MHFLVRNKYGGLLTEKEIGKEVIINGWVNKRRDHGGLIFLDIRDRSGIVQVVFDPGEKESFKLAQKVRSEYVLAVKGKVRKRPKGTQNPQLKTGNIEIEVKEMQVLNKSAALPFELGEADKVSEKLRLKYRFLDLRRKRMKGILELRHKVVKTVRGFLDENGFREIETPYLTKSTPEGARDFLVPSRLTPHTFYALPQSPQLFKQILMVCGFERYYQLARAFRDEDLRSDRQPEHTQIDIEMAFITEEDIIKLAQSLMLKTFEIIGVKASFEEMKYDEVIERYGSDKPDVRYDLKIFDVSKVFRNSEFKVFSQAVAKKGS... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
A0A538IRC8 | MGGDIARLFVALALPAAVKEELARAIEVLGSRVAGARWVPKENLHLTLAFLGRVEDDRVADVSGAVAAAVEGHVEFTVRLGSLGAFPSAKRARVVWLGLDDPTRGLAGVADSVGEAREKLGFPREARAFTPHLTLARVKTPAPVSLDATVRPIAFPVQRIGLFESRLGRPHAVYNELATFPFRRGS | 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: 186
Sequence Mass (Da): 19909
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A0A2M7TTG2 | MHFDIITLDPEMFESPFGAGIIGRAIKNKKIKIKFHQMRQWAWNNYGAVDDKPYGGGVGMLIRVDVIDKAIKTLCPYRDISLEKGDLKPKIILTGAKGKRFTQKDAYRLSKEKNIIIICGRYEGFDERISKLVDEEISIGDYVLTGGELPAMVMIDSISRLLPGVLGKDESSFDESFSNENEKEYPQYTRPADFEGEKVPEVLLSGDPTKIKEWQEKQKNGWW | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 223
Sequence Mass (Da): 25412
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A0A6I2YNX0 | MRVGIVGAGQLARMLAEAASALGIETVVLAESASEGAAKTATELKIGSPHDRAAMEDLAQSVDVVTFDHELVDLEIIAELESSGVRLSPSSSALLYAVDKAEMRSLLHARGLPCPAFEIIAPGDTSSAKTLGEQFGWPFVIKAARGGYDGKGVFVVQNATEAADVIASLHERNITALIEENVEIVAELAALICRSHDGEIAAWPVVETAQIDGVCREVLIPGSLSEQHRLEGEAIARAVGDVVGVVGIMAVELFVTKDGLLINELAMRPHNSGHWTQDGSVTSQFENHLRAVANLPLGSTEVNARAVASVNIFGTQEGGS... | 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... |
A0A3A4V382 | MKNDIFWMKKAIKLAEKGRGNVSPNPLVGAIVVKDGEMIASGYHQKFGEPHAEIYALSKAIDTKDASLYVTLEPCCHKGKTPPCTELIKKHELKNIIIGSSDPNPIVSGRGVAELKKAGFRVKTSFLEDEIKKQNEAYFKYITSGLPFVTIKSAITLDGKIADNKGFSKWISGSDARAAVQKLRADNDAIMTGIGTVLADDPMLNVRDIKPGSFKPPLRLIIDPKAKLPLDSNIVKTASEVPTIVCVGFISSSKKAALEKAQVEIATFKANNGIFNLKEILAYLAKKDISSILIEAGASLNESALSQGIVDKVVFFIAPK... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A7K0UXQ8 | DYDAVDVVILPPFTDIRSVQTLIDGDRLRLTYGAQDLSPEVSGAFTGDISGSMLNKLGCSYVAVGHSERRAIHKEDDSIVNRKIKAALVNEITPIFCIGEELEIREAGTHVEHVLNQVRNGLKGFHKPDLKKIVFAYEPVWAIGTGKTASAGDAEEVCSAIRAELIKIGSDEIAQSARILYGGSVKSSNIVEIMQQPNVDGVLVGGASLDAEEFAKIAKFHRVGAA | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A7K1A6K6 | MPEQPDPFELFGLEPSTPPAAPQPPTPAEPSSSAAEAQSSLDTPADAPASPAPTGGDDGEYVAIKGGGGGRGGRWALLLGVPLLVVALVIAVAGFWVKGKIDPGSPGEEVAFTITKGATTSQIATSLAEKKIVSSATVFEWYVKWKGGDPFQAGDYEGLRVNSSMGDVVDILKAGPPPPKTVSFLVREGLWVSEFKKIALEKFPTMTPAALDAALANTHPSLQPAGSTNIEGFLFPATYEIAQQDIGNAQKLIDQMVAAFDRVSQSEGLPDATAKLKGVAGAKSISPYEALIVASLVESEAKVDEDRPKIARVIYNRLAR... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 418
Sequence Mass (Da): 44126
Location Topology: Single-pass membrane protein
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A0A7K0KML7 | MSTTSTAIITVDGPSGSGKSSVSRAVARQFGLHYLDTGAMYRALTWAALRHGIDLTDADAIAATADSVQLAWSTDPDESWIRVDDVDVSRAIREQPVTSAVSTVSAEPRTRAVLVALQRRAVSDALAQQRGIVVEGRDIGSVVLPEADLKVWLVADPEVRAARRAAEDVAEGRADAGPGAVPPSGASTSTSTSISTRTSTGTAPAAGMAGSAAPSVAADLARRDAADAGRTASPAMRAHDAVIVDATELTLAEVVAKVVALVRERVGP | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 268
Sequence Mass (Da): 27516
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A0A523V004 | MKEASKKSERKTINDYYLKKKIDLSENAIKVLERRYLKRDEVGNLLEKPREMFVRVARNIASAEKKYEKTEKEILEIEKDFFDMMTDLDFLPNSPTLMNAGKELQQLAACFVLPVGDSMSDIFETLKETALIQKSGGGVGYSFSRIRPRNDIVLSTRGVSSGPISFMTVFNAATDTIKQGGTRRGANMGILRVDHPDILDFITAKDNNEKLTNFNISVGVTETFIRAVENDEKYEIVNPRTKEVFDRYNAREVFSMIVEHAWKNGDPGIIFLDRLNKDNPTPHIGQIESTNPCITGNTLISTNKGWIKAEELHNQIECGE... | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A4P5SXQ3 | MAVGQFRTLAYIAAGGIIGSLGRFGIDVLVAGNLPLTPQDFPISTLVVNVLGCLAIGILAPLLLARSNWTNARPFLITGILGGFTTFSALAVQSGIMLLDGQAWRATIYLLATLAGGLLAVRLGMLISNRQPQ | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 13864
Location Topology: Multi-pass membrane protein
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A0A523SBE6 | MQDQIKKEGKLYPLDTSKLERIPPYNIEAEESLLGAMLISRDAIISVIEVVTAEDFYRKSNQEVFNTVKELYVKGEPADPITVADHLGKRGLLDEVGGKTFVHSLISNIPLAANAEYYAQIVRSNSILRKLIYAATEIATMGYEVPQDLNSTVDKAQQLIFSIYKDLNRGSTRDKVSVMKDIVTEAYELVEVLHEAKSDISGIPTGYIDFDRITSGFQNSDLIVIASRPGMGKTSLVMGMAKHIATREKLPIAIFSLEMSKQQVALRLMSAESRINLQKLRDGKIKDDEWIRLARAVEKLAECKIYIDDTAFLTVMDLRS... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 470
Sequence Mass (Da): 53091
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A0A7K0A9C3 | MLARAFGEVRANHGAPGVDGISIDDIEEFGVEGFLDDIARALKDRTYRPQPLRRVEIPKAEPGQVRVLGIPTVRDRTVMTAAKLVLEPIWEADFLPVSFGYRPGRSTHDALEATRVEANRGADWVLEADVSDAFGKLDHDALMAQVARRVCDRQMLKLIRSWLRAGVLEGGVVTDTGSGTPQGSPISPLLCNIALHVLDEEWTRQGRALGKLVRYADDAVALCATRERAEEAWRRMAAVLRPLGLELNPDKTKIVCLTKGRQGLDFLGYHLHKLQSWRGKGRWYLQRWPSARNMAAVRAKIRSVTHRRFVGFTVEAVVDG... | Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be i... |
A0A6I3FBR1 | MHLQLAHLAVAHYPGTWRADDAELVEHRLGAQFLNDADHAVGDDDTTEQRIFRRSGNDHHRRQDADHEVDRGDDVAADDLADRARGRCWNGVGETPRDSVGNFGAREAGARVGDEAGHGCDVRRSRNQATTRVGSVLVIGLTGGIGSGKSTVAGLLADCGAVVLDVDAVGREVIAPGGLAEADVLAEFGVGVADAAGHVDRAALGRAVFGQPEALARLTAISHPAINTELAARLAALPVASLVVLDMAILVESNLGKLPDGNGYTKVVVVEAPTELRVDRAVARGMSADDVRARIAAQASDAQRRAVADVVLTNDGDRDR... | 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... |
A0A0F2J4A4 | MKNKIYLLLFLLLISSCVSSQSRNDTISQVSTISALMDGIYDGSVTYEELSKLGDFGLGTFQQLDGEMAAIDGVFYQIKHNGAVNTVNPSMRTPFAVVAFFDEDIGKTIKTTMSYKQTRDYITSILPSANFLYAIKIKGTFDNIKVRSVPAQDKPYPDLTTALKQQNVFDYTNIKGTLIGFWFPDYMKSLNVSGYHFHFLSDDKKIGGHVLDFTIKEGQFIIDQSGKFQMIMSDVEALK | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 239
Sequence Mass (Da): 26822
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A0A7C5DVY2 | RGANMGVLRFNHPDILEFIQAKKRGGEFENFNLSVAITNQEMEAVKKKQKFPLVNPRDGKVWREISASEIFNAICESAWSSGEPGCIFIDEINRKHPLKELGTIEATNPCGEVPLLPYESCNLGSINLAHMVTEGKIDYPKLGKTVHTAVHFLDNVIDANHHPLPETNQMAKANRKIGLGVMGFADLLVKIGIPYYSKQALKIAEEVMQYIMLQARRASMELASRRGTFPNFEKSTWHSQNLPLRNATLTSIAPTGSISIIAGCSNSIEPYFALSFRRYVLENTELIEVNPLLEDYLRELKLSQKDWEKILTQGTLQNME... | 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... |
Q0ABC1 | MDEETPATTRHRVFFALWPDEALRDGLARLARSLRGGRPVPRGHLHLTLAFAGLVTAEQVACLQRAAAGVRAPAFTLRLQTLGGFARARVAHVAPDEQDLPPALPELAGQLNRALVACGVPAERRGFRPHVTLRRDARPPRPRSVSLPEWSVDRFVLVESGDRGRPGPYRVLAEWLLQRSTE | 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: 182
Sequence Mass (Da): 20096
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A0A3P8UR39 | MGSGESTTRKVSFGVDDEDRVRILRGVKVIMLIQLSSQGERETALGKIMSLEREQTRQEAEKTKVLAQQLQKKDSQLRALDAFYKEQLAQLEKRNWEEYEHSKERFHEAVSKTESSVRYHSVDPVCLGLQAQILSCYRENKDQTLTCSNLAKEYMQCINAAKKVRILFYPFSRSKIYYGYYDISSCGTLLIYCRQLSVFKHKHIINIYSF | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 210
Sequence Mass (Da)... |
A0A3D1YXS9 | MASPPGMLENAKTGWDKLDINQKMIILMTIILFVVALGSLFYWVSRPSYSVLFSNLSSEDAGAIVAKLQEKKVPYRLNGSSIIEVPSNQVHEARIQLAGEGLPEGGTVGFEIFDQTNFGLSEFAQKLNYRRALEGELGRTISQINEIEGARVHIVLPEPSLYKDKENPATASVVIKPRAGARLADSKVQGIVNLVSKSIEGLKTENITVVDTTGNILNEATGDSSFASGGNYTKTQLGAKEAYEGTLEKSIESMLGTVLGSESNAVVRVSADLDFTQKSTASKIVKQEEEPVVISEEVDKEKYEGQGASPGGIPGVTSQV... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 541
Sequence Mass (Da): 58536
Location Topology: Multi-pass membrane protein
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A0A3D3YWW6 | MYGRGKEATMAGRFGSVVTAMVTPFRDDFSLDLDRAQEIAAYLLDNGSDGLVVAGSTGESPTLTEREKADLFRAVVEAAKGKGKVVCGTGTYSTQESIELTRVAQDAGADGALVVTPYYNRPPQRGLLAHFTAVAESTDLPILLYNIPSRTATLIELDTLLRLAEVPNIVGVKDATADFNTASRLIQQAPDGFELYSGDDWATFAFVCLGGVGVVSVASHVVGERMREMIEL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
EC: 4.3.3.7
Catalytic Activity: L-aspartate 4-semiald... |
F3BDE7 | MIKKVARFVAKWEMLNKADKVVVGVSGGADSVCLLFVLMELQKTIGFDIIVVHVNHLLRGEDAESDEKYVRELCEKYHLTCEVYRENVEWIAKNKRESLEEAGRNVRREAFEQTLKKYGGTKIALAHHRNDNAETLLMNLARGSGLAGLGGMRPVKENRIRPLLCLERKEIEEYLLKRQIAYCTDETNYSDAYTRNRVRNHVIRTLEQGVNEKTVAHFSETMERIWELQDYMEEEAERRYDRVSLEKENKTVLLKEEYEKLPPILRGMVIKKAIVSMTKKEKDIHAVHIEEVQKLMGNQVGRQIHLPYGVCACRCYEGIC... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A3P8UKH7 | MSFSFFFLLLSLALQTGAKLSGDTEVDVDDGHDWDMDNINQAAGLDLLEGDIEQGMPTKNSIQGEEFRWPRTVPYILEDSLDMNAKGVILKAFDQYRLKTCLDFTPWSGEKNYISVFKGSGCFSSVGNQNVGKQRLSIGKNCDRLGTVEHEFLHALGFWHEQSRDDRDDYVTIIWDQIEPGKEHNFRIRDDSESSSLGVPYDYGSVMHYSKTSFNVGSEPTIVTRIPHFRDVIGQRMGFSANDLAKLNRLYNCTQSSTFVDSCDFEEENICGMVAEGENNMWERRSSVSAGPQTDFSHMGQCPGQGHFMHFSTASGDSGK... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 682
Sequence Mass (Da): 76274
Location Topology: Single-pass type I membrane protein
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A0A836TMP4 | MPERQWKNKRRLMKPVNKRKNTRPNTSFKSELKRRFDMWLLQHLQAFIFSLGQFAKYPLSSLLTSAVIGISLALPASFYMLFDNVRFVSSSWDGSVQVTLFLQTEINDEQAATFANKLKDNKNINETTFIKRADALAEYQKLSGFADALNALDENPLPNVILVKPELNNINESDTEALIKELEAMPEVDAAQYDSQWFKRLLYLLDIVNRVIIILSTLLAVGVLLIIGNTIRLSIYNRRAEIEITKLFGGTDSFIQRPFLYSGLWYGAFGGIIAWLLIGISMQLLRGPVKQLANLYASDFQLIGLGFFNSLLLVGTGIAL... | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell inner membrane
Sequence Length: 339
Sequence Mass (Da): 38371
Location Topology: Multi-pass membrane protein
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A0A0R2GYV2 | MKHTQVAIIGAGPVGLFTAFYARLRGLDVTLIDSLENVGGQVNHLYPQKDILDVPGYVKIEGEALIRQLAEQTQQLNPNYMLETTVTDVAYDAVGQTFVLQTNHEALQADRVILAIGHGAFEPKRLPDGIGADLEGEGVYYVVDDLNKFKDQIVLVAGGGDTAVDQALAIAKVAKKVYLTHRRDRFRAMAYTLDQLAVSSIERVTPYNITAISKIADGELEVTLNTSTTEVAQQLMVDSVVVNYGFKSDSQLFEQWRCQPTVARQRCVVQQNMQSSVPGLYAVGDIAGYANKTDLIATGFGEGTIAVNGILQDLEPALAG... | Cofactor: Binds 1 FAD per subunit.
EC: 1.18.1.2
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 338
Sequence Mass (Da): 36668
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A0A523CHQ8 | MTFGAALAELEEIVKALESGQLELEDSLGRYERGVSLLRACRAKLADAQQRVTMLVGEIEDEDAE | 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... |
A0A4P5RCW0 | MAIDLDWLPIAFPHRIWFVLKTLVPRFKGQKLTQLRLLTVHAHPDDEASKGAATVAKYVAEGVEVMIATCTGGERGDVLNPKLKNPENEKQLAEIRKKEMAESIKVLRAKHTWLGFEDSGWPDGEPKPPLPKGCFADISIEEAAKPLIKLIREFKPQVLITYDENGGYPHPDHIRCHEITMFAYENAGRVNKYSDLGFAWQPFKLYYQMSFNSNQMKAIDNAFKELGKTNPYAEWMDESNDDSHRITTQINCAEYFDKRDKALLAHATQVDPDGDWFALPTDVAKRIWPTEDYELAITRVATKTPETDLFAGLR | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylatin... |
F3LDG4 | MRNARRDSLHMSLKVKNDSELDIEDENYGSEFPNGGARPSQKMIDKQRIDRVKNQYDFGRDLSSIINKDNSKKSSESVSEYDMEEVSGDQWVDSDEHDEEYYAEKWDDQPVNNLDSNDLGDERFDGVALGDGNLGDDDLNDKYIDRNQHPTAPAPKEQKSTDQDDVDQQGAGEEYVSNATVKKYEESHDEINEEVNKENSEKRSAEEPISRQSKYNSPTYQQPEQVPLNLEESVPVLMESVIEDSMSNDDIHEQSFESTIEEDDIDVDVISAEDTLNAEKNNEAGIDDELSESIYNKSSDNIEKKNKTPKANIRPVGKHV... | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 5... |
F3LGA3 | MAKNSITWNNFDSYSQQSLGLAKAVESSIRQLLDKQERVVLCVPGGSTPAEFFQVLSEVPIEWSRVTVLLNDERWVPLDHPQSNEAMLRKNLQRQAAKKVNIVSFYSPNLSIEEGVEAFNRQYSHVFPLDICVLGMGTDGHTASIFPDMESLEHAINLDQAPALIVSNVPNKEPRVSLNLSALLTSNRHYLLIRGAEKKKVLERAASKAIPLLPVSYVLAAANTHPFYAA | 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... |
A0A4P5SC77 | MSTPDIAISQRITTQRALRGRKIDPANIIFEIALILSLLTSLGFVILLLATVFSDGVGVFQERGFGFFTSNLSRIPEQAGIAQALFGSAALAVIVVLVAFPLGITTAVYLEEYAPDNKLMTLVRLNIRNLAGVPSVVYGLLGLAVFVKLLGTDMAGGTGITGGRTIISGGLTLSVLVLPIVVITSSEALRAVPASLREGAYGVGATKWEVTKKLVLPNALPGILTGTVLSLSRAIGETAPLILVGAFYGTFFTTGDTGTLGKFTTTYTALPQVIYQWATEAQSEFNVELTSAAICVLIGLTFVANIAAILLRNRYEKRW | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 319
Sequence Mass (Da): 33756
Location Topology: Multi-pass membrane protein
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A0A4Y7TJ79 | MKRKLKGGLYAPRKKVKVASNLEDLPWKTLSRPIETGLSGDDGILELEEVEGVEVVYEETEKGRVTKFKVQPENDKEAEAEDEDEAEESESSTEEEGRFDCAFAICPYVLVFTRSLGESSLPEWRPFSLNQRVGKALLGKQFAKPTPIQSASLPPALKGKDIVGIAQTGSGKTLAYGLPILHHLLSQKRPSAKRRRPLRALVLCPTRELALQVTTHLNELLNAGNVNKKEGRPPHVSIAAIVGGMSAQKQRRIIDRGIDVLVATPGRLWDIISDDDTMAKELRNLKFLILDEADRMIEAGHFAELENILRLTLREASDEQ... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 735
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 82445
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A0A522T949 | MRESLRGYAQGVLYLASQSDKYNQVVNDLRAFNTILDSQEMLAEVVSDPSIPARKRQAILGDLLASKVDVLAIQLLETIVGTENPRAIVDTISDLVRLISGDEVFSLDGGFATTGRIAGYSQALLESLQGTDALELVEEELFRFARIVESNMRIRRVLSGVGSVPDQRKSLVTALLSGRCHPMTLRIAEFAASIDRLRDFVEVLDSVVARAAELRNRRIAVVKSATELTQDQKDQITAALSRAVGVEVEMRTSVDPSLVGGVVAVIGDTVFDGSVRTRIEQLRVRLGLSATVKSRERN | 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... |
A0A537YM37 | MTTLNRRTFLKGAGVLGAASLAGPAISKDWAFAKAPLGTPATPIEHILIDCQENRSFDHYFGYAPFAGTFGPPAGYAQPDGNGGSLEPYQFTALSTPDIGHSWNAVHGEWDAGAMDGFLTTDGVNAMGYYTAQELPFYYSLFSDFTLCGNYFCSLLGPTWPNRFYTAAGTSGGITTNGIWGFGVFDYPIILDLLEDAGITWKVYNIGWDSVPYGNTDNVFVFWKRWAKDQRTRGSKGGYLNDLRRDRLPQVSFLVPSYARGWDEHPPADVSVGMGIQEELVTALRASSAWDTSAYVITYDEHGGYFDHVAPPQLDAFGLG... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine
EC: 3.1.4.3
Subcellular Location: Secreted
Sequence Length: 407
Sequence Mass (Da): 44419
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A0A537XIK4 | MTERVQVGAYGVLAVADREGPEPLPGQFYMLAAARGWGAGAGERPHLPRACSVQRVRPGGELEFLLEDVGPGTHRLLELGAGDQLWLTGPLGRGFSAPPDGRRAVLVGGGVGLAPLVILADALLAHGIVATTLLGFRDRSCACAAEQLAEFRLATDDGSVGHHGPVTDLLAAELGAGQPSVVYACGPPAMLDAVRGVCARAAVPAQLALESGMACGFGACFGCVVPTRSGYLRLCVDGPVLAADDLHGPLDPHPGPPPGPAGGGDRPPAPGTPDRAPAALPAERAMVAGTPSAPAPPAPGAGRGKVAFCGLELAHPVING... | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 621
Sequence Mass (Da): 63359
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W3AID9 | GCCCISLNEVVIHGIPDRHRILKDGDIVSVDTCTSYHGYNADATRTWAVGNVSDDAKKIMKVCYDAFWKGAEQAVEGNHLNDICATIGNYVESQGCGVITDYCGHGIGSEIHMDPEVPNYDLHRKGPKLCAGMVLAVEPMITLGSPAVHTGADGWAVIPDDGSISCHYENTILITENGPEILTLIK | 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.
Function: Removes the N-terminal methionine from nascent proteins. The ... |
A0A0N1LCD2 | MNLRESICGLILAGGAGQRFGGQDKGLQILAGRPLADHVLARLAPQVSQVLISANRNASAYERAGARVLADVAPHPGGAVPIPGAQGPLGGLLAAWAATPHDWIALCPVDAPLLATDLVARLAAARQDGDAAVVCRTREGPEPLFALVHRRTQSVLAQRLTAGERAAQGFWRAVDARELDCSEISDSFANVNTPQALADLEARLAAPPAQSR | 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... |
A0A803XWV3 | SSKPSYLGLFSTKTLVEANNEHVVEVRTQLLQPADENWDPTGTKKIWRCESSRSHTTIAKYAQYQASSFQESLREENEKKSHHKDHSDNESTSSDNSGRRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPESYWGVMNDFCEKNNMNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMIKY... | Catalytic Activity: 2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate
EC: 1.14.11.68
Subcellular Location: Nucleus
Sequence Length: 459
Sequence Mass (Da): 52860
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A0A3A5V1I8 | MYSPNRFVFSCLLLKNEFFSIFLHKLEVTNMPAQFMLQQIGLVALGGAIGAGLRYIIGNWISYETFPIATITVNLVGSFLLGIIALSTSQNIISSELALFLGTGMIGAFTTMSAFSMDTIELLQNGNTSNAAIYVMLTFSLCPILAWSGWLLGDKFLV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 158
Sequence Mass (Da): 17236
Location Topology: Multi-pass membrane protein
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A0A2E9XD76 | MRPEVTTLRKLLSNFLPVREKMTSLLSKKEPVFTVVSSNSPLRYVAMLASMLMLLLAGAVAVVQASGPSGVEDSGNSFHYFLRHIIAVAVAIIGLLFTLHIDYRKWRKWAGGLIFISFLGLIAVEVVGSSANGSTRWIDLGPLNFQPSELLKLSTVIGLASFLAQRRRQIAISKKLVMSVMGALAAMGLVVAVLQSDLGTAVLIAVMVVGMLFVSGVPIRYLLFPLSLVAAAGGILIASEPYRRSRIVGMLNPLDYCGNETWQLCQAWATLANGGLTGTGFGSGHAKWGWVPAAHTDFVFAVIGEEVGFLGGVVIIGLLG... | 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)-... |
A0A7W1F6X8 | MPQEQEHKKVQKKGDGAGGPDVDAAQTQESSKAAKLKEEMDDLLDEIDSVLEENAEEFVKSYVQKGGE | Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Function: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.
Sequence Length: 68
Domain: The N-terminal unstructured half of P... |
F3LIA3 | MTFILGITGGIASGKTTATKTLESLGVEIVDADIVARYVVSNDSSNNSSALAKIVDHFGSAILLASGELDRTRLRDIIFSDLTEKRWLENLLHPIVRKQIIQQLSAIKSPYGVLSSPLLFEKEQQELVNRTLVIDVPIEAQNTRATLRDNVNQQQISRIMDTQLSREERNKKADDIISNTGNIEELQEKITVYHNRLLNKIRAL | 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... |
A0A3A5UYS0 | MDSVHQENSEGVMPMMKVRELGVVPYEDAQALMKELQQQRIDGQIPDTLLILSHPEVVTVGPRARNDGILPPSDYETIGVDRGGGLTWHGPGQVVGYPIFKWGERDGEASVADIIHTIEGWLIDALATFGVNGERDERMQGVWVNGRKVCSIGLSFLRWVSRHGFSVNLNTPPGRVEGVAGCGLVADTTTSLAHLGYTISPEAFVKALLPVVNTTLES | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
A0A3A5V4J4 | MGTDVERTDGNLPNTAEEDLRSLEESYAELRDETQQLINERTTLEAEMRTLRKRIERLDENVNLLKMPPLIVGHIQDILDHERAIVRSSNGTVFQVSLNQRLDPEMLKPGTRVALNQDSLSVVELLTEAWDPMVSGAEMVEKPDISYQDVAGLDEQVESVREAIELPLVKPELFEKVGIVPPKGVLLVGPPGCGKTLLAKAVANHTNATFIRMVGSELAQKYIGEGGRMVRELFSLAKEKAPSVIFLDEIDAIGAKRLDGSTSGDREVQRTLMQLLAELDGFDALKDVKIIAATNRPDILDDALLRPGRFDRVIEIPIPD... | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of pro... |
E3I7Y3 | MTKSEIDEATVRRIAHLARVKVTAEEAKSLQRELNGILSWVEELNAIPTDGVEPLTSVGGAKLHMREDVVTDGNKPADVLKNAPKSEDGFFLVPKVIE | 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 ... |
A0A537VXB9 | MTRALGVDLGTGRTGIAVGSFGVAHPLTVIESKDDDAIVAQIARLATDEGAQEIVFGLATSLDGTEGPATARQRSIAAAVGDATGLPVHLWDERLTTAEANRALIGAGVRRKQRRGVVDKVAATILLQSYLDAHRAGSETT | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 14615
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A0A350SG42 | MKIAVFGGSFNPLHYGHLFIAEEARTELGYDRVIFVPSNISSHKNDFSGLDPACRLEMLEEVLNNFDYLLLDSCDIERGGVSYSVDTIEHIYRKYSFTGKPGFIIGDDLTSGFTGWKNYQELKKMIDLIVVKRNFNKKIDSGLPDYYIDNTILPLSSTEIRNRVKSGKTIKNLVPESVRLKIIKNGYYK | 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... |
A0A7J9WZW8 | MKANNPSQALAVTLVDEFVRNGITHASLSPGSRSAPLAFALAAEQRLELHVSIDERSAAFLALGCARATGRPALLACTSGTAAANFLPAVVEAFNDGVPLVVLTADRPPELRGTGANQTIDQLKLYGDSVRWFCEVGAPEAHPAQPPYWRSTACRAVAEAAGATGGASGPVHLNLSLREPLVPEALDGFDLDLSGRPDGRPWTATERPRVLPSEPELDEVAQLVARTERGIIVAGAGAPGAESLLELARRIGYPVLAEPASNARTGDPAIAHYEALLRSPNFAERHPAELVLRFGKTGLSRALGRYLDTCREHVGVVRLG... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A662DCD6 | MEHRPEAPFGRVATAVITPFTDEGPIDYAAFWRLVRHLADNATDSIVVAGTTGESPTLSKPEKMALFAAAVDAAAGKIKVVAGGTNSDTAESIEFAVSAAASGVDGMMVVTPYYSKPPQRGIVAHMHAIADATDLPVMIYNIPGRTATLIEIDTLVEVCEHPNVVAVKDAVDDLDWSRRAIQALPDGIAVYSGSDGLTKDLVAAGAVGVVSVASHLAGREISAMVDALIEGDIVKAEKLHDLLMPLNDALFSEPSPMPLKGALTAYWDSVGVPRLPLVSANPETVEAVGVALEAINEYRSP | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyru... |
A0A3D2VKJ7 | MTAPRTRAARLHAITQVLNAQPVRSQAELAHLLSAQGIAVTQATLSRDLVEIGAVRSRAADGSLVYRVNTAPSASTLPTSAQRLERAVSELVLDVQASGNIVVVHTPPGGAQFLASAIDGGEVPGVMGTVAGDDTVLLVSQSPDGGGAVVEYLVSLTTSKGSNL | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 164
Sequence Mass (Da): 16705
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A0A7W1N7E2 | MRLQPLLTADETRRAEQAHQGSLEELMERAGSAVAQTVLRGFPGRVTVVCGKGSNGGDGHVCARVLRASGRHVTVVDEVGDLGEPDVIVDALFGIGLRDAPREDAARMIERINASSRPVVAVDVPSGVNASTGEIPGVAVRATTTVTFGAAKVGLAIAPGRLHAGSVTVAPLGLRPREHEHSLVPASVLLEIPAKHAESTKYSAGSVLVVGGSRGLTGAPMLAALAAFRADAGYVAVAAPESTLSVLETTLLEVVKHPLQEDSSGRLLPRAADAIFEAAEKADAVAIGPGLGRSDGTVELVRILLERLPMPVVLDADGLW... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A7K0SXE4 | MTSHPSSGVSPDVTGAWLEGDDPGERKFLTIPSLLLENGDRLEEVTIAYQSWGVLNEARDNAVLINHALTGWSDVPGWWPSMVGPGLPFDTDKYFILCPNVIGGCQGSTGPSSIAPDGKRYGSRFPTLTIRDMVAAEVAFSDALGIQKYRLAVGPSLGGMRALEWAITLPDRIGAICTIGSSAVATGDQIGTASIQIRAIRNDPNFHNGDYYESKRGPVDGMGIARRIAHLTYRTEAEMDVRFGRELQGDDTGRYAVESYLDHQASKLNHRFDANTYICLTEAMNSHDVGRERGGVASALGAITVPVVVVSIDTDRLFPP... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
EC: 2.3.1.31
S... |
A0A7W0UL27 | MDRITIRGLVARTSVGVSTEERARPQTVVIDIVIEADLAPAGRSDDLADTISYSEVTAEVAGLVASSSASLLEHLAERIATELLARHDARNVVVEIGKEPPPVPQDVAGISVRIERPGAPEV | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A7X7PLG0 | MADVVLITGGSRSGKSALAQAMAEALPRPRVFVATYPGEDDAEMAARVRRHQTARAAGGWTTVEEPLDVAGVLRRSTGGTYVVDCLSLWVSNLMWRTALRAAGEVAGSGQAGLPATTSELPCQSVAESVTEDDIGAACRSLIAAGGRIGGTVVYVTNEVGLGVVPDNAVARQYRDLLGRCNQAMGAA | 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... |
A0A952HSL7 | GASLISISPFWFVILTTFIVTTGTVFLMWIGEKITEFGIGNGISMIILAGIVAGIIPAILKTYELLKVGEISILTLLLAVLIIVLVVAGIVYIQEAERRIPIHHARRSISIINQSASYLPFKLNPSGVIPIIFAVAILMFPATIAQFFAGHSEIARIIVDYLSPQSYVYLVLYVGLIIFFSYFYTAILINPIDIADNLRKSGAFIPGVRAGTQTVEYLNYVLTRLVFAGSIFLAVIAVLPIMLIKLLNVPFYFGGTSALIVVVVALDTIHQIEAYLAMKKYEGFLKRG | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
A0A3N5MYR8 | LVDAARRLDADPATAAVVAGAPAAADSARRAGFAAVAADAAGVALQPVPRALSAVPDALSSWDTVAALLRDRRLAVFLDFDGTLSPIVDRPDDARMTPSGGPALARLSALCPVAIVSGRDLGDVRRRAGVPSLWYAGSHGFEYVSPDGEAHEHEQAGQAVAALAEAEQQLSARLRDLPGAIVENKRFALAAHYRMVAEQRATEVIDAVAEVGAQYPVLRMTGGRKVAELRPNIDWDKGKALHWLLEQIAPDDGDVLPLYAGDDLTDEDALTAIGERGFGVVVRNYELGDRPTAAHVGVDDPEEFCAVLERVSDLLEEG | 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: 318
Sequence Mass (Da): 33606
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A0A538KJC4 | MTVDTVSLEQVVAAARAAGDAVLDEYERGGVARSKSDGSPVSEADERSQEIILSHLAEIAPETPVVAEEGPQASLAAPHERFWLVDPLDGTKEFLDRTDEFTVNIALIEDRVPVLGVVLAPARGLLFAAAPTVGASVEDGAGRRSIVARSIPPDGATLVSSRSHGDREALDRFTGGRRVARATVAGSSLKFCLLAAGEADLYPRFGRTMEWDTAAGDAILRAAGGRVTDLEDRPLTYGKPGFENPHFIAWGRG | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
EC: 3.1.3.7
Subcellular Location: Cell membrane
Sequence Length: 253
Sequence Mass (Da): 26802
Location Topology: Peripheral membrane protein
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A0A7X6SIV7 | MAPALRLIIFGRQGAGKGTQATRLAAHYGIPHISTGDMLRASAATGSEFGLQVKAIMDAGGLVSDDVMEGVVRERLAQPDAATGFLLDGYPRTPGQAEFLNELLAPGGVDLALNLDVPEEVVVERITKRRVCESCGATYSLGDASADSASCAKCGGTVSQRADDTEESVRKRLATYLAQTEPLMQWFDDRDKLVTVNGVGHPDDIAAALVAAIDAGAPGSH | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A8J6YS66 | MERYMAVELNSDSMERAGERVSLGVYYRLTKPGIVFANLLGTVAGFLLAMKGAPFTPDLMVTFFFSLLGIALVIAGGTTLNNVIDRDIDGYMERTKDRPIHSGRVSVKTATFFGLSLAVAGEAVLTFGVHPQAAFLALIGFVVYVIIYTLWLKRITTLNTVIGGISGAMPTVMGYVAVTGRMDLTAWILFSILFLWQPPHFLALAMRRHTDYRNACVPMLPNVKGFGETKKQIFYYTLSMFPVSLMLYPLRAVGWLYLIGALLLGAVYLFKAYQGLYQRGEEEKRWASFMFRYSIIYLTLLYLLMMIDAA | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
A0A4Y4CSW0 | MSPFSIAGLVGVVPGPAPAAAEHTAVALLPGGAGYGLVGLALLAAGLLVWSLVLRRRVAARTQALQAARAELEGLRAAGEEARLRLDAETAGRIRELDDTAAEFRAIVEAASSGIVLMRDRHIVHCNRRMDEIFGYAPGEQIGQPTRIWYASDEEWARIGEEVYRKIWQGENHQREAQVRRKDGSPVWVRMSGRALDLAHPERGLVGIIEDITREREMLEEAQRARAMAEDGARMKSDFLANMSHEIRTPMNAIVGMAYLALRTDLTARQRDYLEKIQGAGQHLLGIINDILDLSRIEAGKLVVEHIPFSLERMIVNVTA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 973
Sequence Mass (Da): 104883
Location Topology: Multi-pass membrane protein
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A0A7J4G100 | MQEYFVLGAKKLMYKIDRDEFNLPFMKERGYIRRQCKICKAYFWTLDEDAEVCGEAPCVDYTFFDNPPTRRRYSLREMRNAFLKFFEKNDHEIINPYPIVARWRDDLLITIASIADFQPYVTSGEASPPANPLVISQPCLRLEDIDKVGFTSGRHMTIFEMGGAHAFNDSRKNIYKYWKNETIEYHHEFATKELGIPEELITYKEHFWVGGGNAGPDLEGIISGLEVSTLVFMKYKIDEEGKLFETPILTVDTGYGMERWTWLSQGIYYGFEAIYGDLFKWLTEKFEVSIPRRTLKRFALMSPTLTDKELNKFGEVISQI... | 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... |
A0A6L6C6X3 | MAASVRSVALLGATGSIGTQTLDVLRRSPEQFKLVALSGGTRTHELIAIAREFRVPLVGVLNEDDAQIVAAELPGVDVVVGDAGLDSLARSADVVVNAVVGFAGLTATLAALDAGKRLALANKESLVAAAPLVDQVRAHRDCDLVPIDSEHCAIHQCLAGADATDGYRSVKRLLLTASGGPFRTKSLSELQHVTKADALAHPTWAMGPKITIDSSTLMNKGLEVLEAAALFGIGVDRIDVVVHPQSIVHSMVEYVDGSTLAQLSHPDMRLPIAYCLGLPERLDHSWGAISFTDALTLTFEPPNRQAFPALDLAYEAGRRG... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A2D9X1P8 | MMSLYNIFSNCSGVSIDSRTIQKDALFIALTGDNHDGHHYVESAFKQGAGYAIIDNPAFKINSRCILVDNTLQALQDLARYHRTQLTTTTVIAIVGSNGKTTTKNLIQAIFSSSFKTQATQGNLNNHIGVPLTILSLSQDCEFAVIEMGANHPGEHHLLCSIAQPHAGIITNCGKDHLEGYGSIEGVIDANCELYDYLRDTNGTIFVNHHDPILNARVSDLATIHYAHSDQAIDNVLTTGSAITLYPNVSLRLSHHTTMTTHSITIDSHLLGDFQINNMLSAACIGLYFKVSLEMIKHAIESYVPNNNRSQIIQWNSNTI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A1Y1JZB2 | EMYAIFGNSDRSATYSDTLEMKYLERCLLETLRLYPPVPLIARKINQDVKLASGNYTVPAGCTVIIATYKLHRNPDIYTNPDEFNPDNFLPERCIKRPYYAFIPFSAGPRGCVGRKYAILKLKVLLATIMRNFVVKSDASESE | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 143
Sequence Mass (Da): 16278
Location Topology: Peripheral membrane protein
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A0A2G8JTD1 | RLTNRVFDTVGVEYNSSLNEETFTAGCSAILSTLVAEDLEESCHNDFNGTDQFYLVELLSYGGSATRLQESEMGEYLEDLDKNYSPQTYSECFDEEVLFDELVNDHVVGATIGEVASVSARIIANLIEGQCIGHALYPNPEEFTDSILEVYGSNGMLPLQGLVDILQDLALINHDESVMTSSEEEDHDHKDVSADHTDHDHDHDHDHDHDHDHHRRSVIELDESVRQKRHVDYVHEVVRLNIDRCLSAKEIFLSHGMNTSKGLTHEDFHEICPALIQQKVGDYCKEEHRHHTAGKDKLKSYIYGSIFVLLVTLSALLGAL... | Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Subcellular Location: Membrane
Sequence Length: 609
Sequence Mass (Da): 67820
Location Topology: Multi-pass membrane protein
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A0A952LI01 | MNETEIIQTLLNIRFTDVLDILIVSVIIYYLLKFLAGTRGWQILIGLLILLLFWIVAKIFQFETLGWIFENLWSVGIFIIVVLFQPELRRGLAKLGEKGIFKFLSPSNKKVVDDVIRACLFMADRKIGSLIVFERTVDLTNYIEGFVRIDAEITPEILITIFTPQTPLHDGAVIIKEKKIAFARAFLPLTVSTDIPENVGTRHRAALGITEETDAVAVVVSEERGEISLAVDGKLHRNLDVLMLRKKLYKLLEIEKPSTFEMLRKRLKKTKHENK | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 275
Sequence Mass (Da): 31448
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A0A367I7Y4 | MESSIVLFGPPGAGKGTQAGRIVQATGKPQVSTGDMLRAAVAAGTELGRIAKGHMESGGLVPDDVIIGLIEERVKAQDAENGLLFDGFPRTVAQAEALAEIAPVSLVIAIEVEDESIVGRITGRFTCGACGSVYHDQFRPCKVEGQCDECGSSDFKRRTDDSEETVRARLSAYHEQTSPLALWYEQRGLLHRIDGNASIDEVGVRVSKILVE | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A538CWR8 | MAAEVAELTFRAMGSDAHVIVVGGPADSATRARARIDELEQRWSRFIADSEISVLNRSAGEYVEVSDDTRLLVERAIEAWRISGGSFDPTVLGAVIRAGYDRSFDTLSDAPSAGISALLLGCTDIEITGHGVRLPAGTGFDPGGIGKGLAADLVAEATMAAGADGVCINLGGDLRVHGRSPEGDGWTIDIEHPLSSAPIARVGVAEGAVATSTTLRRQWKVDGAPRHHLIDPATGLPSDSDLTLACVITANAWAAEVLAKAVLLRGSTCCCAVRPTRSIYSEVLARRRSSSIGRDASTPPTASARTSATRFCRHD | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 315
Sequence Mass (Da): 32942
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B5ECD6 | MWVLASFFPLAALALQWLLWERLRPYVWLFFYPAVFLSSWAGGRVAGLLATAFSATVVWYFFIPPEQSFSLEHPSTAIALLIFAGMGILFSLFHERLRRADRQIRLTLAEATSGREQLERRMEERTKELVDLVDELRRKETDLRRSQELLKLFIEYAPVPLAMFDSEMRYLYASRRWRSDYGLGNRPLVKVSHYEIFPEIPQHWKELHQRGLAGEILREEAEEFRRADGTVQWLRWELRPWYDAGGMVGGIVIFSEDITNRKCAEDALQKLNEELELRVVQRTETLDQILGEREAQNAELQRAYHELEAETAQRIRMVEE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 554
Sequence Mass (Da): 63631
Location Topology: Multi-pass membrane protein
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A0A537VAB7 | MTDFVDGRLARRWKRTSQLGAFLDTTADKVLVTGVLIALVAVGRASAWVGFVIIAREIVVFGLKGVASSAEGSIVNPSRLGKAKANLQFLAIFVAIWRPDILVGGRFVDEWLMWVAAIITVWSGIDYVGRYAGAFTRVRER | Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 141
Sequence Mass (Da): 15455
Location Topology: Multi-pass membrane protein
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A0A162R5X2 | MSDSSSRKRLTARRKKKHGIEGKFHQDVMGVTFLEVCHAKDLPPERNLARTSFDMDPFVVVSYGTSTFRTSAVRHNLNPVWNEKLFFHVRHHEANFHLKFTVYDREKFSGNDLVAWCQVPIQDIIQQHKEMQFADSQDEEIDMIEQEMDRLTFPLQMVNPDKWKNKRPSLTIRAKFMPYEEIRKMFWLSLAKAYDAEHTGTLSRLQVQSMLETIGSTITEATIDRFWSNSGKDPKMEDQEITLEELVNSLENYMQAEAEYNGNWPTSPTMTPSASGDNMEGLGLSMMQMAMDQDDDDQDEDEDEDEDDEEEDWNVEKVIR... | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A538HKL8 | MRRGAVPNACRRWTSSPTRTPGSRVSVPAEPEVAQLSARAIGLDDIEGPVVVACSGGADSLALLVVAVARGLTPTAAYIDHGLRPESRYEAELVAGAAQRLGAQFSSTRVCIEPGRNLEARARAARYTALEATRARVGASVVLVAHTADDQAETVVLNLLRGSASAGLGGMAVRRGTVVRPFLRVRRSETEAACTALGLDPVRDPMNNDLSYRRVWVRRVVLPLLSEGAGRDLVPVLERQARLLRAESDYLDELAGAAWPLPDGSTPAPALTRLPLVLARRAVRMWVGPPPPTWNEVERVLAVARCEVVATEVGGGRRIS... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A537TKX3 | MVRRTACAPAAPGRENPDPLPEAVRFAKWHGLGNDYLLLERDDVGSPLDPPLVRRLCDYHFGIGSDGVIEVVAAAGETADVLIWNPDGSTAELSGNGTRIAARWLARRAGASEVRITVGPREVLARMREGLAVETEMGRIEVAPREPLEVDGTALEFTPVSVGNPHAVIALEPERAELLRLGPLVEHHPRFPDRTNVQLVRVDSRREATVGVWERGAGETLSSGTSACAVAAAAIANGWCESPVTIHLAGGDLLVEIDQEMNARLTGPAQEICRGEVADELLDDVSRGDGR | 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... |
G1N1Z8 | MSMVLTLLVSVHRLCRLFAMSGAERLAVPECVSQAGCWAAGGSRERREVSPGVNSDVRAALERILPALQRSIACAKQAAGPAEMGKAIAEIFQLVEEAWGMPTLGRDVAKALCDAIRLEGGLDLLLNLLYTAELETKCQAGQLLEQILVAENRDRIARIGLGVILNLAKERDVLQLAQSVSGILEHMFKHTEETCSQLISDGGLDAILYWCRWTDPVVLRHCAMALANCAMYGGQGNQRLMIKKKAAEWLFPLVFSRDDEFIRLHACLAIAVLATNKEIEKEVERSGTLALVEPFIASLDPEQFACDMLGSSDNSQGRTA... | Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
EC: 3.2.2.6
Subcellular Location: Cell projection
Sequence Length: 717
Sequence Mass (Da): 79858
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A0A7K0A1Z2 | MRDVTYCLAGTALGDLFVASTEQGVCTVDFEPNSLNWIDHLAGSTIRKNQQAVKPIVDEIQSYLAGELQTFTCDVDLTFATAYAQRVLHELRKVPFGEVTSYGQLARRIGSSPRAVGGAVGRNPIPIIVPCHRVLAGDGSLGGFSGGLDRKRALLAIEGRVDLPGGWFSARAPEVAQV | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A5D0R1 | MSRIEILPNLCTAANLFFGVMAIAAVINHNFQLSVALVIIAAILDRADGALARRCNAISSFGKEFDSLADLVSFGVAPAALLYSVTNSKWHAAGLACFVLFTLCGAFRLARFNISDNSSCFQGVPITIAGSVMALLVALLPHSVFIILLSSVMLSAAMVCTIRIPKI | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 17677
Location Topology: Multi-pass membrane protein
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A0A1W9SF13 | MAINAGASALGLVSSMPSGPGVISEDLIAEVSAAIPVGITSVLLTSQQNPASIIEQHQKCRTNAIQLCDRLSVITPRELQDAMPGTDIMQVIHVTGQNSIEEAVSIAPFVNAILLDSGNKSLPIKVLGGTGKIHDWKISREIRDRVEVSVYLAGGLTPENVAEAIREVSPFGVDVCNGVRTNGLLDKRKLQKFLEQVNSAT | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 201
Sequence Mass (Da): 21333
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A0A350SIQ6 | MQGIRELRSRIKSISGTAKIIKAMEMVSSSRIRKAQVRILEARPFMNKIEAFISELSVFPGAFLNPLTKSNDDYESVIILGITSDRGLCGSYNSNMIRHIEKRIEYYESLGKKVQLWITGIKGKNYFRYIGRNIEKSYDHLSDYPKFFDAREICNDFIDEYLEKRTGRVELNFTKYNGLFEQKPVTRQVIPLPLEKMRERLYIELGITEQINSFSKEEFLFEPSSNEVMLSLVPEYINTLMYTALLESTASEIAARMTAMKSASDSAEKMKKLLNNKYHRARQQQITIEISEIASGADALINL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 303
Sequence Mass (Da): 34937
Location Topology: Per... |
A0A538CUR5 | MSGTDPYLHPPLHAVRDAVARALAEDLTPIGDLSAALVPSDAHAEAEFVVRTRGVLAGTACATETFRQIDERIHVEWAVGEGSLVAARTAVGVVRGPLPSILTAERTALNFLGHLSGVATRVRALVDALLDAGGDDAPRVWDTRKTTPGLRALEKAAVRAGGGRNHRGNLSDWVMLKDNHLTGIGITAGVARARDLWPGRAVHVECERQEQVVEAVGAGADAILLDNMSPVEITECVRLVHDAGLGSRRPLLEISGGVTLENAPSYARAGADMISSGSLTNSAPVLDIGLDIHPMTTTTPGPERGARPERPSERGARPER... | 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: 337
Sequence Mass (Da): 35604
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A0A537XSN1 | MPTYRRYPVTFARGKGFYLYDETGRPYLDFVAGVAVTALGHAHPAVTEAVARQAGRLVHTSNLYYTEPMADLAGRLTGLLGWPDGRVFFANSGAEANECALKLVRKASRVRSSTGERRFRETRAETIAAWGSFHGRTMQTLAATGQPAKWEAFRPLPPGFVHVPYDDAPAIGAAVSAATAAVLLEPVQGEGGVVVPGEGYLPEVRSICDARGVALVLDEVQTGLGRTGEWFGFQAYGDRAVPDVISLAKALGNGFPIGACVARGRYATAFGPGDHATTVGGGPVVCAAALAVLDTIERDGLVERARKVGDYLRQGLAGLV... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
... |
A0A2M8EP44 | MDEETAGTIQETHEETQTESENPIVAVAGQFGLNGQMFTAQLINFLLVLIVLWRFAYRPIVRMLDEREEKIEKSVKQADEIEKRVSEIEKERDEVMNTARREAQEIADKAHKQGEERREEIIGAAKREVERVIVKGKEQLVAEKEAMMRELKKEIIDIAMKAATRIAEDQIDESKSKSLAEEAVRKMI | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 188
Sequence Mass (Da): 21654
Location Topology: Single-pass membrane protein
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A0A2W4LBX1 | MRGIILAGGSGTRLHPITMGVSKQLVPVYDKPMIYYPLSTLILAGIRDVLVITTPHDAPQFERLLGDGSQFGISISFAVQHEPNGLAQAFVIGADHVGNDHAALVLGDNIFYGPGLGSTLQRFNAVDGAAIFAYRVADPTAYGVVEFDAEGRAISLEEKPAKPKSKYAVPGLYFYDNDVVEIARSLKPSARGELEITDLNRRYLEQGRLQGGGPPP | Function: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
EC: 2.7.7.24
Catalytic Activity: alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose
Sequence Length: 216
Sequence Mass (Da): 23221
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Q0A6U3 | MSAKAAEAAPTAQSDTQQVIRRNGALTAFDPDKIQLAMKKAFLAVEGERSADAARIQQVTAELTAQVVQALTRRPTATPIHIEDIQDQVELALMRAGEHKVARAYVLYREEHARKRRQEATDEPPRLHMTRTDGEQVPLDESLLRRVLHHACHELADTDPERVAREAWRNLYDGVTEQEVHKALILSARSLIEQEPAYGHVAARLLQHQLNGEALRFLDFPYDGAPGADPGYTDYFARYIRRGVELELLDEQLLTFDLERLAEALMPERDLQFNYLGLQTLYDRYLQHWDGTRFELPQAFFMRVAMGLTLQEVEREERAI... | Pathway: Genetic information processing; DNA replication.
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... |
A0A1V5TE70 | MQNKKIQTRKRFFSLEGIDGSGKTTQMDLLQKALEEKGFSCLRIREPGGSMISERIRELLLDSKFKGLMADKAELLLYNAARAQIIEECIKPALDSGKIVLADRFAWSTYAYQGFGRNLDKQMIFDLSVITCGEFLPELTIVLDIDVLKSRKRMAKENKVPDRLESEALSFFERVRQGYLNVVEEFPQHAVLVNADQSQEKIHLELLTHVLNRLN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 215
Sequence Mass (Da): 24624
|
A0A4D6XPV2 | MERYKYLFQKLHSSNNRCLIPFLTIGDPSLKLSYKIIYFILKKRLAHALELGIPFSDPLADGQIIQKANIRALKSNITLKKCFFLIKNIRNIFKKIPIGILIYANMVYQKGIQNFFYECYVSGIDSVIIPDVPIEENQYFKKTAELYGIHFIIMCPPDADKDLLEKISMLATGFIYLLSRTGVTGNNKTLNTPSILKTIEKLKKYTSTPLIQGFGISKIEHIEYALKNKVSGIVCGSAIISIIEHLYEKKPHLIFKKMHTLLSSFKKTTIYKK | 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... |
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