ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q00718 | MPPRVVRLPSLTGLRWFAALAVFACHIAQQQFFADQQVGTALLHITTLGSIAVSVFFLLSGFVLAWSARDKDSVTTFWRRRFAKIYPLHLVTFLIAGVIIFSLAEPTLPGGSVWDGLVPDLLLVQSWLPEPTIIAGFNTPSWSLSCEFAFYLTFPLWYRLVRKIPVRRLWWCAAGIAAAVICVPFVTSQFPASAETAPGMPLNELWFACWLPPVRMLEFVLGIVMALILRTGVWRGPGVVSSALLLAAAYGVTQVVPPMFTIAACSIVPAALLITALANADVQGLRTGLRSAVLVRLGEWSFAFYLVHFMVIRYGHRLMGGELGYARQWSTASAGALALAMLAVAIVAGGLLHTVVENPCMRLLGRRRPVATAPDPATDEAPKLTRA | Function: Catalyzes the acylation of the mycaminose sugar during midecamycin biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42172
Sequence Length: 387
Subcellular Location: Cell membrane
EC: 2.3.1.-
|
Q7AFA1 | MSRVSQARNLGKYFLLIDNMLVVLGFFVVFPLISIRFVDQMGWAAVMVGIALGLRQFIQQGLGIFGGAIADRFGAKPMIVTGMLMRAAGFATMGIAHEPWLLWFSCLLSGLGGTLFDPPRSALVVKLIRPQQRGRFFSLLMMQDSAGAVIGALLGSWLLQYDFRLVCATGAVLFVLCAAFNAWLLPAWKLSTVRTPVREGMTRVMRDKRFVTYVLTLAGYYMLAVQVMLMLPIMVNDVAGAPSAVKWMYAIEACLSLTLLYPIARWSEKHFRLEHRLMAGLLIMSLSMMPVGMVSGLQQLFTLICLFYIGSIIAEPARETLSASLADARARGSYMGFSRLGLAIGGAIGYIGGGWLFDLGKSVHQPELPWMMLGIIGIFTFLALGWQFSQKRAARRLLERDA | Function: Confers resistance to norfloxacin and enoxacin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44391
Sequence Length: 402
Subcellular Location: Cell inner membrane
|
A6TA11 | MQKYFVEARQLLALAIPVILAQVAQTAMGFVDTVMAGGYSATDMAAVAIGTSIWLPAILFGHGLLLALTPVVAQLNGSGRRERIAPQVRQGFWLAGFVSVLIMVVLWNAGYIISSMHNIDPLLAEKAVGYLRALLWGAPGYLFFQVARNQCEGLAKTKPGMVMGFIGLLVNIPVNYIFIYGHFGMPELGGVGCGVATASVYWVMFASMLWWVRRARTMRDIRCAERFSGPDFAVLLRLVQLGLPIALALFFEVTLFAVVALLVSPLGIIDVAGHQIALNFSSLMFVLPLSLAAAVTIRVGFRLGQGSTIDAQVSARTGVGVGVCLAVFTAIFTVLMRKQIALLYNDNPEVVTLASHLMLLAAIYQISDSIQVIGSGILRGYKDTRSIFFITFTAYWVLGLPSGYLLALTDMIVPRMGPAGFWCGFIIGLTSAAIMMMLRMRFLQRQPSSIILQRAAR | Function: Multidrug efflux pump that functions probably as a Na(+)/drug antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49641
Sequence Length: 457
Subcellular Location: Cell inner membrane
|
B4EWN4 | MQKYIKEARSLLALGIPVIIAQFSQTAMGVVDTVMAGAVNATEMSAVAVGTSIWLPTILLGQGILMALTPIVAQLNGSGQRKHIANRTQQGFWLATFLSIMVIAILYNSRFIIEAQHDIEPELAEKAIGFIHAIMWGAPGCLYYQVLRSQCEGLSKTKPGMIIGFIGLLINIPVNYAFIYGKFGAPQLGGIGCGVATASVFWAMFLMMRYYVRRAPTQRDVMPKKRLVLPEFHTIKRITLLGLPVGLALFFEVTLFAVVALLVSPLGVTAVASHQIALNFSSLMFMFPLSLGIAATIRVGYNLGQRSTEQARTSAITALAVGLMLASCTAIFSIIFREKIALMYNDNIEVVTLASHLMLFAALYQLSDSVQVIGSGVLRGYKDTRSIFFITFIAYWVIGLPSGYLLGRTDYIVEAMGPAGFWIGFILGLTASAIMMGTRIWWIQRQSDEVVLLRSER | Function: Multidrug efflux pump that functions probably as a Na(+)/drug antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50030
Sequence Length: 457
Subcellular Location: Cell inner membrane
|
Q8N635 | MANSFAARIFTTLSDLQTNMANLKVIGIVIGKTDVKGFPDRKNIGSERYTFSFTIRDSPAHFVNAASWGNEDYIKSLSDSFRVGDCVIIENPLIQRKEIEREEKFSPATPSNCKLLLSENHSTVKVCSSYEVDTKLLSLIHLPVKESHDYYSLGDIVANGHSLNGRIINVLAAVKSVGEPKYFTTSDRRKGQRCEVRLYDETESSFAMTCWDNESILLAQSWMPRETVIFASDVRINFDKFRNCMTATVISKTIITTNPDIPEANILLNFIRENKETNVLDDEIDSYFKESINLSTIVDVYTVEQLKGKALKNEGKADPSYGILYAYISTLNIDDETTKVVRNRCSSCGYIVNEASNMCTTCNKNSLDFKSVFLSFHVLIDLTDHTGTLHSCSLTGSVAEETLGCTFVLSHRARSGLKISVLSCKLADPTEASRNLSGQKHV | Function: Single-stranded DNA-binding protein required for homologous recombination in meiosis I. Required for double strand breaks (DSBs) repair and crossover formation and promotion of faithful and complete synapsis. Not required for the initial loading of recombinases but required to maintain a proper number of RAD51 and DMC1 foci after the zygotene stage. May act by ensuring the stabilization of recombinases, which is required for successful homology search and meiotic recombination. Displays Single-stranded DNA 3'-5' exonuclease activity in vitro.
Sequence Mass (Da): 49313
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
Q0WUA3 | MVNFVSLCDIKYGFVPKNSTDLFVKRKIHKLPSRGDVITRLPVFGSNARENLNAKPRRNLRVRPIFCKSYGDAAKVYQEEEIPRAKLIWRAIKLPMYSVALVPLTVGASAAYLETGLFLARRYVTLLLSSILIITWLNLSNDVYDFDTGADKNKMESVVNLVGSRTGTLAAAITSLALGVSGLVWTSLNASNIRAILLLASAILCGYVYQCPPFRLSYQGLGEPLCFAAFGPFATTAFYLLLGSSSEMRHLPLSGRVLSSSVLVGFTTSLILFCSHFHQVDGDLAVGKYSPLVRLGTEKGAFVVRWTIRLLYSMLLVLGLTRILPLPCTLMCFLTLPVGNLVSSYVEKHHKDNGKIFMAKYYCVRLHALLGAALSLGLVIAR | Function: Involved in the synthesis of phylloquinone (vitamin K1). Catalyzes the transfer of a prenyl chain to 2-carboxy-1,4-naphthoquinone.
Catalytic Activity: 1,4-dioxo-2-naphthoate + H(+) + phytyl diphosphate = CO2 + demethylphylloquinone + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42037
Sequence Length: 382
Subcellular Location: Plastid
EC: 2.5.1.130
|
P39582 | MNQTNKGEGQTAPQKESMGQILWQLTRPHTLTASFVPVLLGTVLAMFYVKVDLLLFLAMLFSCLWIQIATNLFNEYYDFKRGLDTAESVGIGGAIVRHGMKPKTILQLALASYGIAILLGVYICASSSWWLALIGLVGMAIGYLYTGGPLPIAYTPFGELFSGICMGSVFVLISFFIQTDKINMQSILISIPIAILVGAINLSNNIRDIEEDKKGGRKTLAILMGHKGAVTLLAASFAVAYIWVVGLVITGAASPWLFVVFLSVPKPVQAVKGFVQNEMPMNMIVAMKSTAQTNTFFGFLLSIGLLISYFR | Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33838
Sequence Length: 311
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Subcellular Location: Cell membrane
EC: 2.5.1.74
|
P32166 | MTEQQISRTQAWLESLRPKTLPLAFAAIIVGTALAWWQGHFDPLVALLALITAGLLQILSNLANDYGDAVKGSDKPDRIGPLRGMQKGVITQQEMKRALIITVVLICLSGLALVAVACHTLADFVGFLILGGLSIIAAITYTVGNRPYGYIGLGDISVLVFFGWLSVMGSWYLQAHTLIPALILPATACGLLATAVLNINNLRDINSDRENGKNTLVVRLGEVNARRYHACLLMGSLVCLALFNLFSLHSLWGWLFLLAAPLLVKQARYVMREMDPVAMRPMLERTVKGALLTNLLFVLGIFLSQWAA | Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK). Attaches octaprenylpyrophosphate, a membrane-bound 40-carbon side chain to DHNA. The conversion of DHNA to DMK proceeds in three stages: the removal of the carboxyl group of DHNA as CO(2), the attachment of the isoprenoid side chain, and a quinol-to-quinone oxidation, which is thought to be spontaneous.
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33594
Sequence Length: 308
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Subcellular Location: Cell inner membrane
EC: 2.5.1.74
|
P65651 | MASFAQWVSGARPRTLPNAIAPVVAGTGAAAWLHAAVWWKALLALAVAVALVIGVNYANDYSDGIRGTDDDRVGPVRLVGSRLATPRSVLTAAMTSLALGALAGLVLALLSAPWLIAVGAICIAGAWLYTGGSKPYGYAGFGELAVFVFFGPVAVLGTQYTQALRVDWVGLAQAVATGALSCSVLVANNLRDIPTDARADKITLAVRLGDARTRMLYQGLLAVAGVLTFVLMLATPWCVVGLVAAPLALRAAGPVRSGRGGRELIPVLRDTGLAMLVWALAVAGALAFGQLS | Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30014
Sequence Length: 292
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Subcellular Location: Cell membrane
EC: 2.5.1.74
|
O07134 | MASFAQWISGARPRTLPNAVAPVVAGTGTAAWLHSAVWWKALLALVVAVALVIGVNYANDYSDGIRGTDDHRAGPMRLVGSRLAFPRSVLTAAVVGLTVSTVAGLALALLSAPWLIMVGATCIAGAWLYTGSSKPYGYKGFGEVAVFVFFGLVAVLGTEYTQALRVDWVGLVLAVSTGALSSSVLVANNLRDIHTDTQSHKFTLAVRLGDAHTRQLYQALLVATGVLTVVLMVATSWCAVGLVATPLALRAMRPVRSGRMGPDLTPVLRDTGLAMVVWAIAVAGALTLAGSVTY | Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30671
Sequence Length: 294
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Subcellular Location: Cell membrane
EC: 2.5.1.74
|
P73962 | MTESSPLAPSTAPATRKLWLAAIKPPMYTVAVVPITVGSAVAYGLTGQWHGDVFTIFLLSAIAIIAWINLSNDVFDSDTGIDVRKAHSVVNLTGNRNLVFLISNFFLLAGVLGLMSMSWRAQDWTVLELIGVAIFLGYTYQGPPFRLGYLGLGELICLITFGPLAIAAAYYSQSQSFSWNLLTPSVFVGISTAIILFCSHFHQVEDDLAAGKKSPIVRLGTKLGSQVLTLSVVSLYLITAIGVLCHQAPWQTLLIIASLPWAVQLIRHVGQYHDQPEQVSNCKFIAVNLHFFSGMLMAAGYGWAGLG | Function: Involved in the synthesis of phylloquinone (vitamin K1). Catalyzes the transfer of a prenyl chain to 2-carboxy-1,4-naphthoquinone.
Catalytic Activity: 1,4-dioxo-2-naphthoate + H(+) + phytyl diphosphate = CO2 + demethylphylloquinone + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33247
Sequence Length: 307
Pathway: Cofactor biosynthesis; phylloquinone biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.5.1.130
|
Q8GYN9 | MADSNELGSASRRLSVVTNHLIPIGFSPARADSVELCSASSMDDRFHKVHGEVPTHEVVWKKTDFFGEGDNKEFVDIIYEKALDEGIAKITINRPERRNAFRPQTVKELMRAFNDARDDSSVGVIILTGKGTKAFCSGGDQALRTQDGYADPNDVGRLNVLDLQVQIRRLPKPVIAMVAGYAVGGGHILHMVCDLTIAADNAIFGQTGPKVGSFDAGYGSSIMSRLVGPKKAREMWFMTRFYTASEAEKMGLINTVVPLEDLEKETVKWCREILRNSPTAIRVLKAALNAVDDGHAGLQGLGGDATLLFYGTEEATEGRTAYMHRRPPDFSKFHRRP | Cofactor: The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.
Function: Involved in the biosynthesis of phylloquinone (vitamin K1). Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) (By similarity).
Catalytic Activity: 2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
Sequence Mass (Da): 37056
Sequence Length: 337
Subcellular Location: Peroxisome
EC: 4.1.3.36
|
P23966 | MAEWKTKRTYDEILYETYNGIAKITINRPEVHNAFTPKTVAEMIDAFADARDDQNVGVIVLAGAGDKAFCSGGDQKVRGHGGYVGDDQIPRLNVLDLQRLIRVIPKPVVAMVSGYAIGGGHVLHIVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEQLEEETIKWCEEMLEKSPTALRFLKAAFNADTDGLAGIQQFAGDATLLYYTTDEAKEGRDSFKEKRKPDFGQFPRFP | Cofactor: The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.
Function: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
Catalytic Activity: 2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
Sequence Mass (Da): 29899
Sequence Length: 271
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7.
EC: 4.1.3.36
|
P0ABU1 | MIYPDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNIGVIILTGAGDKAFCSGGDQKVRGDYGGYKDDSGVHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGASYMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMTEEGQEGRNAFNQKRQPDFSKFKRNP | Function: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
Catalytic Activity: 2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
Sequence Mass (Da): 31633
Sequence Length: 285
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7.
EC: 4.1.3.36
|
A6W5P6 | MNPSTALATVLVDTLVRLGLRHLVLSPGSRSAPLAYAAARAADEGRLTLHVRVDERSAGFLALGLARAGELVAVVTTSGTAVANLHPAVLEAHHAGVPLVVLSADRPHELRGSGASQTADAQARMFLPSVRYSADVPAPVDPDRQAPAWRSLLSRAVAFARGLRGDGPGPVHLNVGFADPLTPSPGDVPPGPGLTQVHGPGAPAPVALERGPRTLVLAGDAPDPATGAAARELAESAGWPLLAEPSSGARGGERAVGPYRLLLDAVDAEGPLGAVERVVLFGHPTLSRPVTRLLARDDVELVVVSAAGTWSDAGFRAARVVPAAQVQGPPGAGEQEFAARWDRAGKLAADAVDAALDAEAGLSGPWAAREVVAACAADGSTLVVAASNAIRDVDLTARPLGVRTVSNRGLAGIDGTTATAEGVALATGPTRLLLGDLAFLHDANALLPVPGEVRPDLTVVVVNDDGGGIFETLEHASAVDRATFERVVATPHGVDVAALCAAFGVAHSRPATRAEALAALTARPRGLRVVELVTARDRVRPRLERIAAAVRAAVA | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 56606
Sequence Length: 555
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
|
Q9CHK0 | MTNEYLAPFVDELFNLGVREAVFSPGSRSTALAMLFEEYKKYDTYVNIDERSAAFFALGIAKAKKRPVVLVCTSGSAAAHHFPAVLEAKMSRVPLIILTADRPAELQFVGAPQTVDQTRFFGNFVNHFENLEAPHIQKQSQTENFWTYPRKVAQRAVLSAISPLSGPVQINVPLRDLLVPELKSENYEKGRSKHAFKFYEGQAQVILPFDEALLSGKTLILAGANFDKDYSEALLKLAEQLKAPILADPLSNLRNHNHPLVIDSYDAFLANNDLKTQLKADAILLFGQMPVSKRLQQFVAFNNEAEFIQVDPALDYRNPSLTTTTMVQSDVLPFASSIKKVNSDSSYLEKWQNAQEKMRQLLEKVTYEESPFEGRYVQELQKHLEALDAQLLVSNSMEIRDIDYWWKKADAKVRILGNRGVNGIDGTESTALGIATTGKPTVLLTGDLSMLHDLNGLIVGKTHELNLTIVLFNNDGGGIFHHLAQKGVPNFDYLFSTPHGLNFAGLAELTGLDYHLVSGYADFGQQFEASLHQSGIHLLEIKTDKDLSLALHQKYTTYEN | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 62524
Sequence Length: 560
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
|
B1MZ27 | MVNDTLTINTKHLLYALYASGVKHFVVSPGSRTTPIALMLAEYERQNSEIVVYIDVDERSAGFFALGIAKTRQEPVVVLGTSGTAITEYMPAVAEAKVSHIPLIVLSTDRPAELQNNGAPQTLPQHRLFGELTPYFVSFTLQDEHEDNTAYIDYMTQKLVHSAMDTGQPLQINLPLRKPLMPKLHDSHDVSITPLTFEKTHIHILPIVIKQTHVVILAGPNEAADYKDELLQFSRDHQVPVIADILSRARTTDTIFGVDSLIKAHYLTDEYRPDLVIRFGGTPVSARVLQWLQRENIPVWHVDGHAGNDHSRHVTRAFQMTPTAFLTQLALTNDMTFYQRWQQLNDIPRHAVGEASVSCMLNRILPENTAVFVANSMAIRDMDDVFSGRTTQKIYANRGVNGIDGVVSTALGMSTVSSQRSILLTGDLTLFHDMNGLMMAKKYQLNIDIIVINNNGGSIFSFLPQSQADEYFEDMFGTPLDLDMSKVAYLYDMPYIQLKGAAALGECLSHQVHGPRLIEINFDRQENVANHRELLELNQHE | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 60615
Sequence Length: 541
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
|
Q8Y6K9 | MTNHEQVLTDYLAAFIEELVQAGVKEAIISPGSRSTPLALMMAEHPILKIYVDVDERSAGFFALGLAKASKRPVVLLCTSGTAAANYFPAVAEANLSQIPLIVLTADRPHELRNVGAPQAMDQLHLYGSHVKDFTDMALPENSEEMLRYAKWHGSRAVDIAMKTPRGPVHLNFPLREPLVPILEPSPFTATGKKHHHVHIYYTHEVLDDSSIQKMVTECTGKKGVFVVGPIDKKELEQPMVDLAKKLGWPILADPLSGLRSYGALDEVVIDQYDAFLKEAEIMDKLTPEVVIRFGSMPVSKPLKNWLEQLSDIRFYVVDPGAAWKDPIKAVTDMIHCDERFLLDIMQQNMPDDAKDAAWLSRWTSYNKVAREIVLAEMANTTILEEGKIVAELRRLLPEKAGLFIGNSMPIRDVDTYFSQIDKKIKMLANRGANGIDGVVSSALGASVVFQPMFLLIGDLSFYHDMNGLLMAKKYKMNLTIVIVNNDGGGIFSFLPQANEPKYFESLFGTSTELDFRFAAAFYDADYHETQSVDELEEAIDKASYHKGLDIIEVKTNRHENKANHQALWAKIADALKALN | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 64685
Sequence Length: 580
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
|
B1HY21 | MSERKNLTDYVYKMVASLVQVGVENVVVSPGSRSTPLAYAVASTKQIKMYRQVDERSAAFFALGLAKATAKPVVLLCTSGTAAANYFPAIVEASYARVPLIIITADRPHELREVGAPQTINQPHLYGSHVKWSVDFPLADGAAPTLPFIERHIARAVAIATSAPFGPVHLNVPFREPLLIDLQDELPTMTFKHSSMGQLIPTTSAMQELSSILNSTRKGFMIVGELALGTDLAFLWEFVRQLKWPVIVESLSNMRAAVPEDCLPYLVTTYDAIMKSEDFKALVQPDTVLRIGAQPVSKFIMQFITKTQPSAYVIIDEDPMFRDATGVSTHFIHANIDQWLTHLTLTNTAFEESYLAEWQKANQLASTYIEQYSEIEKDEGAMVSRLLKMIPDGSDIFVSSSMPVRDIDTFLLATPKDIRFFANRGTNGIDGVVSTALGFSQGNDRETYLLIGDLAFLHDVNGLIATRYQECNLTILVMNNDGGGIFSYLPQSTVEAHYEDLFGTPTALEFQDIAHMYNMDYVRVDTIAELSGKFSSVKKRPLRLVEIFTDRAENVQAHRELWNRINAELKA | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 63508
Sequence Length: 571
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
|
A0QLC9 | MNPSTTQARVVVDELIRGGVRDVVLCPGSRNAPLAFALADADRAGRIRLHVRIDERTAGYLAIGLAIAAGAPVCVAMTSGTAVANLGPAVVEANYARVPLIVLSANRPYELLGTGANQTMEQLGYFGTQVRAAISLGLAEDAPERLDALNATWRSATCRVLAAATGSRTANAGPVQFDIPLREPLVPDPEPHGAPTPAGRPGGRPWTYTPPVSFDQPLDIDLSPDTVVIAGHGAGTHPNLAQLPTVAEPTAPAPDNPLHPLALRLLRPKQVIMLGRPTLHRPVSALLADPQVPVYALTTGPRWPDVSGNSQATGTRAVTTGAPSPAWLHRCEQANRHAVAAVRGQLAAHPLTTGLHVAAAVADALRPGDQLVLGASNPVRDAALVGLDSHHIRVRSNRGVAGIDGTVSTAIGAALAHEAAHDGRTVALIGDLTFVHDSSGLLIGPTEPTPRRLTIVVSNDNGGGIFELLEQGDPRFSDVSSRVFGTPHDVDVGALCRAYHVESAQIEVGELAAALDEPGPGMRVLEVKADRSSLRQLHAAIKAAL | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 56722
Sequence Length: 545
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
|
P9WFW8 | MSAHVATLHPEPPFALCGPRGTLIARGVRTRYCDVRAAQAALRSGTAPILLGALPFDVSRPAALMVPDGVLRARKLPDWPTGPLPKVRVAAALPPPADYLTRIGRARDLLAAFDGPLHKVVLARAVQLTADAPLDARVLLRRLVVADPTAYGYLVDLTSAGNDDTGAALVGASPELLVARSGNRVMCKPFAGSAPRAADPKLDAANAAALASSAKNRHEHQLVVDTMRVALEPLCEDLTIPAQPQLNRTAAVWHLCTAITGRLRNISTTAIDLALALHPTPAVGGVPTKAATELIAELEGDRGFYAGAVGWCDGRGDGHWVVSIRCAQLSADRRAALAHAGGGIVAESDPDDELEETTTKFATILTALGVEQ | Function: Catalyzes the conversion of chorismate to isochorismate.
Catalytic Activity: chorismate = isochorismate
Sequence Mass (Da): 38938
Sequence Length: 372
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
EC: 5.4.4.2
|
Q9CPI5 | MDNLQSIKAQFIAQINAYQPEKDRDIVVFQCNTETTFSLLAWLKAQQYYPQFYLHGRDGATKWASIGQVRQFSDVSAAAHFIQEQQLALLGGLQFYGDALFVLPRLLLQQRQDGMTITLFIDGKQFEQDKLVALACLSTFEKQTALQTVKQEISLISQKADQAEWCRWVEQGLQKIKQGELSKIVLANERCFKTAAPLAATDLLAESEKYNLGCYHFMLAESEQRAFIGSSPELLYRRHGLQLKTEALAGTAFMGEDEQQNQQQSDWLLHDKKNEYENQLVVDGICQNLQPFVQQITIEKVELKKLRKVQHLRRRISAQLKAGCGDKDILLAMHPTAAVAGLPQLEAKQALRKLENFDRTWYAGTLGVMGPAYADFCVTIRSAFIEQAENDSQLCVFAGAGIVEGSIPLLEWREIERKAMGLVSLLQQNQL | Function: Catalyzes the conversion of chorismate to isochorismate.
Catalytic Activity: chorismate = isochorismate
Sequence Mass (Da): 48727
Sequence Length: 431
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
EC: 5.4.4.2
|
Q3ED65 | MAALLGIVSPVTFTGKHPVNSRSRRRTVVKCSNERRILFNRIAPVYDNLNDLLSLGQHRIWKNMAVSWSGAKKGDYVLDLCCGSGDLAFLLSEKVGSTGKVMGLDFSSEQLAVAATRQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFNKSNQSVTTFMQGWMIDNVVVPVATVYDLAKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMGNLVAMR | Function: Involved in the biosynthesis of phylloquinone (vitamin K1). Methyltransferase required for the conversion of 2-phytyl-1,4-beta-naphthoquinol to phylloquinol.
Catalytic Activity: demethylphylloquinol + S-adenosyl-L-methionine = H(+) + phylloquinol + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29051
Sequence Length: 261
Subcellular Location: Plastid
EC: 2.1.1.329
|
A1JKU0 | MTLACCKLDPHPQSPARQHTGPWLVWLHGLLGSGQDWLPVAELCGDYPSLLIDLPGHGNSVALTTTGFEDISRQISETLQANGIREYWLAGYSLGGRIAMYHACYGHKVGLQGLLVEGGNLGLESDELRKARFEQDCQWAQRFRHEPLPQVLADWYQQDVFADLDSQQREQLVAVRANNHGPAVADMLEATSLGHQPWLLPALQCLSVPYTYLCGERDHKFQQVAHQYKLPLRTLARAGHNAHRANPGAFAALVLSFLSQSSFLPLSSFLPPSR | Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
Catalytic Activity: 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate + pyruvate
Sequence Mass (Da): 30412
Sequence Length: 274
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
EC: 4.2.99.20
|
P77781 | MIWKRKITLEALNAMGEGNMVGFLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL | Function: Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB.
Catalytic Activity: 1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA + H(+)
Sequence Mass (Da): 14945
Sequence Length: 136
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 7/7.
EC: 3.1.2.28
|
A0A0H3GEM5 | MGLQETIGIEIVSVEKGKAVVQLEVTEKVHQPFGYLHGGVSVVLAEHAASIGAAKSIEPDEIVFGLEINANHLASKQAGLVTATAEAIHIGKSTQVWEIKITDETEKLLCISRCTIAVKKKRK | Function: Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A . Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol .
Catalytic Activity: 1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA + H(+)
Sequence Mass (Da): 13198
Sequence Length: 123
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 3.1.2.28
|
A0QRI8 | MNTRADVVVVGAGPAGSAAAAWAARAGRDVVVVDAAQFPRDKACGDGLTPRAVAELQRLGMASWLDTRIRHHGLRMSGFGADVEIPWPGPSFPATSSAVPRTELDDRIRSVAADDGAKMMLGTKVVDVTHDSSGRVDAVVLDDGNTVGCAQLIVADGARSTLGRVLGRTWHRETVYGVAIRGYIASPRASEPWITSHLELRSPEGKVLPGYGWMFPLGNGEVNIGVGALATAKRPADAALRPLMSYYADLRREEWGLVGEPRAGLSALLPMGGAVSGVAGPNWMLIGDAAACVNPLNGEGIDYGLETGRLAAELMTSGGVTDYSSAWPTLLQEHYARGFSVARRLALLLTLPRFLQVTGPVAMRSATLMTIAVRVMGNLVTDEDADWIARVWRTAGLASRRIDQRVPFS | Function: Catalyzes the reduction of a single double bond in the isoprenoid tail of menaquinone (MK-9) in M.smegmatis, likely the beta-isoprene unit, forming the predominant form of menaquinone found in mycobacteria, MK-9(II-H2).
Catalytic Activity: AH2 + menaquinone-9 = A + beta-dihydromenaquinone-9
Sequence Mass (Da): 43404
Sequence Length: 409
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 1.3.99.38
|
P9WNY8 | MSVDDSADVVVVGAGPAGSAAAAWAARAGRDVLVIDTATFPRDKPCGDGLTPRAVAELHQLGLGKWLADHIRHRGLRMSGFGGEVEVDWPGPSFPSYGSAVARLELDDRIRKVAEDTGARMLLGAKAVAVHHDSSRRVVSLTLADGTEVGCRQLIVADGARSPLGRKLGRRWHRETVYGVAVRGYLSTAYSDDPWLTSHLELRSPDGAVLPGYGWIFPLGNGEVNIGVGALSTSRRPADLALRPLISYYTDLRRDEWGFTGQPRAVSSALLPMGGAVSGVAGSNWMLIGDAAACVNPLNGEGIDYGLETGRLAAELLDSRDLARLWPSLLADRYGRGFSVARRLALLLTFPRFLPTTGPITMRSTALMNIAVRVMSNLVTDDDRDWVARVWRGGGQLSRLVDRRPPFS | Function: Catalyzes the reduction of a single double bond in the isoprenoid tail of menaquinone (MK-9) in M.tuberculosis, likely the beta-isoprene unit, forming the predominant form of menaquinone found in mycobacteria, MK-9(II-H2).
Catalytic Activity: AH2 + menaquinone-9 = A + beta-dihydromenaquinone-9
Sequence Mass (Da): 43870
Sequence Length: 408
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 1.3.99.38
|
Q9BUN1 | MVPAAGALLWVLLLNLGPRAAGAQGLTQTPTEMQRVSLRFGGPMTRSYRSTARTGLPRKTRIILEDENDAMADADRLAGPAAAELLAATVSTGFSRSSAINEEDGSSEEGVVINAGKDSTSRELPSATPNTAGSSSTRFIANSQEPEIRLTSSLPRSPGRSTEDLPGSQATLSQWSTPGSTPSRWPSPSPTAMPSPEDLRLVLMPWGPWHCHCKSGTMSRSRSGKLHGLSGRLRVGALSQLRTEHKPCTYQQCPCNRLREECPLDTSLCTDTNCASQSTTSTRTTTTPFPTIHLRSSPSLPPASPCPALAFWKRVRIGLEDIWNSLSSVFTEMQPIDRNQR | Function: Involved in control of cellular proliferation. Onconcogenic modifier contributing to the tumor suppressor function of DNMT3B.
PTM: Phosphorylation sites are present in the extracellular medium.
Sequence Mass (Da): 36769
Sequence Length: 341
Subcellular Location: Secreted
|
Q569E4 | MVPAACMLLWALLLSLEYRAAGAEDQTTTPTATTIGMQRVSFRFGGPARSLHSTNPTARTTVPGKLRVTLEDENDALATADRLALPAAAELLSTVTGYSRSSVPSPSDWEEDGSLEEGVVDTRKTTNGPVSLFSTTNTVGSSGTTGRFLANSQEREIKLTTDVRSLSSKTTVVDLSSESTLQQWSTPGSTPSPWLKPSFTAMPSPEDLRVVLMPWGPWHCHCKSGTMSRSRAGKLHGLSGRLRVGALNELRTEHRPCTYQLCACNRHLEECPLDSSLCSDHSCSSRAPFQSSTTSLVPVHLRRRPILPPTSPSPSPALAFWKRVRIGLEDIWNSLSSVFTETQPVERIQR | Function: Involved in control of cellular proliferation. Onconcogenic modifier contributing to the tumor suppressor function of DNMT3B.
PTM: Phosphorylation sites are present in the extracellular medium.
Sequence Mass (Da): 38118
Sequence Length: 350
Subcellular Location: Secreted
|
P30341 | MLQAHTGYDLAIIGSGAGAFAAAIAARNKGRSVVMVERGTTGGTCVNVGCVPSKALLAAAEARHGAQAASRFPGIQATEPALDFPALISGKDTLVGQLRAEKYTDLAAEYGWQIVHGTATFADGPMLEVALNDGGTATVEAAHYLIATGSAPTAPHIDGLDQVDYLTSTTAMELQQLPEHLLILGGGYVGLEQAQLFARLGSRVTLAVRSRLASREEPEISAGIENIFREEGITVHTRTQLRAVRRDGEGILATLTGPDGDQQVRASHLLIATGRRSVTNGLGLERVGVKTGERGEVVVDEYLRTDNPRIWAAGDVTCHPDFVYVAAAHGTLVADNALDGAERTLDYTALPKVTFTSPAIASVGLTEAQLTEAGIAHQTRTLSLENVPRALVNRDTRGLVKLIAERGTGKLLAAHVLAEGAGDVITAATYAITAGLTVDQLARTWHPYLTMAEALKLAAQTFTSDVAKLSCCAG | Cofactor: Binds 1 FAD per subunit.
Function: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
Catalytic Activity: H(+) + Hg + NADP(+) = Hg(2+) + NADPH
Sequence Mass (Da): 49671
Sequence Length: 474
EC: 1.16.1.1
|
P16172 | MKTEIQEIVTRLDQQSNKGEGGESMKWLFRPLLQMLAGGESVTIEDMATTTGKPVEEVKKVLQSLPSVEIDEQGRVVGLGLTLIPTPHHFTVDGKQLYAWCALDTLIFPALIGRSVNIESPCHSTGEPIRLNVEPDHIVSVEPSTAVVSIVTPDDMSSIRTAFCNEVHFFSSPNAAEDWLDQHPGGKVLSVEDAFELGRLMGTRYEESRPANGSCCDI | Function: Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase.
Catalytic Activity: an alkylmercury + H(+) = an alkane + Hg(2+)
Sequence Mass (Da): 23863
Sequence Length: 218
EC: 4.99.1.2
|
Q8G9P0 | MDKTIYSKKIAESLSSGNHPEEFATLFVTLLRQLVMGRPVSREALGTALGWSGQRVATVLEPAPGTEYDEQGNIIGLGLTLRETPHVFEVDGRRLYTWCALDTLMFPALIGKTARVTSRCVATGRPITLTVAPEAVLQVEPAETMVSLLTPDASPDIRCSFCCHVHFFASPSVANAWASTHPGIELVPVENAFGLGHLIAHKLLEDSERNTA | Function: Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase.
Catalytic Activity: an alkylmercury + H(+) = an alkane + Hg(2+)
Sequence Mass (Da): 22981
Sequence Length: 212
EC: 4.99.1.2
|
P30342 | MDSQAQQLATRLTTAFNGGGAASSRPWLWRPLLQLLAQGRPVTVEQIAQATDRTPDQVREALAANPDTEYDERGRITGSGLTQNPTPHHFEVDGQQLYTWCALDTLIFPAILGRPAHVTSPCHATGTPVRLTVEPDQVTSVEPATAVVSIVTPDAPASIRTAFCNQVHFFATPDAGKGWLEEHPVATVLPVADAYQLGRPLTEALLTGDTPPGCC | Function: Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase.
Catalytic Activity: an alkylmercury + H(+) = an alkane + Hg(2+)
Sequence Mass (Da): 23026
Sequence Length: 215
EC: 4.99.1.2
|
P22905 | MSAITRIIDKIGIVGTIVGSFSCAMCFPAAASLGAAIGLGFLSQWEGLFVQWLIPIFASVALLATLAGWFSHRQWQRTLLGSIGPVLALVGVFGLTHHFLDKDLARVIFYTGLVVMFLVSIWDMVNPANRRCATDGCETPAPRS | Function: Involved in mercuric ion uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15526
Sequence Length: 144
Subcellular Location: Cell inner membrane
|
Q50919 | MGLMTRIADKTGALGSVVSAMGCAACFPALASFGAAIGLGFLSQYEGLFISRLLPLFAALAFLANALGWFSHRQWLRSLLGMIGPAIVFAATVWLLGNWWTANLMYVGLALMIGVSIWDFVSPAHRRCGPDGCELPAKRL | Function: Involved in mercuric ion uptake and binding. MerC-mediated Hg(2+) uptake does not require MerP.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14964
Sequence Length: 140
Subcellular Location: Cell inner membrane
|
A0JN95 | MLRYPYFCRIHKNFLSCWLESGIYNLGVWPKKIHATAERYNEYEAQEETDQTGIQELHRSQDRDSGVMTKLHIPVMVDEVVRCLAPQKGQVFLDMTFGSGGHTRAILQKEPDITLYALDRDPTAYAIAEQLSELYPKQIRAILGQFSQAEALLMKAGVQPGTLDGVLLDLGCSSMQLDTPERGFSLRKDGPLDMRMDGDRYPDMPTAADVVNALDQQALASILRAYGEEKHAKKIASAIIQARGLYPITRTQQLASIVAGAFPPSALYARKDLLQRPTHIATKTFQAFRIFVNNELNELYTGLKTAQKFLRPGGHLVALSFHSLEDRIIKRFLLGISMTERFNLSARQKVIQKSQLDSDQENKEGVSTGKAPLMWKLIHKKVLTPEDEDVQDNPRGRSAKLRAAIKL | Function: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA. Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits.
Catalytic Activity: cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 45768
Sequence Length: 407
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.-
|
A6NJ78 | MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLRPGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSVRQQVMKTSQLGSDHENTEEVSMRRAPLMWELIHKKVLSPQDQDVQDNPRGRSAKLRAAIKL | Function: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA . Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits .
Catalytic Activity: cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46121
Sequence Length: 407
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.-
|
Q9DCL4 | MLRYPYFYRTYNRLFSHFVDSGASNLDVCPHTIHTAVALHTESKAVEGTALCGPQKVYSSEEKELEAMAKLHIPVMVDQVVHCLAPQKGQVFLDMTFGSGGHTRAILQKEPDVMVYALDRDPVAYAIAEQLSRLYPTQIQALLGQFSQAEALLMKAGVQPGTIDGILMDLGCSSMQLDAPERGFSLRKDGPLDMRMDGDRYPDTPTASDVVNALDQQALASILRAYGEEKHAKKIASAIIQARSTYPISRTQQLASIVAGAFPPSAVYARKDLLQRSTHIATKTFQALRIFVNNELNELYAGLRTAEKFLKTGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSIRQKVKQTSQLDSDQETEERHSVRAPLKWELIHKKVLTPEDQDVQDNPRGRSAKLRAAIKL | Function: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA. Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits.
Catalytic Activity: cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 45282
Sequence Length: 406
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.-
|
Q5R5T5 | MIRYPYFCRMYKECLSCWLESGIPNLGVWPKTIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVLHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAETLLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNAFDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYARKDLLQRSTHIATKTFQAVRIFVNNELNELYMGLKTAQKFLRPGGRLVALSFHSLEDRIIKRFLLGISMTERFNLSVRQQVMKTSQLGSDHENTEEVSKRRAPLMWELIHKKVLSPQDQDVQDNPRARSAKLRAAIKL | Function: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA. Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits.
Catalytic Activity: cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46169
Sequence Length: 407
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.-
|
Q09357 | MSQNNEMHPRNPYRNKPPDFKALAVEYPEFRKFCQYVSNGKVTFDFKKDAAVRCLTQTLLKKDFNLDVEIPPGHLVPRVPQKLNYCLLIDDLLKANKLTKNVIGIDIGTGTSCIHALIGARQFNWKFIATDGDEKSVRVAHENVAKNGLSSSICVVHVNPDVKTVLMDVVNTIPDTDYAFCMCNPPFFEKGNGDDKFCEDISSSTETYSNRVASEFRTAPHSATFASSAELFVDGGEVAFVNRIIDDSVLLRDRIKIYTTMIGRKSSLKPLQNRLQRFGDDVKIMISVLNQGKTKRWMLAWTFSKSVSLTTIDRPISFQCPKPGLTRLMQEISILNGRLRQEDTLAIVAEFKCVTWTNQRARKRAKAILSESSIKKAKWNFSNVACQVAFGAGDGKDSYTDAGNFVSSESIPTNNLNAWDNASQAYFPLPNGEVPGPIIRIRIQVFSEDSYDSISFELISGSKQHLHQLVQYLKNLICR | Function: RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating splicing of S-adenosylmethionine synthase transcripts (sams-3, sams-4 and sams-5) . Able to N6-methylate a subset of mRNAs containing the 5'UACAGAAAC-3' nonamer sequence . Plays a key role in S-adenosyl-L-methionine homeostasis: under rich-diet conditions, catalyzes N6-methylation of S-adenosylmethionine synthase mRNAs (sams-3, sams-4 and sams-5), directly inhibiting splicing and protein production of S-adenosylmethionine synthase . In addition to mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6 snRNA) . Required for gamete production, inhibiting germ cell proliferative fate and ensuring germ cell meiotic development . Also promotes progression of the mitotic cell cycle in those germ cells that continue to proliferate . Plays a role in the development of the vulva, somatic gonad and embryo .
Catalytic Activity: an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53805
Sequence Length: 479
Subcellular Location: Nucleus
EC: 2.1.1.346
|
Q6DC64 | MALNKSMHPRNRYKDKPPDFVYLASKYPEFQKHVQTTLTGRVTLNFKDPEAVRALTCTLLKEDFGLTIEIPLERLIPTVPLRLNYIHWVEDLIGGQGNPQRGIDIGTGASCIYPLLGATMNGWFFLATEVDDICFNYAKKNVEQNHLAELIKVVKVPQKTLLMDALKEESIVYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSINTGGVTEIMAEGGELEFVKRVIHDSLQLKKRLRWYSCMLGKKCSLAPLKDELRKQGVAKVTHTEFCQGRTMRWALAWSFYDDVPVPSPPCKKRKLEKARKPLTFTVLKATVAELQAQTPHSSPTESVSAWLENILTDLKVLHKRVPGGEVELSLFLTAVENTWIHSRQKRREQGRHLRELPRAQEPPSEETSVTEQQQQPDIPPESPANAEALQHFLFKCLVNVKQEEEKDVLVEMHWVEGQNKDLMNQLCTCLKNALFRQVAKPT | Function: RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts. Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs). In contrast to the METTL3-METTL14 heterodimer, only able to methylate a limited number of RNAs: requires both a 5'UACAGAGAA-3' nonamer sequence and a specific RNA structure. Plays a key role in S-adenosyl-L-methionine homeostasis by mediating N6-methylation of MAT2A mRNAs, altering splicing of MAT2A transcripts: in presence of S-adenosyl-L-methionine, binds the 3'-UTR region of MAT2A mRNA and specifically N6-methylates the first hairpin of MAT2A mRNA, impairing MAT2A splicing and protein expression. In S-adenosyl-L-methionine-limiting conditions, binds the 3'-UTR region of MAT2A mRNA but stalls due to the lack of a methyl donor, preventing N6-methylation and promoting expression of MAT2A. In addition to mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6 snRNA): specifically N6-methylates adenine in position 43 of U6 snRNAs.
Catalytic Activity: adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53621
Sequence Length: 471
Domain: The VCR (vertebrate conserved) regions bind the first hairpin of MAT2A mRNAs. The VCR regions interact with the internal stem-loop within U6 snRNAs, inducing the conformational rearrangement of the A43-containing region of U6 snRNA, thereby modifying the RNA structure to become suitable for productive catalysis by the methyltransferase region.
Subcellular Location: Nucleus
|
Q554C9 | MSEIDTNDIKKEMDNKNYRDPTDNKELLKWTKKKRKRSNDSMHINNFYRYNPPNFKLLASKYPTFDKYIINKTEKIYNIDWKDSNATKELTRVLLDHDFGLRIELPDNYLCPTLTLRINYLYWISDQLKNLKIILNDNDNDNKIIKGIDIGTGTSCIFPLLGAKLFNNWSFIGIDIDDKVLEYAQNNITINSLNSKITLFKNEKNSDILLKLLNYKEGSNTFNSSNDDHQDNHDDDDDDEEYFADFCLCNPPFFKDLNENNNNKNNNPKSNCTGSVNEMVTDGGEFEFVKRIIKESFQLKCKIRFYTTMIGRKVNLNPLINILIKQYYLPKNQIQTTELVQGNTSRWVLSWYFLNKSTNLETKENNNINNNNNNNNNNNINNNNQFLTRMERRKLYREGITLNLDSDDNNNNNNNNNNNNNNNNNNNNNNNNNNNKIVEIIKLILDNNDIIYKTDENNIKYECKYLLNNVIVGSSIKLDRDIEFLFTIFIDLTTRLILFKPIDPKINNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNNNNSCDGEIINSNLFFILKFLENIKNEIKLK | Function: RNA N6-methyltransferase that mediates N6-methylation of adenine of U6 small nuclear RNA (U6 snRNA).
Catalytic Activity: adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 66632
Sequence Length: 568
EC: 2.1.1.346
|
Q290Z2 | MVRNKKNKYAMHPRNILRVPPDYTKLAIKYRDFRQVCELELTGKVSVNFRNEKTLRELSKMLLKEYFELDVDFAPGSLVPTLALRLNYILWLEDMLLPLNLETVRGIDVGCGSSCIYSLLGAKKNGWNMLALESKEENIDYARENVRRNNLEDLIEVYAQPDKSNIFKSYFETEKLRKEFHFCLCNPPFFDSNSPNPFGGNTRNPQRRPAPNNVRTGSAEELTCEGGEVHFVQRIIEESQLNKQRVLIFTSMLGVKASVPKILDYLKERQITNVTTTEFHQGHTTRWAVAWSHQPTPLSPGTQCN | Function: RNA N6-methyltransferase that mediates N6-methylation of adenine of U6 small nuclear RNA (U6 snRNA).
Catalytic Activity: adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35174
Sequence Length: 305
EC: 2.1.1.346
|
P56859 | MPAKMHSNYPSDSETAELRDSTESGYVSGGSSEEYLPEIVFTKPHLQFLNRQLQFLEPQDVLRWCVTSLPHLYQTTAFGLTGLVIMDMLSKLSIPRPQMVNLIFLDTLHHFPETLKLVDNVRKRYPLQHIHVYKPQGVETEEEFAKKHGERLWEKDDQLYDWIAKVEPAQRAYRELNVHAVLTGRRRSQGGKRGDLDIIEVDEAGLIKINPLANWTFDQVKQYVKENDIPYNELLDKGYKSVGDYHSTSPVKENEDERSGRWKGQAKTECGIHNPRSKYAQYLMDMERKRQEEALSQALQNKLTTA | Function: The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.
Catalytic Activity: [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol
Sequence Mass (Da): 35447
Sequence Length: 306
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3.
EC: 1.8.4.8
|
Q86W50 | MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHVQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKSTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIIYDFCMCNPPFFANQLEAKGVNSRNPRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTYTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLASVMKELSLKASPLRSETAEGIVVVTTWIEKILTDLKVQHKRVPCGKEEVSLFLTAIENSWIHLRRKKRERVRQLREVPRAPEDVIQALEEKKPTPKESGNSQELARGPQERTPCGPALREGEAAAVEGPCPSQESLSQEENPEPTEDERSEEKGGVEVLESCQGSSNGAQDQEASEQFGSPVAERGKRLPGVAGQYLFKCLINVKKEVDDALVEMHWVEGQNRDLMNQLCTYIRNQIFRLVAVN | Function: RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts . Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs) . In contrast to the METTL3-METTL14 heterodimer, only able to methylate a limited number of RNAs: requires both a 5'UACAGAGAA-3' nonamer sequence and a specific RNA structure . Plays a key role in S-adenosyl-L-methionine homeostasis by mediating N6-methylation of MAT2A mRNAs, altering splicing of MAT2A transcripts: in presence of S-adenosyl-L-methionine, binds the 3'-UTR region of MAT2A mRNA and specifically N6-methylates the first hairpin of MAT2A mRNA, preventing recognition of their 3'-splice site by U2AF1/U2AF35, thereby inhibiting splicing and protein production of S-adenosylmethionine synthase . In S-adenosyl-L-methionine-limiting conditions, binds the 3'-UTR region of MAT2A mRNA but stalls due to the lack of a methyl donor, preventing N6-methylation and promoting expression of MAT2A . In addition to mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6 snRNA): specifically N6-methylates adenine in position 43 of U6 snRNAs . Also able to bind various lncRNAs, such as 7SK snRNA (7SK RNA) or 7SL RNA . Specifically binds the 3'-end of the MALAT1 long non-coding RNA .
Catalytic Activity: adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 63621
Sequence Length: 562
Domain: The VCR (vertebrate conserved) regions bind the first hairpin of MAT2A mRNAs . The VCR regions interact with the internal stem-loop within U6 snRNAs, inducing the conformational rearrangement of the A43-containing region of U6 snRNA, thereby modifying the RNA structure to become suitable for productive catalysis by the methyltransferase region .
Subcellular Location: Nucleus
|
Q9CQG2 | MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKTTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIVYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLESVMKELSLKASSLGSETAEGIVVVTTWIEKILTDLKVQHKRIPCGREEVSLFLTAIENSWIHLRRKRRERVRQLREVPRAPEDVILALEERKSTPKELSSGQDVAHSPQESALCGLDVPGGEAAADGGHCLSQKLLCQEETPEATEDERDEERGGMEAMESCKGSSNGAQDGEASEKGDRLDGAAGRYLFKCLVNIKKEAGDAVVEMHWVEGQNRDLMNQLCTYVRNQILRLVAS | Function: RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts . Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs) (By similarity). In contrast to the METTL3-METTL14 heterodimer, only able to methylate a limited number of RNAs: requires both a 5'UACAGAGAA-3' nonamer sequence and a specific RNA structure (By similarity). Plays a key role in S-adenosyl-L-methionine homeostasis by mediating N6-methylation of MAT2A mRNAs, altering splicing of MAT2A transcripts: in presence of S-adenosyl-L-methionine, binds the 3'-UTR region of MAT2A mRNA and specifically N6-methylates the first hairpin of MAT2A mRNA, preventing recognition of their 3'-splice site by U2AF1/U2AF35, thereby inhibiting splicing and protein production of S-adenosylmethionine synthase (By similarity). In S-adenosyl-L-methionine-limiting conditions, binds the 3'-UTR region of MAT2A mRNA but stalls due to the lack of a methyl donor, preventing N6-methylation and promoting expression of MAT2A . In addition to mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6 snRNA): specifically N6-methylates adenine in position 43 of U6 snRNAs (By similarity). Also able to bind various lncRNAs, such as 7SK snRNA (7SK RNA) or 7SL RNA (By similarity). Specifically binds the 3'-end of the MALAT1 long non-coding RNA (By similarity) .
Catalytic Activity: adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 62341
Sequence Length: 553
Domain: The VCR (vertebrate conserved) regions bind the first hairpin of MAT2A mRNAs. The VCR regions interact with the internal stem-loop within U6 snRNAs, inducing the conformational rearrangement of the A43-containing region of U6 snRNA, thereby modifying the RNA structure to become suitable for productive catalysis by the methyltransferase region.
Subcellular Location: Nucleus
|
Q10270 | MSSIDTPANKLQAKTLFHPEHLEYINKQLSELSPQDILKWCRWTLPSLFQTSALGLSGLVIMDMLSKMDMNVPLIFINTLHHFPETLDLLEKVKTKYPNVPVHVYRCAEAANEKEFAQKFGEKLWETDESRYDFLVKVEPASRAYSDLNVLAVFTGRRRSQGGERGSLPIVQLDGPVLKINPLANWSFTEVHNYIITNNVPYNELLNKGYRSVGDWHSTQPVREGEDERAGRWRGREKTECGLHSHPQSKFAQYMAELKKKETADQ | Function: The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier (By similarity). Required for methionine synthesis.
Catalytic Activity: [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol
Sequence Mass (Da): 30561
Sequence Length: 266
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.8.4.8
|
C7C8V4 | MLDHGTPIQPVSLPAAELDLGAVGGIAWPEPVQRRLRVGLLNNMPDSALVQTERQFRRLIGPGVELRLFSLDTVPRGPLARAHLDRFYETQGALAGAGLDALVVTGAEPKAERLADEPFFPALAAVVDWADASGVPTLFSCLAAHAAVLHLDGIERRPLPTKHSGIYACTAVAHHPLLAGMPASVPVPHSRWNDLPEQALTARGYRVLRRSEQVGVDLFVRERGASMVFLQGHPEYDGDTLAREYRRDIGRFLDGERDTPPALPENYYVDEAVLRLDAFAAVARAYRSPALHADFPTMAETLPRPAAWQEAAAGLFRNWLALVSDRVALAA | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 36028
Sequence Length: 331
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.46
|
P80877 | MTTIKTSNLGFPRIGLNREWKKALEAYWKGSTDKDTFLKQIDELFLSAVKTQIDQQIDVVPVSDFTQYDHVLDTAVSFNWIPKRFRHLTDATDTYFAIARGIKDAVSSEMTKWFNTNYHYIVPEYDESIEFRLTRNKQLEDYRRIKQEYGVETKPVIVGPYTFVTLAKGYEPSEAKAIQKRLVPLYVQLLKELEEEGVKWVQIDEPALVTASSEDVRGAKELFESITSELSSLNVLLQTYFDSVDAYEELISYPVQGIGLDFVHDKGRNLEQLKTHGFPTDKVLAAGVIDGRNIWKADLEERLDAVLDILSIAKVDELWIQPSSSLLHVPVAKHPDEHLEKDLLNGLSYAKEKLAELTALKEGLVSGKAAISEEIQQAKADIQALKQFATGANSEQKKELEQLTDKDFKRPIPFEERLALQNESLGLPLLPTTTIGSFPQSAEVRSARQKWRKAEWSDEQYQNFINAETKRWIDIQEELELDVLVHGEFERTDMVEYFGEKLAGFAFTKYAWVQSYGSRCVRPPVIYGDVEFIEPMTVKDTVYAQSLTSKHVKGMLTGPVTILNWSFPRNDISRKEIAFQIGLALRKEVKALEDAGIQIIQVDEPALREGLPLKTRDWDEYLTWAAEAFRLTTSSVKNETQIHTHMCYSNFEDIVDTINDLDADVITIEHSRSHGGFLDYLKNHPYLKGLGLGVYDIHSPRVPSTEEMYNIIVDALAVCPTDRFWVNPDCGLKTRQQEETVAALKNMVEAAKQARAQQTQLV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
PTM: In response to oxidative stress, Cys-719 can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation leads to loss of catalytic activity and methionine auxotrophy.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 86806
Sequence Length: 762
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
|
Q7VRI8 | MPVLSHILGFPRIGLYRELKHALEQYWEKKITENKLLDIGRMLRMRHWKQQINSGINLIPIGDFSWYDHVLDMSIMLNNIPTRFHILSQKKNTLNMLFSIARGDSINNTTITPSEMKKWFNTNYHYIVPEFVQNQIFKLNCTQLLAEIDEALSLNHPIKPVLLGPLTYLWIGKTKETKEFDRLSLLPSLLLVYKEIFNILSKKNIQWIQIDEPALVLELPQTWLKAYLHAYDQLYQTKIKLLLTTYFGKIYHQLPIIKQLKVNGLHIDLTNCSDNDISLLHEQLPKKWILSAGIINGKNIWKTNLYDWFLKLNTITHQRSLWIGSSCSLLHSPIDLNIESKLNNNIKNWFAFAIQKCSEIKLLCDALNSNHNDNSDQQNILKKYYNTNIQRLNSNIINNPQVQERCKNIITLDHSRKTKHITRMKLQHNRFNLPLYPTTTIGSFPQTSEIRKLRLKFKNKQINEDYYYTHIQQYIKKIIQEQEKLDLDILVHGEPERNDMVEYFGENLKGFVSSQHGWIQSYGSRCIKPPIIIGDISRPIPITIPWINYAQSLTNKPVKGILTGPITIMTWSFAREDIPRHMIALQLALAIRDEVMDLEKSGIGVIQIDEPALREGLPLKKSEQSYYLKWAINTFKITVSSVKDNTQIHTHMCYSEFNEIIDDILKLDVDVISIESSRSDLQLLQFIKTAGKKLNEIGPGIYDIHSIHQPSINEIMDKLKKLLQYIPKDRLWINPDCGLKTRSWNEIRESLNNMVIAAKTLRINNGLNN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 89643
Sequence Length: 769
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
|
Q2KYF3 | MTITHNLGFPRIGAQRELKRAVEAYWAGKQTADELLATGRALRAAHWRRQADSGLRFVPVGDFAWYDHILEWTTLLGAVPARFAQPETQAVSLDTLFRMGRGRAPSGKPAAACEMTKWFDTNYHYIVPELVPGQTYRIAREDLFEQVREAQALGYAVKPVIPGPLTWLYLGKGDAFQQGASDEDKLKLLANLLPVYQQVLKRLADQGVEWVQIDEPILALDLPAAWRDAFGLAYAQLAGSPVKVLLATYFDGLKDNLSTVTKLPVAGLHVDLVRAPEQLDDVVEALHADQVLSAGVINGRNVWRTDLDQALRKLEPVARQLGDRLWLAPSCSLLHVPVDLLAETELDAELKSWLSFASQKLDELSLLGRALDGDSSQAVQEGLAAQRAALAARRSSPRIHNPAVGRRMAASEQVSRDRAPFAERIRQQQARLNLPPFPTTTIGSFPQTAEIRGLRRDWKSGALSDSTYEALIRKEIEAVIRFQEKVGLDVLVHGEPERNDMVEYFGELLAGFAFTKNGWVQSYGSRCVKPPIIFGDVARPAPMTVGWSSYAQSLTDKPVKGMLTGPVTILQWSFVRDDQPREATCRQLALALRDEVLDLEKAGVKVIQIDEPAIREGLPLRRADWQAYLDWAVDCFRLSTAGVADDTQIHTHMCYSEFNDIIESIAAMDADVITIETSRSNMELLKAFEDFHYPNDIGPGVYDIHSPNVPDVDWMVGLMQKAGANLSKERLWVNPDCGLKTRAWPETEAALISMVQAARTLRQATS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 85141
Sequence Length: 766
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
|
Q8CMP5 | MTTIKTSNLGFPRLGRKREWKKAIENYWAHKIDKAELDQTLTDLHKENLLLQKNYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGREVNDDLLFDIARGNKEHVASALIKWFNTNYHYIVPEWDNVEPKVEKNTLLERFKYAQSINVNAHPVIVGPITFVKLSKGGHQSFEEKVETLLPLYKEVLQSLVDAGAEYIQIDEPILVTDDSESYEDITRKAYDYFANEGLGKYLVIQTYFERVHLKFLSSLPVGGLGLDLVHDNGYNLKQIEDGDFDQSKALYAGIIDGRNVWAADIEAKKQLIETLQQHTQQLVIQPSSSLLHVPVSLDDETLDESIAEGLSFATEKLDELDALRRLFNDNDLSKYEHYKARYERFQSQSFKNLEYDFESVPTHRKSPFAKRKQLQNQRLNLPDLPTTTIGSFPQTREVRKFRADWKNNRITDAEYQEFLQNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPVIYGDVKWTAPLTVKETVYAQSLTDKPVKGMLTGPVTILNWSFERVDVPRKVVQDQIALAIDEEVLALEEAGIKVIQVDEPALREGLPLRSEYHEQYLEDAVHSFKLATSSVHDETQIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIQDFEDINYDLGIGLGVYDIHSPRIPTEEEITTAINRSLQQIDRSLFWVNPDCGLKTRKENEVKDALTVLVNAVKKKRQESESTTA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 85929
Sequence Length: 748
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
|
Q82LG4 | MTAKSAAAAARATVYGYPRQGRGRELKKAIEGYWKGRLDADALRTTATGLRRDTWQQLAEAGIHEVPTGDFSYYDHVLDTSVMVGAIPARHRAAVEADALDGYFAMARGTQDVAPLEMTKWFDTNYHYLVPELGPDTVFSTDSAKQVAELGEALALGLTARPVLVGPVTYLLLAKPAPGVAADFDPLTLLDRLLPVYAEVLADLRAAGAEWVQLDEPALVQDRTPAELNAAERAYRVLGGLTDRPKLLVASYFDRLGDALPVLAEAPVEGLALDFAEGAAANLDALAAVGGLPGKRLVAGVVDGRNIWVNDLEKSLALLGTLLGLADRVDVAASCSLLHVPLDAAAERDIAPQVLRWLAFARQKTAEIVTLAKGLGHGTDAIAAQLAANRADLVSRADSALTRDPAVRSRTAATTDADARRSGPYPERAAAQRARLGLPLLPTTTIGSFPQTAELRTARADLRAGRIDSAGYEERIRAEIGEVISFQEKAGLDVLVHGEAERNDMVQYFAERLTGYLTTQHGWVQSYGTRYVRPPVLAGDISRPEPMTVPWTTYAQSLTDRPVKGMLTGPVTMLAWSFVRDDQPLGETARQVALALRDEVGDLEAAGTSVIQVDEPALRETLPLRAADRPAYLAWATEAFRLTTGGVRPDTQIHTHMCYAEFGDIVQAIDDLDADVISLEAARSHMQVARELAEHAYPREAGPGVYDIHSPRVPGVDETAALLRKGLEAIPAERLWVNPDCGLKTRGWPETRASLENLVAAARTVRAEHAGS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 83151
Sequence Length: 772
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
|
Q8CWX6 | MTKVSSLGYPRLGENREWKKLIEAYWAGKVSKNDLFAGAKELRLDFLKKQLNAGLDLIPVGDFSLYDHILDLSVQFNIIPKRFAKEPIDIDLYFAIARGNKENVASSMKKWFNTNYHYIVPEWSKQRPKLNNNRLLDLYLEAREVVGDKAKPVITGPITYVALSTGVEDFTAAVKSLLPLYKQVFTELVKAGASYIQVDEPIFVTDEGKDYLQAAKAVYAYFAKEVPDAKFIFQTYFEGLIDSQVLSQLPVDAFGLDFVYGLEENLEAIKTGAFKGKEIFAGVIDGRNIWSSDFVKTSALLETIEEQSAALTIQPSCSLLHVPVTTKNETDLDPVLRNGLAFADEKLTEVKRLAEHLDGREDPAYDLHIAHFDALQAADFRNVKLEDLSRVATKRPSDFAKRRDIQQEKLHLPLLPTTTIGSFPQSREIRRTRLAWKRGDISDAEYKQFIQAEIERWIRIQEDLDLDVLVHGEFERVDMVEFFGQKLAGFTTTKFGWVQSYGSRAVKPPIIYGDVQHLEPITVEETVYAQSLTDRPVKGMLTGPITITNWSFERTDIPRDQLFNQIGLAIKDEIKLLENAGIAIIQVDEAALREGLPLRKSKQKAYLDDAVHAFHIATSSVKDETQIHTHMCYSKFDEIIDAIRALDADVISIETSRSHGDIIESFETAVYPLGIGLGVYDIHSPRVPTKEEVVANIERPLRQLSPTQFWVNPDCGLKTRQEPETIAALKVLVAATKEVRQKLGN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 84141
Sequence Length: 745
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
|
Q2RMS5 | MAQSEYLFTSESVSEGHPDKVCDRISDAIVDAFLAEDPHSRVALETMATTNFVVLAGEVRGPDSLTHDRLKEIAREAIKDIGYEQRGFHWKDAEIVSHVHSQSADIAVGVDAAGNKDEGAGDQGIMFGYACTETEELMPAPIALSHAILKSLAEFRHGGDTSFGPDSKSQVTLRYVDGKPVGAASVVVSTQHAGNLSQDEVRELVRPHVLKVLPEGWMCPEEEFYVNPTGRFVIGGPDGDCGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLAEKCVIQVSYAIGVSKPLSVYVNTQGTGQVDEQRLAVVLQQLMDLSPRGIRQHLQLSRPIYARTAAYGHFGRKPEKDGGFSWERTDLVAGLKTAFGA | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 41753
Sequence Length: 389
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
A7NVX9 | METFLFTSESVNEGHPDKLCDQISDAVLDACLQQDPDSKVACETCTKTNMVMVFGEITTKANVDYEKIVRDTCREIGFVSDDVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYHNDGGARVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVANGLARRCIVQVSYAIGVPEPLSVFVDTYGTGKIPDREILKIVKENFDFRPGMISINLDLKRGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWEKTQA | Cofactor: Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate (By similarity). Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 43114
Sequence Length: 393
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
P19358 | MSKSKTFLFTSESVGEGHPDKICDQVSDAILDACLEQDPFSKVACETAAKTGMIMVFGEITTKARLDYQQIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGLHYEKSLEDLGAGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLPWLRPDTKTQVTVEYEDDNGRWVPKRIDTVVISAQHADEISTADLRTQLQKDIVEKVIPKDMLDENTKYFIQPSGRFVIGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLCKRVQVQFSYAIGIAEPLSLHVDTYGTATKSDDEIIEIIKKNFDLRPGVLVKELDLARPIYLPTASYGHFTNQEYSWEKPKKLEF | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42256
Sequence Length: 384
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
EC: 2.5.1.6
|
Q9SJL8 | METFLFTSESVNEGHPDKLCDQISDAILDACLEQDPESKVACETCTKTNMVMVFGEITTAAKVDYEKIVRSTCREIGFISADVGLDADKCNVLVNIEQQSPDIAQGVHGHLTKKPEDIGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNKTCPWLRPDGKTQVTVEYKNDGGAMIPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPAKYLDDNTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVAAGLARRCIVQVSYAIGVPEPLSVFVDTYKTGTIPDKDILVLIKEAFDFRPGMMAINLDLKRGGNFRFQKTAAYGHFGRDDPDFTWEVVKPLKPKA | Cofactor: Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate (By similarity). Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate . Involved in the biosynthesis of lignin .
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42497
Sequence Length: 390
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
P50305 | MSQHKFLFTSESVSEGHPDKMCDQISDAVLDAHLAQDPHAKVACETVTKTGMIMLCGEITSKAVVDYQVLVRNVIKKIGYDDSSKGFDYKTCNVLVALEQQSPEIAAGVHVDKDSDDVGAGDQGIMFGYATDETEEAMPLTLLLSHKLNRKLHELRRSGELEWVRPDSKTQVTIEYASEGGACVPLRVHTVVISTQHSPDISLDDLRKELIEKVIKAVIPANLIDDKTIYHLNPCGSFIIGGPMGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPTKVDRSAAYAARWVAKSLVKSGLCRRCLVQVSYAIGVAKPLSVMVFSFGTSALNEGELLKIVNDNFDLRPGMIIKDLDLKKPIYEPTAENGHFGHNEFPWEQPRHLQIDVELLKKIGGKTISNGNGIAH | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 44034
Sequence Length: 404
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
EC: 2.5.1.6
|
P40320 | MPQKTNGHSANGCNGSNGNSYDMEDGATFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSKGFDFKTCNVLLALDQQSPEIAAGVHVNRAEEEIGAGDQGIMFGYATDETEECMPLTVVLAHKLNEKIAELRRSDVFWWARPDSKTQVTCEYLFNQGSAVPKRVHTIVVSMQHSEKISLETLRSEVMEKVVKVVIPAKYIDANTIVHINPCGLFVIGGPMGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDFTKVDRSAAYAARWVAKSLVKAGLCKRCLVQVSYAIGLAEPLSITVFDYGTSHKSQKELLDIIRRNFDLRPGKIVKDLNLRQPIYQRTSTYGHFGRAGFSWEEAKPLEIDN | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 44697
Sequence Length: 408
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
EC: 2.5.1.6
|
Q58605 | MRNIIVKKLDVEPIEERPTEIVERKGLGHPDSICDGIAESVSRALCKMYMEKFGTILHHNTDQVELVGGHAYPKFGGGVMVSPIYILLSGRATMEILDKEKNEVIKLPVGTTAVKAAKEYLKKVLRNVDVDKDVIIDCRIGQGSMDLVDVFERQKNEVPLANDTSFGVGYAPLSTTERLVLETERFLNSDELKNEIPAVGEDIKVMGLREGKKITLTIAMAVVDRYVKNIEEYKEVIEKVRKKVEDLAKKIADGYEVEIHINTADDYERESVYLTVTGTSAEMGDDGSVGRGNRVNGLITPFRPMSMEAASGKNPVNHVGKIYNILANLIANDIAKLEGVKECYVRILSQIGKPINEPKALDIEIITEDSYDIKDIEPKAKEIANKWLDNIMEVQKMIVEGKVTTF | Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 45252
Sequence Length: 406
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
EC: 2.5.1.6
|
P56878 | MKNFVFTSESVSEGHPDKIADQISDAVLDEILKHDPNGRVACETFVTTGLVLVGGEITTNTYVDIEQVVRNKIQEIGYNNPNYGFDGSCCAVISSIIKQSPDIAMGIDNENEEEIGAGDQGMVFGYACNETKSLMPAPIYYAHLLMKRQAYLRKQNILSWLRPDAKSQVTLRYENNKPIVIDSVVLSTQHHPEIQQKDLIEAVIEEIIKPTLPTNLLHKDTKYLINPTGRFVIGGPVADCGLTGRKIIVDSYGGMAKHGGGCFSGKDPTKIDRSAAYMARYIAKNIVGAGLADRCEIQISYAIGVADPVSVYAETFGTSKLSNEQTTKLITEHFDMRPGKIIKNLKLHTQCYQKTATYGHFGREDENFTWEQLDKVDIFK | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42149
Sequence Length: 380
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
Q5LLL2 | MSRQNYIFTSESVSEGHPDKVCDRISDAVLDAFLTEEPEARVACETFATTNRVVIGGEVGLSDQAKLREYMGRIDQIARDCIKDIGYEQDKFHHETVEITNLLHEQSAHIAQGVNAAEGKDEGAGDQGIMFGYATTETPALMPAPIQYSHAILRRLAEVRKNGTEPALGPDAKSQLSVIYRDGMPVGVSSLVLSTQHLDPDLTSADIRAIVEPYIREVLPEGWLSADTVWHVNPTGKFVIGGPDGDAGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLADKCTIQLSYAIGVSKPLSIYADTHGTGDIAPAAIEKAIDTVMDLTPRGIRTHLGLNKPIYERTAAYGHFGREPEADGGFSWERTDLAEALKKAV | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42217
Sequence Length: 393
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
Q980S9 | MRNINVQLNPLSDIEKLQVELVERKGLGHPDYIADAVAEEASRKLSLYYLKKYGVILHHNLDKTLVVGGQATPRFKGGDIIQPIYIIVAGRATTEVKTESGIDQIPVGTIIIESVKEWIRNNFRYLDAERHVIVDYKIGKGSSDLVGIFEASKRVPLSNDTSFGVGFAPLTKLEKLVYETERHLNSKQFKAKLPEVGEDIKVMGLRRGNEVDLTIAMATISELIEDVNHYINVKEQVRNQILDLASKIAPGYNVRVYVNTGDKIDKNILYLTVTGTSAEHGDDGMTGRGNRGVGLITPMRPMSLEATAGKNPVNHVGKLYNVLANLIANKIAQEVKDVKFSQVQVLGQIGRPIDDPLIANVDVITYDGKLTDETKNEISGIVDEMLSSFNKLTELILEGKATLF | Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 44663
Sequence Length: 404
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
EC: 2.5.1.6
|
Q7M7Z2 | MRKEFLFTSESVTEGHPDKMADQISDAILDYIIERDPKARVACETLLSNGFCVIAGELKTTTYAPMQEIAREVIREIGYTDALYGFDYRSAGILNGVGEQSPDINQGVDREDGEIGAGDQGLMFGYACRETETLMPLPIFLSHKITEGLAKARKDGTLPFLRPDGKSQVTVRYVDGKPVGIDTIVVSTQHAPDVSQERLRDAVIEEIVYKVLPKEYLGDDIRFFVNPTGKFVIGGPQGDAGLTGRKIIVDSYGGSCPHGGGAFSGKDPSKVDRSGAYAARYVAKNLVASGVCDKATIQIAYAIGVVEPVSILVDTHGTGKVEDDQLETCVRQLFRLTPKGIIESLDLLRPIYKKTASYGHFGRELPEFSWEKTDKAELIKNYFNLK | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42316
Sequence Length: 386
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
Q89LP2 | MVRFEGISKTYPAYRGKPGVNALQDIDFAIPRGSITGVIGRSGAGKSSLVRLINGLEKPTTGRVIVDNKDISALAGRELRLAQRSIGMIFQHFNLLSSRTAADNIALPLEIAGWARADIKARVAELLALVGIADKHDRYPSELSGGQKQRVGIARALATRPSVLLSDEATSALDPQTTRAILDLLANINRELGVTIVLITHEMSVVRQLAREVVVLDAGHVVESGHVADIFTHPKHPITQSFLAEVVGDSLPVSLASRIVSEPSAGGQAVIRVQVRGAGAGDTVVARLARELGLDVALLAARIDEIGGQHVGSLVLGVPGSEDVQARVLAWLSQYQFPAERLGYVA | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36744
Sequence Length: 346
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
|
Q2YIV5 | MQHAAVCSGTSRHRRTTVTIEKPPATSAPIVEMKDVRRMFGETAAINGVSLSVARGEILGIIGRSGAGKSTLIRCVNGLEKPDTGSIHIEGREITSLDEDALRPVRRRIGMVFQHFNLLSAKTAAQNIALPLKIAGMPKAERIKRVAELLELVGLSDKASHYPAQLSGGQKQRVGIARALAAEPAVLLSDEATSALDPETTQSILALLKDINAKLGLTILLITHEMDVIRRIADRVIVLDHGLIAEEGPVWKVFANPQSPVTQSMLQVLTPELPAIWRNRLEKKGDQAILRVKLSGMAAKGAFFNDVAAATSLAPQLIHGGMDTIQGEPVGTLFIGLPAEDKTKLKAAIGYLNTHADATEVLGYVSGNA | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39445
Sequence Length: 369
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
|
Q0PAB6 | MIKIKNLKKYYGKELVINDVSLEIKKGEIYAIVGHSGAGKSTLLRCINGLENYQEGSLKVFDQEIKDLSQKKSKELRMLRKDIGMIFQNFALMERKNVFENVAMPLRTHYTQCKFHAKLFNKEYMSEKEIAQKVNSLLEIVGLDHKNKSYPRELSGGQKQRVAIARALALNPKILLSDEATSALDPNTTKNILELISKINAEFGITVVLVTHEMDVVKDIAQKALLLEHGQIIGSGAIDELFLRPNAKMKEFLGESDFLPEHGLNIKLYFPKEVAQNSVITHMARTLNIDFNIVWGKIEKLNGKALGNLVININEKDKDKVLDYIEKSGVLWEVAS | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37997
Sequence Length: 336
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
|
Q3J1N0 | MRDEQATGAAITFDRVEKSFAQKGGAPVMALSDCTLTVEPGAITGIIGRSGAGKSTLLRMVNGLERPTGGRVLVGGRDVGAADGAELREIRREVGMIFQHFNLLASRTVFGNVALPLEIAGRPSSEIRTRVADLIARVGLEALADRYPAELSGGQKQRVGIARALATGPKVLLSDEATSALDPETTQTVLRLLADINRDLGLTILLITHEMGVVRDIATHMAVIDGGRIVEAGPTYDIFVRPEHPTTRSFLSGVTGVTLPAFVASRLRPAPPEGPSQEVIRITFAGRHATDPMLARLTGELGIAVNILAGAIEEIGPHPFGNLLVSVETPRGAEARAYLERHQLLTEVLGYVG | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37421
Sequence Length: 353
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
|
Q9Z8Q8 | MSEQHSPIISVQDVSKKLGDHILLSKVSFSVYPGEVFGIVGHSGSGKTTLLRCLDFLDMPTSGSISVAGFDNSLPTQKFSRRNFSKKVAYISQNYGLFSSKTVFENIAYPLRIHHSEMSKSEVEEQVYDTLNFLNLYHRHDAYPGNLSGGQKQKVAIARAIVCQPEVVLCDEITSALDPKSTENIIERLLQLNQERGITLVLVSHEIDVVKKICSHVLVMHQGAVEELGTTEELFLNSENSITNELFHEDINIAALSSCYFAEDREEVLRLNFSKELAIQGIISKVIQTGLVSINILSGNINLFRKSPMGFLIIVLEGEVEQRKKAKELLIELGVVIKEFY | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38075
Sequence Length: 341
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
|
Q1QVQ7 | MIKLEGVSKTYGAGPTAVHALKNIDLDVPQGAIHGVIGLSGAGKSTLIRCVNLLERPTSGRVIVDGQDLTRQDAEALRQSRHQLGMIFQHFNLLASRTVFDNVALPLELMGVSKSDIRERVEPLLDLTGLTDKARQYPAQLSGGQKQRVAIARALASRPKVLLCDEATSALDPQTTASILELLQDINRKLGLTILLITHEMEVVKSICHRVGLISDGELVEEADVGDFFTAPATRLGRDFLNAFLELEPPQALVERLEETAGPHTHPVVRLAFSGATVATPLISRLARDSGVDVSILQAKVESIQGRTLGLMIAELIGSPDTTSRALTQLEAHDINVEVLGHVQRDA | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37445
Sequence Length: 347
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
|
Q97KD5 | MIEIKNVSKYFSGNKVLKDVDLKIKGGEIFGIVGHSGAGKSTLLRCINGLETYDEGNVIVFGKDLKQINGKNLREFRKEVGMIFQNFNLLNRKDVYHNISLPLEVWGVPKNEIASRVKELLELVDLTDKIHSKPSNLSGGQKQRVAIARALALNPKILLCDEATSALDPNTTKSILNLLRTINSKLGITIVIVTHQMEVVKGICERVALIDAGVIKETGDVENLFLNPSSEMKKLIGQSDDDVLPKEGINIRVIFPKNSSEGALITSMARELNVDFSIVWGKLERFRDDVLGSLVINISEENKEVICNYLVSHNAIWEVA | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35490
Sequence Length: 320
Subcellular Location: Cell membrane
EC: 7.4.2.11
|
Q18C09 | MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNTKGLRKLIGEESIILPKGTNIKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLIINISDKSGEQVKQYLTSKGIRWEEMINE | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35915
Sequence Length: 321
Subcellular Location: Cell membrane
EC: 7.4.2.11
|
G0J5N4 | MNLQSPHLTIEMTQEIFYCQEALSLESGESFPEFQLSFTTQGQLNANKDNVIWVLHALTGDANPHEWWSGLIGEDKFFDPSKYFIVCANFLGSCYGSTQPLSNNPNNGKPYYYDFPNITTRDIASALDKLRIHLGLEKINTVIGGSLGGQVGLEWAVSLGEKLENAIIVASNAKASPWIIGFNETQRMAIESDSTWGKTQPEAGKKGLETARAIGMLSYRHPMTFLQNQSETEEKRDDFKISSYLRYQGLKLANRFNAMSYWILSKAMDSHDIGRGRGGTPVALSNIKCKVLSIGVDTDILFTSEESRYISKHVPKGTYREISSIYGHDAFLIEYEQLQYILKSFYLENNG | 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
Sequence Mass (Da): 39422
Sequence Length: 351
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
D3P9D1 | MKENSVGLVKTKYVTFKDDFYFESGRILSPITVAYETYGKLNEKKDNAILICHALTGSAHAAGYNSPDDQKPGWWDDMIGPGKAFDTDKYFIICSNFLGSCYGTTGPASIDPSTGKPYGLKFPVFTVKDMVKLQKKLIDYLGIEKLLCVAGGSMGGMQALEWAVTFPEKTYSIIPIATAGRITPMAIAFNTIGRFAIMKDPNWMNGDYYGKTFPRDGLAIARMAGHITYMSDKSFHKKFGRRYATFGGIYDFFGYFEVENYLRYNGYKFTERFDANSYLYIIKAMDIFDLSYGYGSYEEAIGRIEADSLFITFTSDFLFPSYQTEEIVNIMKNHGKNPEWVNIESDYGHDAFLLEFDTQTSCIKEFLSKIYNKVANQ | 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
Sequence Mass (Da): 42708
Sequence Length: 377
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q1J115 | MTALISQPDLLPPPAPERCPPQQTARLFRETPLLLDCGQVVQDVRVAYHTYGTPSDHAILVLHALTGTSAVHEWWPDFLGEGKPLDPTRDYIVCANVLGGCAGSTGPAELPRVNGEDPPLTLRDMARVGRALLEELGVRRVSVIGASMGGMLAYAWLLECPDLVDRAVIIGAPARHSPWAIGLNTAARNAIRAAPGGEGLKVARQIAMLSYRSPESFALTQSGWGTRRPGTPDITTYLEHQGEKLSTRFCERSYLALTGAMDRFQPTDAELRSIRVPVLVVGISSDVLYPPAEVRTYAGLLPRGQYLELQSPHGHDAFLIDPQGLPEAAAAFLHGA | 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
Sequence Mass (Da): 36245
Sequence Length: 336
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q5FUF4 | MDISASPSIADGPVYTHQTVRLDSGLDLECGVHLAPLEVAYCTYGTLSPARDNAILVCHALTGDQYLAERNPLTGKPGWWSRMVGPGLPIDTDRYFVVCSNVLGGCMGTTGPRSICAETGKAWDSEFPPITMHDIVAAQAKLIDHLGIDRLFAVIGGSMGGMQALTWAADFPDRVFAAMPIATSPFHSAQNIAFNEVSRQAIFADPDWHDGHYRDFGAIPARGLGVARMMAHITYLSEEALSRKFGRRVRHDAATAVPASSSPSLFGEMFEVESYLRHQGSSFVRRFDANSYLTITRAMDYFDLAAEHDGDLANPFRKSQTRFCVVSFSSDWLFPTSQSRLLVRALNRAGANVSFVEIESDRGHDAFLLEEPDFDRTIRGFIAGAAEHAALKAGER | 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
Sequence Mass (Da): 43314
Sequence Length: 396
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
P45131 | MSVQNVVLFDTQPLTLMLGGKLSHINVAYQTYGTLNAEKNNAVLICHALTGDAEPYFDDGRDGWWQNFMGAGLALDTDRYFFISSNVLGGCKGTTGPSSINPQTGKPYGSQFPNIVVQDIVKVQKALLDHLGISHLKAIIGGSFGGMQANQWAIDYPDFMDNIVNLCSSIYFSAEAIGFNHVMRQAVINDPNFNGGDYYEGTPPDQGLSIARMLGMLTYRTDLQLAKAFGRATKSDGSFWGDYFQVESYLSYQGKKFLERFDANSYLHLLRALDMYDPSLGYDNVKEALSRIKARYTLVSVTTDQLFKPIDLYKSKQLLEQSGVDLHFYEFPSDYGHDAFLVDYDQFEKRIRDGLAGN | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine . Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine .
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 39990
Sequence Length: 358
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
B9LTF0 | MSTVPTDHGVAALGEFVFECGQSVPDLEVAYETHGEFDGDNVVLVCHALTGSQNVARSPAPERNEGTRGAGQAGQARAWWDDIVGPGKAIDTTKYYVVCANVPGSCYGTTGPASERPADLDLPEEPDHDRWGTAFPPVQVEDWARSQRRLLDHLGVGRLRAVVGGSVGGMNVLEWAKRYPDDVDRVVAIATAGRLDAQCLALDAVARRAIRADPNWNGGNYYGEGRPSPDEGLALARQIGHIMYLSKASMERKFGRRSAGRDSLTREEGDLGLPPEPTAAFFPYREVESYLDYQAEGFSERFDANSYLYLTRAMDEYDLSAGHGTDADALAAFEGEALLMSFTADWHFTVEQSSSLAAAFRDRDVPVAHHVIDSDHGHDAFLVEPEHVGPPLRDFLVEGVGGRAVSDDGGGGGNDSARPERDHAPVHASLFKG | 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
Sequence Mass (Da): 46766
Sequence Length: 433
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
P57715 | MPTTELDGFTFACGDTVDSLTVAYRTYGDYTGSNAVLVCHALTGSQHVRGRADGDDRGWWPDIVGPGRPIDTTEYFVVCANVPGSCHGTDGPPADGPGGDPWGTAFPPVTVPDWTRCQRRLLDTLGVDRLHAVVGGSVGGMNALDWARRYPDDVHRIAAVATAPRLDAQCLGLNAIARRAIRGDPNWNDGDYYGGAHPDRGLALARQLGHVMYLSKASMADKFGRRTATTDTALPADPAAEFFATRDVESYLDYQADTFVARFDANSYLYLLRAMDAYDLAAGRPSVADALAAFDGDALVLSFTGDWHFTAAQSATVADAFRAGGAAGVAHHVVDSDYGHDAFLVDSAAVGPPLADFLAAGTDGAAVTDATGGV | 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
Sequence Mass (Da): 39365
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q6ADB9 | MDWQTTSADTAPSSFITEEQDRSLFGKPPASGAWKESDPVGGRRFAGIGAFGFESGESLPFVRIAYETWGELSPARDNAVLVLHALTGDSHAVGAAGPGHRTSGWWQGIIGPGKAIDTDRWFVAVPNMLGGCQGTTGPTSIAPDGAEWGARFPFTTIRDQVKAQAAFADALGIGRWAAVVGGSMGGMQALEWAVGFPERVERLAVIAAPPHSTADQIAFNSVQLGAIRTDPLFHGGSYYDEKDGEGPHQGLALARRMALITYRSLSELNDRFERTWQSGISPLGDGGRFAVESYLDFHGNKFTRRFDANSYLTLVQAMNSHDVGHDGSGLAAALSRVTATTLVVGIDSDRLFPVDGQELIASHLPAALDGRVPLVVRSHFGHDGFLIEDDLIGGQLRRLFAA | 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
Sequence Mass (Da): 42932
Sequence Length: 402
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q8CBH5 | MAADDKVAILTDDEEEQKRKYVLADPFNGICREPEPPSNETPSSTETSAIPEEEIDWIEKHCVKVNNDLLISKVFYFFFYSAYGSLYPLLPVYYKQLGMSPSQSGLLVGIRYFIEFCSAPFWGVVADRFRKGKIVLLFSLLCWVLFNLGIGFVKPATLRCLPKIPPTAHPTNVSHPVTVLPMNSSTVAFFSTPPKLLQKRDVQLSETEPNISDIDLVSTALTLTSEPTRRPQTEAITHPVTGLILNTSTVTLPPTGNVTRETTIAVVTTTKSLPSDQVTLVYDQQEVEAIFLIILVVVIIGEFFSASSVTIVDTVTLQYLGKHRDRYGLQRMWGSLGWGLAMLSVGIGIDYTHIDVLIDGKGCKPPEYRNYQIVFIVFGVLMTMALIVATQFRFRYNHFNNSDGKGKEVEIPQVERDNSTESSEETPTAATHSQAFNFWDLIKLLCSVQYGSVLFVAWFMGFGYGFVFTFLYWHLEDLNGTTTLFGVCSVLSHVSELTAYFFSHKLIELIGHIRVLYIGLACNTARYIYISYLENAWTVLPMEVLQGVTHAAIWAACISYLSAAVPPELRTSAQGILQGLHLGLGRGCGAMIGGVLVNYFGAAATFRGIGMACLVILLLFALIQWLAVPDEEEDKTMLAERIPVPSSPVPIATIDLVQQQTEDVMPRVEARLPPKKTKHQEEQEDVNKPAWGVSSSPWVTFVYALYQVKELIQLTRESRASEIQPLQVTLCWASVASAPLLPPCSSKHMGNRKTGMLAKDISGLRSLCHSVYQVA | Function: MHC class I receptor. Binds only to H-2 class I histocompatibility antigen, K-D alpha chain (H-2K(D)).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86076
Sequence Length: 775
Subcellular Location: Membrane
|
Q0VA82 | MPLEESGENTPLLRGEIISDGDTDRSRWRSIRVMYFTMFLSSVGFTIVITSIWPYLKKIDESADASFLGWVVAAYSLGQMVASPFFGLWSNHRPRREPLVCSIFINVSANIYYSYVYLPPSHNQIHMLLARTFVGIGAGNVAVVRSYVAGATSLKERTSAMANMSACQALGFILGPALQAVLSFIGETGVSVDVIKLQVNMYTAPALLAACFGVINILLVILVLREHSVDDHGNRIRPINYTPEERVDVPPEVEGDIDHIAVFTSNVLFFIILFIFAVFETISTPLSMDMFAWTRKEAVLYNGIILAAIGFESILVFLVVKVVSARVGDRPLLLGGLILIFVGFFMLLPWGNQYPKIQWTDINNNTIPPIQLAPTPASNSSLEPIGCPSEQTWCLFTPVIHLAQYITSDILIGVGYPTCNVMSYTLYSKILGPKPQGVYMGWLTASGSGARTLGPVFVSHFYTILGPRWAFSAICGIVLAAIVMLSAMYKRLVAFSIRHGRIAE | Function: May be a carrier that transport small solutes by using chemiosmotic ion gradients.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55486
Sequence Length: 504
Subcellular Location: Lysosome membrane
|
Q8NHS3 | MAGLRNESEQEPLLGDTPGSREWDILETEEHYKSRWRSIRILYLTMFLSSVGFSVVMMSIWPYLQKIDPTADTSFLGWVIASYSLGQMVASPIFGLWSNYRPRKEPLIVSILISVAANCLYAYLHIPASHNKYYMLVARGLLGIGAGNVAVVRSYTAGATSLQERTSSMANISMCQALGFILGPVFQTCFTFLGEKGVTWDVIKLQINMYTTPVLLSAFLGILNIILILAILREHRVDDSGRQCKSINFEEASTDEAQVPQGNIDQVAVVAINVLFFVTLFIFALFETIITPLTMDMYAWTQEQAVLYNGIILAALGVEAVVIFLGVKLLSKKIGERAILLGGLIVVWVGFFILLPWGNQFPKIQWEDLHNNSIPNTTFGEIIIGLWKSPMEDDNERPTGCSIEQAWCLYTPVIHLAQFLTSAVLIGLGYPVCNLMSYTLYSKILGPKPQGVYMGWLTASGSGARILGPMFISQVYAHWGPRWAFSLVCGIIVLTITLLGVVYKRLIALSVRYGRIQE | Function: May be a carrier that transport small solutes by using chemiosmotic ion gradients.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57628
Sequence Length: 518
Subcellular Location: Lysosome membrane
|
Q6GPQ3 | MASIDDDDDERTPLLQDSHIGELVETQKQLKSRWWSIRVMYLTMFLSSVGFSIVMTSIWPYLQKVDQSADASFLGWVIASFSLGQMVASPLFGLWSNHRPRREPLVVSITILVAASCLYAYVHVPASHNKYYMLLARTFVGFGSGNVAVVRSYVAGATSLSERTGAMANISAFQAMGFILGPAFQAALSVIGETGITINGISLQVNMYTAPALMGALLGIGNIILIFAIFREHRVDDLEKNVSSINSESEVTDVEKANEGPIDQIAVISSNILFFVVLFVFAIFETISTPLTMDMYAWTRTQAVFYNGIILAAVGVESVIVFLTVKILCKKTGERVLLLGGLAVIWIGFFILLPWGNQMPKIQWTDLQNATIHNTTQWTSSIPSSGNHSVEPTGCPVIQTWCLYTPVIHLAQYLTSDILIGVGYPICNVMSYTLYSKIIGPKPQGLYMGWLTAAGSAARTLGPVFVSQIYTHLGTRWTFGIICAFVALSLLHLTAVYKRLIPFSTRYERL | Function: May be a carrier that transport small solutes by using chemiosmotic ion gradients.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56163
Sequence Length: 510
Subcellular Location: Lysosome membrane
|
A0QYL8 | MSAPQAAIDTDHADRHGPRRAWAAVGVLALVGTLNYVDRFLPSVLAEPIKHDLELSDTAIGVINGFGFLIVYAVMGIAVARVADRGAFGAVVAGCLTLWGTMTMLGGAVQSGFQLALTRVGVAIGEAGSTPAAHAYVARNFVPQRRSAPLAVITIAIPLASTASLLGGGLLAQSLGWRTAFVIMGAVSVVLAPLVLLVVGVRQSLPAAPAVVDKTAGGWWNLLRKPSFLIVVAGTAFISAAGYSLTTFSPAFLMRTRGMSLGEVGVEYGLATGAIGVLGLLIVGRLADRLAERDPRWLLWIVVTLTLVLLPASVLAFVVEDRMLCVLFLALSYAIGTSYLAPSIAAIQRLVLPEQRATASAMFLFFNAVFGSVGPFVVGMLSDSLTDDLGAQALGRALLLLVAAMQLVGAICYWLASARYRRDIIEEAR | Function: Probably plays a role in bacterial growth and resistance to antibiotics.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44969
Sequence Length: 429
Subcellular Location: Cell inner membrane
|
E5AE35 | MSTLCAFPVPYSTIEVLNIVLPYRTYSARLLYLHAPLGNHLPFCHRSYNVLHLRQDCDSHMYSAGNDVRLSQEAVTMSDQRSHDTTADQSARDASSLDTRKIHGFPWFLLVISVLSSIFLYALDNTIVADIIPAIANDFSSINDLGWLSVGFVIGGVAVIMPLGKLYGILNTKWLYITSVVLFMAASAVCGAAPDMNAEIVGRVFAGAGGIGMYIGTMILLSINTSDQERPAYLSLVGLVWGIGTVLGPVIGGSFEKVDWRWAFYLNLVIGALLFPVWFFLLPSFHPAKHLSLNKRLSQFDFVGAILSIGAFVTTIMPINFGGTTYEWNSGTIIALFVVSGVLWIAFAVQQSLTLFTTPADRMFPVQFLKNKEAMLLFICAAAINSAVFVPIYFIPIYFQFSRGDGALDSAIRLLPLIFLLCATILVNGKLMSRFGYYMPWYLVGGVFCLIANVFLCELHPVAAVLVRYTDYKTALLDATTSQSYIYGFEALLGLGAGGSVQAGYAVIQTVVPATDLGYAVSFIMIAQIGGIALGLACASAVFINGATNSLRVLLPLLSDSELQSAISGTGGRFLETLDDNTRVQVIDAVVNNLAKAFIVAYAGAAVSLVASLGFSRKRVFLPTAAAA | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of phomenoic acid, a long chain aliphatic carboxylic acid that does not appear to be essential for pathogenicity but may play a role in allowing to outcompete other fungi in the environmental niche via its antifungal properties . Is probably involved in the efflux of phomenoic acid (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67838
Sequence Length: 628
Subcellular Location: Cell membrane
|
Q947B7 | MAALLVFFSVSLILLAVLFHKRKSSLSSRKRPPPSPLRLPVIGHFHLIGALSHRSFTSLSKRYGEVMLLHFGSAPVLVASSAAAAREIMKNQDVIFASRPRLSIFDRLMYSGKGVAFAPYGEHWRNARSMCMLQLLSAKRVQSFGGIREEETSAMIEKIRRSKPTTVVNLSEMFMALTNGVIHRAVLGRKGDGGDDFNRILIKVIKLLGSFNVGDYVPWLSWINRINGVDAEVEKVGTKLDGSMEGILRKYRRKKVGDDETNFVDTLLQFQRESKDTDPVEDDVIKALIFDMVSAGTDTTFAALEWTMAELIKNPRTLKTLQNEVREVSRNKGGITEDDVDKMPYLKAVSKEILRLHPPFAILLPRELTQDANMLGYDIPRGTVVLVNNWAISRDPSLWENPEEFRPERFLETSIDYKGLHFEMLPFGSGRRGCPGSTFAMALYELALSKLVNEFDFRLGNGDRAEDLDMTEAPGFVVHKKSPLLVLATPRQS | Function: Monoterpene synthase that catalyzes the formation of (+)-menthofuran from (+)-pulegone.
Catalytic Activity: (R)-pulegone + O2 + reduced [NADPH--hemoprotein reductase] = (R)-menthofuran + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 55360
Sequence Length: 493
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.14.143
|
Q9SGU9 | MAHFLETQEPLVFSGKKRNDRDDEDGDALVAKKSALAVCDADPAAAIANIRHEFGEHGGVNMSIEASATFTVMEPDTMRRMFTGELGPDNDFYVYSRHFNPTVLNLSRQMAALEGTQAAYCTSSGMSAISSVMLQLCSSGGHVVAASTLYGGTHALLSHFLPRTCNITTSFVDITDHGAVANAIVEGRTQVLYFESVANPTLTVADIPELSRMAHEKGVTVVVDNTFAPMVLSPAKLGADVVVHSISKFISGGADIIAGAVCGSENLVKEMMDLRGGSLMLLGPTMNAKVAFELSERIPHLGLRMREHSHRAQVYAERMRDLGMKVIYPGLETHPQHKLFKGMVNRDYGYGGLLSIDMETEEKANKLMAYLQNATQFGFMAVSLGYYETLMSCSGSSTSSELDPSQKEAAGISPGLVRMSVGYVGTLEQKWTQFEKAFLRM | Function: Catalyzes the degradation of L-methionine to alpha-ketobutyrate, methanethiol and ammonia. Exhibits a high activity toward L-methionine, L-ethionine, L-homocysteine and seleno-L-methionine, but not L-cysteine. Involved in an alternative cysteine biosynthesis pathway to the reverse trans-sulfuration pathway (methionine->homocysteine->cystathionine->cysteine) in which methanethiol is an intermediate. Mediates also an alternative isoleucine biosynthesis pathway in which 2-ketobutyrate is an intermediate.
Catalytic Activity: H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+)
Sequence Mass (Da): 47821
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 4.4.1.11
|
P32266 | MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL | Function: Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.
PTM: Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of MGM1 (l-MGM1). Further processing by the rhomboid protease PCP1 produces a short peripheral membrane form of MGM1 (s-MGM1). Both isoforms are required for full activity.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 99178
Sequence Length: 881
Subcellular Location: Mitochondrion inner membrane
|
Q9BQP7 | MKMKLFQTICRQLRSSKFSVESAALVAFSTSSYSCGRKKKVNPYEEVDQEKYSNLVQSVLSSRGVAQTPGSVEEDALLCGPVSKHKLPNQGEDRRVPQNWFPIFNPERSDKPNASDPSVPLKIPLQRNVIPSVTRVLQQTMTKQQVFLLERWKQRMILELGEDGFKEYTSNVFLQGKRFHEALESILSPQETLKERDENLLKSGYIESVQHILKDVSGVRALESAVQHETLNYIGLLDCVAEYQGKLCVIDWKTSEKPKPFIQSTFDNPLQVVAYMGAMNHDTNYSFQVQCGLIVVAYKDGSPAHPHFMDAELCSQYWTKWLLRLEEYTEKKKNQNIQKPEYSE | Function: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair. Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells.
Sequence Mass (Da): 39421
Sequence Length: 344
Subcellular Location: Mitochondrion
EC: 3.1.-.-
|
Q9CXC3 | MKLPLTFCRLLSRLNRFSVKASPPVSFSTFSYLCSQKKKNSYEAVDQAKYSRLVRSVLSRGPAQTPESLFKEDDVLYGPVSKHKAAEPEPQARVPQHCFPIFNEERTGKPHTDASSSPLKIPLQRNSIPSVTRILQQTMPPEQSFFLERWKERMVLELGEDGFAEYTSNVFLQGKQFHKALESILSPQENLTGGEEHPQCGYIESIQHILTEISGVQALESAVQHEALKYVGLLDCVAEYRGKLCVIDWKTSEKPKPLIRNTYDNPLQVVAYMGAVNHDAHYSFQVQCGLIVVAYKDGSPAHPHFMDEELCSKYWAKWLLRLEEYTEKQKNLSAPEPA | Function: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair (By similarity). Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells.
Sequence Mass (Da): 38391
Sequence Length: 338
Subcellular Location: Mitochondrion
EC: 3.1.-.-
|
Q5A0Y8 | MSNLYYTVFDTDVCTVLLVLTLNGFVCYASLGKPAIELKGIMAKDFSSLPYQLKPLSTMTGDKIEIDKSVEKFKLLVETPSVSQDIKTELLFGTPLQRKVWKELVKIPAGQTRTYKELADLLGTHSRVIGNCCGANRIAVLIPCHRVVGANNKLTGYRWGKSYKEYLLKQEGIGI | 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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 19492
Sequence Length: 175
Subcellular Location: Nucleus
EC: 2.1.1.63
|
Q6FNR0 | MEDLLYSFVVTDITSALVFVRRQTDALVYASLGLNKKQLLKGARTAFNQLSKKSAIHYNFKQIEVESEQEHVEKFQDTVNKFTKLLEGHIVKDLHYEYMFGTSLQHRIWDELVKIPHGKVTTYKEIADKLKIKNGSRAIGSGIGSNNIAIVIPCHRVVCSNGTLSGYKWSTSLKRKLLEREHVYASNKKDALNKDTKISLMKYKYSA | 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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 23642
Sequence Length: 207
Subcellular Location: Nucleus
EC: 2.1.1.63
|
P26186 | MAETCKMKYTVFHSPLGKIELCGCERGLHGIRFLSGKTPSSDPKEAPASPELLGGPEDLPESLVQCTTWLEAYFQEPAATEGLPLPALHHPVFQQDSFTRQVLWKLLKVVKFGEMVSYQQLAALAGNPKAARAVGGAMRNNPVPILIPCHRVICSNGSIGNYSGGGQAVKEWLLAHEGIPTRQPACKDLGLTGTRLKPSGGSTSSKLSG | Cofactor: Binds 1 zinc ion.
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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 22333
Sequence Length: 209
Subcellular Location: Nucleus
EC: 2.1.1.63
|
Q6BVY4 | MKNIYLLYSIIDVSYTKALIVTNTHGSLYYASLGDKPEVLIVTMKKDFARFKNYVLQPIVGKANSEVSETLEKFRLMAEDPRLINTMHKQIPYEFIFGTELQRKVWNQLMNTNASETVCYSQMASNLGMPKSSRVVGAACGANKIALFVPCHRALTKSGQISGYRWGVPLKQRLLKLEQKPLQKESSLKEK | 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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 21668
Sequence Length: 191
Subcellular Location: Nucleus
EC: 2.1.1.63
|
P16455 | MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSGSPPAGRN | Cofactor: Binds 1 zinc ion.
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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 21646
Sequence Length: 207
Subcellular Location: Nucleus
EC: 2.1.1.63
|
Q6CPW2 | MSHLLVYDFMEHDLANVLIVVKPSTKSLVFVSLSGTKPKLLGDAKKFVSKVNSLSKNKGSIYTLKNKSILKSDDVAWLEQLSFDFLQILAGGIDSQTNIKCEYLLGTEFQKKVWETTKTIKAGATISYQQLAVLLGNPKAVRAIGSALAKNNIAVVIPCHRIIGSKGKLTGFRWGIELKESLLRQEQAI | 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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 20820
Sequence Length: 189
Subcellular Location: Nucleus
EC: 2.1.1.63
|
A5E7M8 | MLVKTLYYRLVEGTFAKAMLVLDEKGTLYYASLGEDSNALRETLVTDFASKQRQFQLKPMVTLSNHERADYTALCFLKLMEEEEDWKNEGEESLQQKGAKRIPIEFIFGTELQRKVWQQLLEIPVGEVRYYGNIVEALGLPKSASRAVGNACGANKIALVVPCHRVIAQTGKLTGYRWGLATKKQILKMELGDAYTTLVSE | 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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 22686
Sequence Length: 201
Subcellular Location: Nucleus
EC: 2.1.1.63
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.