ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q00718 | MPPRVVRLPSLTGLRWFAALAVFACHIAQQQFFADQQVGTALLHITTLGSIAVSVFFLLSGFVLAWSARDKDSVTTFWRRRFAKIYPLHLVTFLIAGVIIFSLAEPTLPGGSVWDGLVPDLLLVQSWLPEPTIIAGFNTPSWSLSCEFAFYLTFPLWYRLVRKIPVRRLWWCAAGIAAAVICVPFVTSQFPASAETAPGMPLNELWFACWLPPVRMLEFVLGIVMALILRTGVWRGPGVVSSALLLAAAYGVTQVVPPMFTIAACSIVPAALLITALANADVQGLRTGLRSAVLVRLGEWSFAFYLVHFMVIRYGHRLMG... | 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.-
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Q7AFA1 | MSRVSQARNLGKYFLLIDNMLVVLGFFVVFPLISIRFVDQMGWAAVMVGIALGLRQFIQQGLGIFGGAIADRFGAKPMIVTGMLMRAAGFATMGIAHEPWLLWFSCLLSGLGGTLFDPPRSALVVKLIRPQQRGRFFSLLMMQDSAGAVIGALLGSWLLQYDFRLVCATGAVLFVLCAAFNAWLLPAWKLSTVRTPVREGMTRVMRDKRFVTYVLTLAGYYMLAVQVMLMLPIMVNDVAGAPSAVKWMYAIEACLSLTLLYPIARWSEKHFRLEHRLMAGLLIMSLSMMPVGMVSGLQQLFTLICLFYIGSIIAEPARET... | 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
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A6TA11 | MQKYFVEARQLLALAIPVILAQVAQTAMGFVDTVMAGGYSATDMAAVAIGTSIWLPAILFGHGLLLALTPVVAQLNGSGRRERIAPQVRQGFWLAGFVSVLIMVVLWNAGYIISSMHNIDPLLAEKAVGYLRALLWGAPGYLFFQVARNQCEGLAKTKPGMVMGFIGLLVNIPVNYIFIYGHFGMPELGGVGCGVATASVYWVMFASMLWWVRRARTMRDIRCAERFSGPDFAVLLRLVQLGLPIALALFFEVTLFAVVALLVSPLGIIDVAGHQIALNFSSLMFVLPLSLAAAVTIRVGFRLGQGSTIDAQVSARTGVG... | 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
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B4EWN4 | MQKYIKEARSLLALGIPVIIAQFSQTAMGVVDTVMAGAVNATEMSAVAVGTSIWLPTILLGQGILMALTPIVAQLNGSGQRKHIANRTQQGFWLATFLSIMVIAILYNSRFIIEAQHDIEPELAEKAIGFIHAIMWGAPGCLYYQVLRSQCEGLSKTKPGMIIGFIGLLINIPVNYAFIYGKFGAPQLGGIGCGVATASVFWAMFLMMRYYVRRAPTQRDVMPKKRLVLPEFHTIKRITLLGLPVGLALFFEVTLFAVVALLVSPLGVTAVASHQIALNFSSLMFMFPLSLGIAATIRVGYNLGQRSTEQARTSAITALA... | 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
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Q8N635 | MANSFAARIFTTLSDLQTNMANLKVIGIVIGKTDVKGFPDRKNIGSERYTFSFTIRDSPAHFVNAASWGNEDYIKSLSDSFRVGDCVIIENPLIQRKEIEREEKFSPATPSNCKLLLSENHSTVKVCSSYEVDTKLLSLIHLPVKESHDYYSLGDIVANGHSLNGRIINVLAAVKSVGEPKYFTTSDRRKGQRCEVRLYDETESSFAMTCWDNESILLAQSWMPRETVIFASDVRINFDKFRNCMTATVISKTIITTNPDIPEANILLNFIRENKETNVLDDEIDSYFKESINLSTIVDVYTVEQLKGKALKNEGKADPS... | 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 RAD5... |
Q0WUA3 | MVNFVSLCDIKYGFVPKNSTDLFVKRKIHKLPSRGDVITRLPVFGSNARENLNAKPRRNLRVRPIFCKSYGDAAKVYQEEEIPRAKLIWRAIKLPMYSVALVPLTVGASAAYLETGLFLARRYVTLLLSSILIITWLNLSNDVYDFDTGADKNKMESVVNLVGSRTGTLAAAITSLALGVSGLVWTSLNASNIRAILLLASAILCGYVYQCPPFRLSYQGLGEPLCFAAFGPFATTAFYLLLGSSSEMRHLPLSGRVLSSSVLVGFTTSLILFCSHFHQVDGDLAVGKYSPLVRLGTEKGAFVVRWTIRLLYSMLLVLGL... | 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... |
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
P... |
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... |
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
P... |
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
P... |
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... |
Q8GYN9 | MADSNELGSASRRLSVVTNHLIPIGFSPARADSVELCSASSMDDRFHKVHGEVPTHEVVWKKTDFFGEGDNKEFVDIIYEKALDEGIAKITINRPERRNAFRPQTVKELMRAFNDARDDSSVGVIILTGKGTKAFCSGGDQALRTQDGYADPNDVGRLNVLDLQVQIRRLPKPVIAMVAGYAVGGGHILHMVCDLTIAADNAIFGQTGPKVGSFDAGYGSSIMSRLVGPKKAREMWFMTRFYTASEAEKMGLINTVVPLEDLEKETVKWCREILRNSPTAIRVLKAALNAVDDGHAGLQGLGGDATLLFYGTEEATEGRT... | 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-... |
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).
C... |
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... |
A6W5P6 | MNPSTALATVLVDTLVRLGLRHLVLSPGSRSAPLAYAAARAADEGRLTLHVRVDERSAGFLALGLARAGELVAVVTTSGTAVANLHPAVLEAHHAGVPLVVLSADRPHELRGSGASQTADAQARMFLPSVRYSADVPAPVDPDRQAPAWRSLLSRAVAFARGLRGDGPGPVHLNVGFADPLTPSPGDVPPGPGLTQVHGPGAPAPVALERGPRTLVLAGDAPDPATGAAARELAESAGWPLLAEPSSGARGGERAVGPYRLLLDAVDAEGPLGAVERVVLFGHPTLSRPVTRLLARDDVELVVVSAAGTWSDAGFRAARV... | 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-carb... |
Q9CHK0 | MTNEYLAPFVDELFNLGVREAVFSPGSRSTALAMLFEEYKKYDTYVNIDERSAAFFALGIAKAKKRPVVLVCTSGSAAAHHFPAVLEAKMSRVPLIILTADRPAELQFVGAPQTVDQTRFFGNFVNHFENLEAPHIQKQSQTENFWTYPRKVAQRAVLSAISPLSGPVQINVPLRDLLVPELKSENYEKGRSKHAFKFYEGQAQVILPFDEALLSGKTLILAGANFDKDYSEALLKLAEQLKAPILADPLSNLRNHNHPLVIDSYDAFLANNDLKTQLKADAILLFGQMPVSKRLQQFVAFNNEAEFIQVDPALDYRNPS... | 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-carb... |
B1MZ27 | MVNDTLTINTKHLLYALYASGVKHFVVSPGSRTTPIALMLAEYERQNSEIVVYIDVDERSAGFFALGIAKTRQEPVVVLGTSGTAITEYMPAVAEAKVSHIPLIVLSTDRPAELQNNGAPQTLPQHRLFGELTPYFVSFTLQDEHEDNTAYIDYMTQKLVHSAMDTGQPLQINLPLRKPLMPKLHDSHDVSITPLTFEKTHIHILPIVIKQTHVVILAGPNEAADYKDELLQFSRDHQVPVIADILSRARTTDTIFGVDSLIKAHYLTDEYRPDLVIRFGGTPVSARVLQWLQRENIPVWHVDGHAGNDHSRHVTRAFQM... | 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-carb... |
Q8Y6K9 | MTNHEQVLTDYLAAFIEELVQAGVKEAIISPGSRSTPLALMMAEHPILKIYVDVDERSAGFFALGLAKASKRPVVLLCTSGTAAANYFPAVAEANLSQIPLIVLTADRPHELRNVGAPQAMDQLHLYGSHVKDFTDMALPENSEEMLRYAKWHGSRAVDIAMKTPRGPVHLNFPLREPLVPILEPSPFTATGKKHHHVHIYYTHEVLDDSSIQKMVTECTGKKGVFVVGPIDKKELEQPMVDLAKKLGWPILADPLSGLRSYGALDEVVIDQYDAFLKEAEIMDKLTPEVVIRFGSMPVSKPLKNWLEQLSDIRFYVVDP... | 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-carb... |
B1HY21 | MSERKNLTDYVYKMVASLVQVGVENVVVSPGSRSTPLAYAVASTKQIKMYRQVDERSAAFFALGLAKATAKPVVLLCTSGTAAANYFPAIVEASYARVPLIIITADRPHELREVGAPQTINQPHLYGSHVKWSVDFPLADGAAPTLPFIERHIARAVAIATSAPFGPVHLNVPFREPLLIDLQDELPTMTFKHSSMGQLIPTTSAMQELSSILNSTRKGFMIVGELALGTDLAFLWEFVRQLKWPVIVESLSNMRAAVPEDCLPYLVTTYDAIMKSEDFKALVQPDTVLRIGAQPVSKFIMQFITKTQPSAYVIIDEDPM... | 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-carb... |
A0QLC9 | MNPSTTQARVVVDELIRGGVRDVVLCPGSRNAPLAFALADADRAGRIRLHVRIDERTAGYLAIGLAIAAGAPVCVAMTSGTAVANLGPAVVEANYARVPLIVLSANRPYELLGTGANQTMEQLGYFGTQVRAAISLGLAEDAPERLDALNATWRSATCRVLAAATGSRTANAGPVQFDIPLREPLVPDPEPHGAPTPAGRPGGRPWTYTPPVSFDQPLDIDLSPDTVVIAGHGAGTHPNLAQLPTVAEPTAPAPDNPLHPLALRLLRPKQVIMLGRPTLHRPVSALLADPQVPVYALTTGPRWPDVSGNSQATGTRAVTT... | 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-carb... |
P9WFW8 | MSAHVATLHPEPPFALCGPRGTLIARGVRTRYCDVRAAQAALRSGTAPILLGALPFDVSRPAALMVPDGVLRARKLPDWPTGPLPKVRVAAALPPPADYLTRIGRARDLLAAFDGPLHKVVLARAVQLTADAPLDARVLLRRLVVADPTAYGYLVDLTSAGNDDTGAALVGASPELLVARSGNRVMCKPFAGSAPRAADPKLDAANAAALASSAKNRHEHQLVVDTMRVALEPLCEDLTIPAQPQLNRTAAVWHLCTAITGRLRNISTTAIDLALALHPTPAVGGVPTKAATELIAELEGDRGFYAGAVGWCDGRGDGHW... | 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
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Q9CPI5 | MDNLQSIKAQFIAQINAYQPEKDRDIVVFQCNTETTFSLLAWLKAQQYYPQFYLHGRDGATKWASIGQVRQFSDVSAAAHFIQEQQLALLGGLQFYGDALFVLPRLLLQQRQDGMTITLFIDGKQFEQDKLVALACLSTFEKQTALQTVKQEISLISQKADQAEWCRWVEQGLQKIKQGELSKIVLANERCFKTAAPLAATDLLAESEKYNLGCYHFMLAESEQRAFIGSSPELLYRRHGLQLKTEALAGTAFMGEDEQQNQQQSDWLLHDKKNEYENQLVVDGICQNLQPFVQQITIEKVELKKLRKVQHLRRRISAQL... | 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
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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 ... |
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... |
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-naphtho... |
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 t... |
A0QRI8 | MNTRADVVVVGAGPAGSAAAAWAARAGRDVVVVDAAQFPRDKACGDGLTPRAVAELQRLGMASWLDTRIRHHGLRMSGFGADVEIPWPGPSFPATSSAVPRTELDDRIRSVAADDGAKMMLGTKVVDVTHDSSGRVDAVVLDDGNTVGCAQLIVADGARSTLGRVLGRTWHRETVYGVAIRGYIASPRASEPWITSHLELRSPEGKVLPGYGWMFPLGNGEVNIGVGALATAKRPADAALRPLMSYYADLRREEWGLVGEPRAGLSALLPMGGAVSGVAGPNWMLIGDAAACVNPLNGEGIDYGLETGRLAAELMTSGGV... | 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)... |
P9WNY8 | MSVDDSADVVVVGAGPAGSAAAAWAARAGRDVLVIDTATFPRDKPCGDGLTPRAVAELHQLGLGKWLADHIRHRGLRMSGFGGEVEVDWPGPSFPSYGSAVARLELDDRIRKVAEDTGARMLLGAKAVAVHHDSSRRVVSLTLADGTEVGCRQLIVADGARSPLGRKLGRRWHRETVYGVAVRGYLSTAYSDDPWLTSHLELRSPDGAVLPGYGWIFPLGNGEVNIGVGALSTSRRPADLALRPLISYYTDLRRDEWGFTGQPRAVSSALLPMGGAVSGVAGSNWMLIGDAAACVNPLNGEGIDYGLETGRLAAELLDSR... | 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 (... |
Q9BUN1 | MVPAAGALLWVLLLNLGPRAAGAQGLTQTPTEMQRVSLRFGGPMTRSYRSTARTGLPRKTRIILEDENDAMADADRLAGPAAAELLAATVSTGFSRSSAINEEDGSSEEGVVINAGKDSTSRELPSATPNTAGSSSTRFIANSQEPEIRLTSSLPRSPGRSTEDLPGSQATLSQWSTPGSTPSRWPSPSPTAMPSPEDLRLVLMPWGPWHCHCKSGTMSRSRSGKLHGLSGRLRVGALSQLRTEHKPCTYQQCPCNRLREECPLDTSLCTDTNCASQSTTSTRTTTTPFPTIHLRSSPSLPPASPCPALAFWKRVRIGLE... | 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
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Q569E4 | MVPAACMLLWALLLSLEYRAAGAEDQTTTPTATTIGMQRVSFRFGGPARSLHSTNPTARTTVPGKLRVTLEDENDALATADRLALPAAAELLSTVTGYSRSSVPSPSDWEEDGSLEEGVVDTRKTTNGPVSLFSTTNTVGSSGTTGRFLANSQEREIKLTTDVRSLSSKTTVVDLSSESTLQQWSTPGSTPSPWLKPSFTAMPSPEDLRVVLMPWGPWHCHCKSGTMSRSRAGKLHGLSGRLRVGALNELRTEHRPCTYQLCACNRHLEECPLDSSLCSDHSCSSRAPFQSSTTSLVPVHLRRRPILPPTSPSPSPALAF... | 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
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P30341 | MLQAHTGYDLAIIGSGAGAFAAAIAARNKGRSVVMVERGTTGGTCVNVGCVPSKALLAAAEARHGAQAASRFPGIQATEPALDFPALISGKDTLVGQLRAEKYTDLAAEYGWQIVHGTATFADGPMLEVALNDGGTATVEAAHYLIATGSAPTAPHIDGLDQVDYLTSTTAMELQQLPEHLLILGGGYVGLEQAQLFARLGSRVTLAVRSRLASREEPEISAGIENIFREEGITVHTRTQLRAVRRDGEGILATLTGPDGDQQVRASHLLIATGRRSVTNGLGLERVGVKTGERGEVVVDEYLRTDNPRIWAAGDVTCHP... | 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 Lengt... |
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
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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
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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
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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
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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
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A0JN95 | MLRYPYFCRIHKNFLSCWLESGIYNLGVWPKKIHATAERYNEYEAQEETDQTGIQELHRSQDRDSGVMTKLHIPVMVDEVVRCLAPQKGQVFLDMTFGSGGHTRAILQKEPDITLYALDRDPTAYAIAEQLSELYPKQIRAILGQFSQAEALLMKAGVQPGTLDGVLLDLGCSSMQLDTPERGFSLRKDGPLDMRMDGDRYPDMPTAADVVNALDQQALASILRAYGEEKHAKKIASAIIQARGLYPITRTQQLASIVAGAFPPSALYARKDLLQRPTHIATKTFQAFRIFVNNELNELYTGLKTAQKFLRPGGHLVALS... | 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... |
A6NJ78 | MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLRPGGRLVALS... | 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-adenos... |
Q9DCL4 | MLRYPYFYRTYNRLFSHFVDSGASNLDVCPHTIHTAVALHTESKAVEGTALCGPQKVYSSEEKELEAMAKLHIPVMVDQVVHCLAPQKGQVFLDMTFGSGGHTRAILQKEPDVMVYALDRDPVAYAIAEQLSRLYPTQIQALLGQFSQAEALLMKAGVQPGTIDGILMDLGCSSMQLDAPERGFSLRKDGPLDMRMDGDRYPDTPTASDVVNALDQQALASILRAYGEEKHAKKIASAIIQARSTYPISRTQQLASIVAGAFPPSAVYARKDLLQRSTHIATKTFQALRIFVNNELNELYAGLRTAEKFLKTGGRLVALS... | 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... |
Q5R5T5 | MIRYPYFCRMYKECLSCWLESGIPNLGVWPKTIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVLHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAETLLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNAFDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYARKDLLQRSTHIATKTFQAVRIFVNNELNELYMGLKTAQKFLRPGGRLVALS... | 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... |
Q09357 | MSQNNEMHPRNPYRNKPPDFKALAVEYPEFRKFCQYVSNGKVTFDFKKDAAVRCLTQTLLKKDFNLDVEIPPGHLVPRVPQKLNYCLLIDDLLKANKLTKNVIGIDIGTGTSCIHALIGARQFNWKFIATDGDEKSVRVAHENVAKNGLSSSICVVHVNPDVKTVLMDVVNTIPDTDYAFCMCNPPFFEKGNGDDKFCEDISSSTETYSNRVASEFRTAPHSATFASSAELFVDGGEVAFVNRIIDDSVLLRDRIKIYTTMIGRKSSLKPLQNRLQRFGDDVKIMISVLNQGKTKRWMLAWTFSKSVSLTTIDRPISFQC... | 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'... |
Q6DC64 | MALNKSMHPRNRYKDKPPDFVYLASKYPEFQKHVQTTLTGRVTLNFKDPEAVRALTCTLLKEDFGLTIEIPLERLIPTVPLRLNYIHWVEDLIGGQGNPQRGIDIGTGASCIYPLLGATMNGWFFLATEVDDICFNYAKKNVEQNHLAELIKVVKVPQKTLLMDALKEESIVYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSINTGGVTEIMAEGGELEFVKRVIHDSLQLKKRLRWYSCMLGKKCSLAPLKDELRKQGVAKVTHTEFCQGRTMRWALAWSFYDDVPVPSPPCKKRKLEKARKPLTFTVLKATVAELQ... | 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-MET... |
Q554C9 | MSEIDTNDIKKEMDNKNYRDPTDNKELLKWTKKKRKRSNDSMHINNFYRYNPPNFKLLASKYPTFDKYIINKTEKIYNIDWKDSNATKELTRVLLDHDFGLRIELPDNYLCPTLTLRINYLYWISDQLKNLKIILNDNDNDNKIIKGIDIGTGTSCIFPLLGAKLFNNWSFIGIDIDDKVLEYAQNNITINSLNSKITLFKNEKNSDILLKLLNYKEGSNTFNSSNDDHQDNHDDDDDDEEYFADFCLCNPPFFKDLNENNNNKNNNPKSNCTGSVNEMVTDGGEFEFVKRIIKESFQLKCKIRFYTTMIGRKVNLNPLI... | 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
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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
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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:... |
Q86W50 | MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHVQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKSTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIIYDFCMCNPPFFANQLEAKGVNSRNPRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTYTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLASV... | 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-M... |
Q9CQG2 | MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKTTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIVYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLESV... | 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 ... |
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]... |
C7C8V4 | MLDHGTPIQPVSLPAAELDLGAVGGIAWPEPVQRRLRVGLLNNMPDSALVQTERQFRRLIGPGVELRLFSLDTVPRGPLARAHLDRFYETQGALAGAGLDALVVTGAEPKAERLADEPFFPALAAVVDWADASGVPTLFSCLAAHAAVLHLDGIERRPLPTKHSGIYACTAVAHHPLLAGMPASVPVPHSRWNDLPEQALTARGYRVLRRSEQVGVDLFVRERGASMVFLQGHPEYDGDTLAREYRRDIGRFLDGERDTPPALPENYYVDEAVLRLDAFAAVARAYRSPALHADFPTMAETLPRPAAWQEAAAGLFRNWL... | 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-succiny... |
P80877 | MTTIKTSNLGFPRIGLNREWKKALEAYWKGSTDKDTFLKQIDELFLSAVKTQIDQQIDVVPVSDFTQYDHVLDTAVSFNWIPKRFRHLTDATDTYFAIARGIKDAVSSEMTKWFNTNYHYIVPEYDESIEFRLTRNKQLEDYRRIKQEYGVETKPVIVGPYTFVTLAKGYEPSEAKAIQKRLVPLYVQLLKELEEEGVKWVQIDEPALVTASSEDVRGAKELFESITSELSSLNVLLQTYFDSVDAYEELISYPVQGIGLDFVHDKGRNLEQLKTHGFPTDKVLAAGVIDGRNIWKADLEERLDAVLDILSIAKVDELWI... | 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 catal... |
Q7VRI8 | MPVLSHILGFPRIGLYRELKHALEQYWEKKITENKLLDIGRMLRMRHWKQQINSGINLIPIGDFSWYDHVLDMSIMLNNIPTRFHILSQKKNTLNMLFSIARGDSINNTTITPSEMKKWFNTNYHYIVPEFVQNQIFKLNCTQLLAEIDEALSLNHPIKPVLLGPLTYLWIGKTKETKEFDRLSLLPSLLLVYKEIFNILSKKNIQWIQIDEPALVLELPQTWLKAYLHAYDQLYQTKIKLLLTTYFGKIYHQLPIIKQLKVNGLHIDLTNCSDNDISLLHEQLPKKWILSAGIINGKNIWKTNLYDWFLKLNTITHQRS... | 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): ... |
Q2KYF3 | MTITHNLGFPRIGAQRELKRAVEAYWAGKQTADELLATGRALRAAHWRRQADSGLRFVPVGDFAWYDHILEWTTLLGAVPARFAQPETQAVSLDTLFRMGRGRAPSGKPAAACEMTKWFDTNYHYIVPELVPGQTYRIAREDLFEQVREAQALGYAVKPVIPGPLTWLYLGKGDAFQQGASDEDKLKLLANLLPVYQQVLKRLADQGVEWVQIDEPILALDLPAAWRDAFGLAYAQLAGSPVKVLLATYFDGLKDNLSTVTKLPVAGLHVDLVRAPEQLDDVVEALHADQVLSAGVINGRNVWRTDLDQALRKLEPVARQ... | 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): ... |
Q8CMP5 | MTTIKTSNLGFPRLGRKREWKKAIENYWAHKIDKAELDQTLTDLHKENLLLQKNYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGREVNDDLLFDIARGNKEHVASALIKWFNTNYHYIVPEWDNVEPKVEKNTLLERFKYAQSINVNAHPVIVGPITFVKLSKGGHQSFEEKVETLLPLYKEVLQSLVDAGAEYIQIDEPILVTDDSESYEDITRKAYDYFANEGLGKYLVIQTYFERVHLKFLSSLPVGGLGLDLVHDNGYNLKQIEDGDFDQSKALYAGIIDGRNVWAADIEAKKQLIETLQQHTQQLVIQPSSS... | 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): ... |
Q82LG4 | MTAKSAAAAARATVYGYPRQGRGRELKKAIEGYWKGRLDADALRTTATGLRRDTWQQLAEAGIHEVPTGDFSYYDHVLDTSVMVGAIPARHRAAVEADALDGYFAMARGTQDVAPLEMTKWFDTNYHYLVPELGPDTVFSTDSAKQVAELGEALALGLTARPVLVGPVTYLLLAKPAPGVAADFDPLTLLDRLLPVYAEVLADLRAAGAEWVQLDEPALVQDRTPAELNAAERAYRVLGGLTDRPKLLVASYFDRLGDALPVLAEAPVEGLALDFAEGAAANLDALAAVGGLPGKRLVAGVVDGRNIWVNDLEKSLALLG... | 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): ... |
Q8CWX6 | MTKVSSLGYPRLGENREWKKLIEAYWAGKVSKNDLFAGAKELRLDFLKKQLNAGLDLIPVGDFSLYDHILDLSVQFNIIPKRFAKEPIDIDLYFAIARGNKENVASSMKKWFNTNYHYIVPEWSKQRPKLNNNRLLDLYLEAREVVGDKAKPVITGPITYVALSTGVEDFTAAVKSLLPLYKQVFTELVKAGASYIQVDEPIFVTDEGKDYLQAAKAVYAYFAKEVPDAKFIFQTYFEGLIDSQVLSQLPVDAFGLDFVYGLEENLEAIKTGAFKGKEIFAGVIDGRNIWSSDFVKTSALLETIEEQSAALTIQPSCSLL... | 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): ... |
Q2RMS5 | MAQSEYLFTSESVSEGHPDKVCDRISDAIVDAFLAEDPHSRVALETMATTNFVVLAGEVRGPDSLTHDRLKEIAREAIKDIGYEQRGFHWKDAEIVSHVHSQSADIAVGVDAAGNKDEGAGDQGIMFGYACTETEELMPAPIALSHAILKSLAEFRHGGDTSFGPDSKSQVTLRYVDGKPVGAASVVVSTQHAGNLSQDEVRELVRPHVLKVLPEGWMCPEEEFYVNPTGRFVIGGPDGDCGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLAEKCVIQVSYAIGVSKPLSVYVNTQGTG... | 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 en... |
A7NVX9 | METFLFTSESVNEGHPDKLCDQISDAVLDACLQQDPDSKVACETCTKTNMVMVFGEITTKANVDYEKIVRDTCREIGFVSDDVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYHNDGGARVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVANGLARRCIVQVSYAIGVPEPLSVFV... | 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 cata... |
P19358 | MSKSKTFLFTSESVGEGHPDKICDQVSDAILDACLEQDPFSKVACETAAKTGMIMVFGEITTKARLDYQQIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGLHYEKSLEDLGAGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLPWLRPDTKTQVTVEYEDDNGRWVPKRIDTVVISAQHADEISTADLRTQLQKDIVEKVIPKDMLDENTKYFIQPSGRFVIGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLCKRVQVQFSYAIGIAEPLSLH... | 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 triphosph... |
Q9SJL8 | METFLFTSESVNEGHPDKLCDQISDAILDACLEQDPESKVACETCTKTNMVMVFGEITTAAKVDYEKIVRSTCREIGFISADVGLDADKCNVLVNIEQQSPDIAQGVHGHLTKKPEDIGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNKTCPWLRPDGKTQVTVEYKNDGGAMIPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPAKYLDDNTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVAAGLARRCIVQVSYAIGVPEPLSVFV... | 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 cata... |
P50305 | MSQHKFLFTSESVSEGHPDKMCDQISDAVLDAHLAQDPHAKVACETVTKTGMIMLCGEITSKAVVDYQVLVRNVIKKIGYDDSSKGFDYKTCNVLVALEQQSPEIAAGVHVDKDSDDVGAGDQGIMFGYATDETEEAMPLTLLLSHKLNRKLHELRRSGELEWVRPDSKTQVTIEYASEGGACVPLRVHTVVISTQHSPDISLDDLRKELIEKVIKAVIPANLIDDKTIYHLNPCGSFIIGGPMGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPTKVDRSAAYAARWVAKSLVKSGLCRRCLVQVSYAIGVAKPLSVMV... | 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 triphosph... |
P40320 | MPQKTNGHSANGCNGSNGNSYDMEDGATFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSKGFDFKTCNVLLALDQQSPEIAAGVHVNRAEEEIGAGDQGIMFGYATDETEECMPLTVVLAHKLNEKIAELRRSDVFWWARPDSKTQVTCEYLFNQGSAVPKRVHTIVVSMQHSEKISLETLRSEVMEKVVKVVIPAKYIDANTIVHINPCGLFVIGGPMGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDFTKVDRSAAYAARWVAKSLVKAG... | 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 triphosph... |
Q58605 | MRNIIVKKLDVEPIEERPTEIVERKGLGHPDSICDGIAESVSRALCKMYMEKFGTILHHNTDQVELVGGHAYPKFGGGVMVSPIYILLSGRATMEILDKEKNEVIKLPVGTTAVKAAKEYLKKVLRNVDVDKDVIIDCRIGQGSMDLVDVFERQKNEVPLANDTSFGVGYAPLSTTERLVLETERFLNSDELKNEIPAVGEDIKVMGLREGKKITLTIAMAVVDRYVKNIEEYKEVIEKVRKKVEDLAKKIADGYEVEIHINTADDYERESVYLTVTGTSAEMGDDGSVGRGNRVNGLITPFRPMSMEAASGKNPVNHVG... | 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-methioni... |
P56878 | MKNFVFTSESVSEGHPDKIADQISDAVLDEILKHDPNGRVACETFVTTGLVLVGGEITTNTYVDIEQVVRNKIQEIGYNNPNYGFDGSCCAVISSIIKQSPDIAMGIDNENEEEIGAGDQGMVFGYACNETKSLMPAPIYYAHLLMKRQAYLRKQNILSWLRPDAKSQVTLRYENNKPIVIDSVVLSTQHHPEIQQKDLIEAVIEEIIKPTLPTNLLHKDTKYLINPTGRFVIGGPVADCGLTGRKIIVDSYGGMAKHGGGCFSGKDPTKIDRSAAYMARYIAKNIVGAGLADRCEIQISYAIGVADPVSVYAETFGTSK... | 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 en... |
Q5LLL2 | MSRQNYIFTSESVSEGHPDKVCDRISDAVLDAFLTEEPEARVACETFATTNRVVIGGEVGLSDQAKLREYMGRIDQIARDCIKDIGYEQDKFHHETVEITNLLHEQSAHIAQGVNAAEGKDEGAGDQGIMFGYATTETPALMPAPIQYSHAILRRLAEVRKNGTEPALGPDAKSQLSVIYRDGMPVGVSSLVLSTQHLDPDLTSADIRAIVEPYIREVLPEGWLSADTVWHVNPTGKFVIGGPDGDAGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLADKCTIQLSYAIGVSKPLSIYA... | 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 en... |
Q980S9 | MRNINVQLNPLSDIEKLQVELVERKGLGHPDYIADAVAEEASRKLSLYYLKKYGVILHHNLDKTLVVGGQATPRFKGGDIIQPIYIIVAGRATTEVKTESGIDQIPVGTIIIESVKEWIRNNFRYLDAERHVIVDYKIGKGSSDLVGIFEASKRVPLSNDTSFGVGFAPLTKLEKLVYETERHLNSKQFKAKLPEVGEDIKVMGLRRGNEVDLTIAMATISELIEDVNHYINVKEQVRNQILDLASKIAPGYNVRVYVNTGDKIDKNILYLTVTGTSAEHGDDGMTGRGNRGVGLITPMRPMSLEATAGKNPVNHVGKLY... | 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-methioni... |
Q7M7Z2 | MRKEFLFTSESVTEGHPDKMADQISDAILDYIIERDPKARVACETLLSNGFCVIAGELKTTTYAPMQEIAREVIREIGYTDALYGFDYRSAGILNGVGEQSPDINQGVDREDGEIGAGDQGLMFGYACRETETLMPLPIFLSHKITEGLAKARKDGTLPFLRPDGKSQVTVRYVDGKPVGIDTIVVSTQHAPDVSQERLRDAVIEEIVYKVLPKEYLGDDIRFFVNPTGKFVIGGPQGDAGLTGRKIIVDSYGGSCPHGGGAFSGKDPSKVDRSGAYAARYVAKNLVASGVCDKATIQIAYAIGVVEPVSILVDTHGTGK... | 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 en... |
Q89LP2 | MVRFEGISKTYPAYRGKPGVNALQDIDFAIPRGSITGVIGRSGAGKSSLVRLINGLEKPTTGRVIVDNKDISALAGRELRLAQRSIGMIFQHFNLLSSRTAADNIALPLEIAGWARADIKARVAELLALVGIADKHDRYPSELSGGQKQRVGIARALATRPSVLLSDEATSALDPQTTRAILDLLANINRELGVTIVLITHEMSVVRQLAREVVVLDAGHVVESGHVADIFTHPKHPITQSFLAEVVGDSLPVSLASRIVSEPSAGGQAVIRVQVRGAGAGDTVVARLARELGLDVALLAARIDEIGGQHVGSLVLGVPG... | 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 Len... |
Q2YIV5 | MQHAAVCSGTSRHRRTTVTIEKPPATSAPIVEMKDVRRMFGETAAINGVSLSVARGEILGIIGRSGAGKSTLIRCVNGLEKPDTGSIHIEGREITSLDEDALRPVRRRIGMVFQHFNLLSAKTAAQNIALPLKIAGMPKAERIKRVAELLELVGLSDKASHYPAQLSGGQKQRVGIARALAAEPAVLLSDEATSALDPETTQSILALLKDINAKLGLTILLITHEMDVIRRIADRVIVLDHGLIAEEGPVWKVFANPQSPVTQSMLQVLTPELPAIWRNRLEKKGDQAILRVKLSGMAAKGAFFNDVAAATSLAPQLIHG... | 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 Len... |
Q0PAB6 | MIKIKNLKKYYGKELVINDVSLEIKKGEIYAIVGHSGAGKSTLLRCINGLENYQEGSLKVFDQEIKDLSQKKSKELRMLRKDIGMIFQNFALMERKNVFENVAMPLRTHYTQCKFHAKLFNKEYMSEKEIAQKVNSLLEIVGLDHKNKSYPRELSGGQKQRVAIARALALNPKILLSDEATSALDPNTTKNILELISKINAEFGITVVLVTHEMDVVKDIAQKALLLEHGQIIGSGAIDELFLRPNAKMKEFLGESDFLPEHGLNIKLYFPKEVAQNSVITHMARTLNIDFNIVWGKIEKLNGKALGNLVININEKDKDK... | 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 Len... |
Q3J1N0 | MRDEQATGAAITFDRVEKSFAQKGGAPVMALSDCTLTVEPGAITGIIGRSGAGKSTLLRMVNGLERPTGGRVLVGGRDVGAADGAELREIRREVGMIFQHFNLLASRTVFGNVALPLEIAGRPSSEIRTRVADLIARVGLEALADRYPAELSGGQKQRVGIARALATGPKVLLSDEATSALDPETTQTVLRLLADINRDLGLTILLITHEMGVVRDIATHMAVIDGGRIVEAGPTYDIFVRPEHPTTRSFLSGVTGVTLPAFVASRLRPAPPEGPSQEVIRITFAGRHATDPMLARLTGELGIAVNILAGAIEEIGPHPF... | 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 Len... |
Q9Z8Q8 | MSEQHSPIISVQDVSKKLGDHILLSKVSFSVYPGEVFGIVGHSGSGKTTLLRCLDFLDMPTSGSISVAGFDNSLPTQKFSRRNFSKKVAYISQNYGLFSSKTVFENIAYPLRIHHSEMSKSEVEEQVYDTLNFLNLYHRHDAYPGNLSGGQKQKVAIARAIVCQPEVVLCDEITSALDPKSTENIIERLLQLNQERGITLVLVSHEIDVVKKICSHVLVMHQGAVEELGTTEELFLNSENSITNELFHEDINIAALSSCYFAEDREEVLRLNFSKELAIQGIISKVIQTGLVSINILSGNINLFRKSPMGFLIIVLEGEV... | 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 Len... |
Q1QVQ7 | MIKLEGVSKTYGAGPTAVHALKNIDLDVPQGAIHGVIGLSGAGKSTLIRCVNLLERPTSGRVIVDGQDLTRQDAEALRQSRHQLGMIFQHFNLLASRTVFDNVALPLELMGVSKSDIRERVEPLLDLTGLTDKARQYPAQLSGGQKQRVAIARALASRPKVLLCDEATSALDPQTTASILELLQDINRKLGLTILLITHEMEVVKSICHRVGLISDGELVEEADVGDFFTAPATRLGRDFLNAFLELEPPQALVERLEETAGPHTHPVVRLAFSGATVATPLISRLARDSGVDVSILQAKVESIQGRTLGLMIAELIGSP... | 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 Len... |
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 Len... |
Q18C09 | MISIKNVNKYYGKIQVLKDVSIEIESGEIFGIIGHSGAGKSTLLRCINGLEEYQEGSVLVSDKEVKSLNEKQMRDLRKELGMIFQHFSLLERKTVFDNVALPLECFGYSKAEIKKRVLELLEVVGISEKKNDKPRNLSGGQKQRVAIARALALNPQVLLCDEATSALDPNTTKSILSLLEDINKKLGITIIVVTHQMEVIKQICGRVAIMENGEVLEVGDTEEIFLRNTKGLRKLIGEESIILPKGTNIKILFPKDISNEAIITTMARELNIDVSIIFGKLEQFKDDILGSLIINISDKSGEQVKQYLTSKGIRWEEMIN... | 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 Len... |
G0J5N4 | MNLQSPHLTIEMTQEIFYCQEALSLESGESFPEFQLSFTTQGQLNANKDNVIWVLHALTGDANPHEWWSGLIGEDKFFDPSKYFIVCANFLGSCYGSTQPLSNNPNNGKPYYYDFPNITTRDIASALDKLRIHLGLEKINTVIGGSLGGQVGLEWAVSLGEKLENAIIVASNAKASPWIIGFNETQRMAIESDSTWGKTQPEAGKKGLETARAIGMLSYRHPMTFLQNQSETEEKRDDFKISSYLRYQGLKLANRFNAMSYWILSKAMDSHDIGRGRGGTPVALSNIKCKVLSIGVDTDILFTSEESRYISKHVPKGTYR... | 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-homoser... |
D3P9D1 | MKENSVGLVKTKYVTFKDDFYFESGRILSPITVAYETYGKLNEKKDNAILICHALTGSAHAAGYNSPDDQKPGWWDDMIGPGKAFDTDKYFIICSNFLGSCYGTTGPASIDPSTGKPYGLKFPVFTVKDMVKLQKKLIDYLGIEKLLCVAGGSMGGMQALEWAVTFPEKTYSIIPIATAGRITPMAIAFNTIGRFAIMKDPNWMNGDYYGKTFPRDGLAIARMAGHITYMSDKSFHKKFGRRYATFGGIYDFFGYFEVENYLRYNGYKFTERFDANSYLYIIKAMDIFDLSYGYGSYEEAIGRIEADSLFITFTSDFLFP... | 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-homoser... |
Q1J115 | MTALISQPDLLPPPAPERCPPQQTARLFRETPLLLDCGQVVQDVRVAYHTYGTPSDHAILVLHALTGTSAVHEWWPDFLGEGKPLDPTRDYIVCANVLGGCAGSTGPAELPRVNGEDPPLTLRDMARVGRALLEELGVRRVSVIGASMGGMLAYAWLLECPDLVDRAVIIGAPARHSPWAIGLNTAARNAIRAAPGGEGLKVARQIAMLSYRSPESFALTQSGWGTRRPGTPDITTYLEHQGEKLSTRFCERSYLALTGAMDRFQPTDAELRSIRVPVLVVGISSDVLYPPAEVRTYAGLLPRGQYLELQSPHGHDAFLI... | 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-homoser... |
Q5FUF4 | MDISASPSIADGPVYTHQTVRLDSGLDLECGVHLAPLEVAYCTYGTLSPARDNAILVCHALTGDQYLAERNPLTGKPGWWSRMVGPGLPIDTDRYFVVCSNVLGGCMGTTGPRSICAETGKAWDSEFPPITMHDIVAAQAKLIDHLGIDRLFAVIGGSMGGMQALTWAADFPDRVFAAMPIATSPFHSAQNIAFNEVSRQAIFADPDWHDGHYRDFGAIPARGLGVARMMAHITYLSEEALSRKFGRRVRHDAATAVPASSSPSLFGEMFEVESYLRHQGSSFVRRFDANSYLTITRAMDYFDLAAEHDGDLANPFRKSQ... | 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-homoser... |
P45131 | MSVQNVVLFDTQPLTLMLGGKLSHINVAYQTYGTLNAEKNNAVLICHALTGDAEPYFDDGRDGWWQNFMGAGLALDTDRYFFISSNVLGGCKGTTGPSSINPQTGKPYGSQFPNIVVQDIVKVQKALLDHLGISHLKAIIGGSFGGMQANQWAIDYPDFMDNIVNLCSSIYFSAEAIGFNHVMRQAVINDPNFNGGDYYEGTPPDQGLSIARMLGMLTYRTDLQLAKAFGRATKSDGSFWGDYFQVESYLSYQGKKFLERFDANSYLHLLRALDMYDPSLGYDNVKEALSRIKARYTLVSVTTDQLFKPIDLYKSKQLLE... | 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 produc... |
B9LTF0 | MSTVPTDHGVAALGEFVFECGQSVPDLEVAYETHGEFDGDNVVLVCHALTGSQNVARSPAPERNEGTRGAGQAGQARAWWDDIVGPGKAIDTTKYYVVCANVPGSCYGTTGPASERPADLDLPEEPDHDRWGTAFPPVQVEDWARSQRRLLDHLGVGRLRAVVGGSVGGMNVLEWAKRYPDDVDRVVAIATAGRLDAQCLALDAVARRAIRADPNWNGGNYYGEGRPSPDEGLALARQIGHIMYLSKASMERKFGRRSAGRDSLTREEGDLGLPPEPTAAFFPYREVESYLDYQAEGFSERFDANSYLYLTRAMDEYDLS... | 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-homoser... |
P57715 | MPTTELDGFTFACGDTVDSLTVAYRTYGDYTGSNAVLVCHALTGSQHVRGRADGDDRGWWPDIVGPGRPIDTTEYFVVCANVPGSCHGTDGPPADGPGGDPWGTAFPPVTVPDWTRCQRRLLDTLGVDRLHAVVGGSVGGMNALDWARRYPDDVHRIAAVATAPRLDAQCLGLNAIARRAIRGDPNWNDGDYYGGAHPDRGLALARQLGHVMYLSKASMADKFGRRTATTDTALPADPAAEFFATRDVESYLDYQADTFVARFDANSYLYLLRAMDAYDLAAGRPSVADALAAFDGDALVLSFTGDWHFTAAQSATVADA... | 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-homoser... |
Q6ADB9 | MDWQTTSADTAPSSFITEEQDRSLFGKPPASGAWKESDPVGGRRFAGIGAFGFESGESLPFVRIAYETWGELSPARDNAVLVLHALTGDSHAVGAAGPGHRTSGWWQGIIGPGKAIDTDRWFVAVPNMLGGCQGTTGPTSIAPDGAEWGARFPFTTIRDQVKAQAAFADALGIGRWAAVVGGSMGGMQALEWAVGFPERVERLAVIAAPPHSTADQIAFNSVQLGAIRTDPLFHGGSYYDEKDGEGPHQGLALARRMALITYRSLSELNDRFERTWQSGISPLGDGGRFAVESYLDFHGNKFTRRFDANSYLTLVQAMNS... | 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-homoser... |
Q8CBH5 | MAADDKVAILTDDEEEQKRKYVLADPFNGICREPEPPSNETPSSTETSAIPEEEIDWIEKHCVKVNNDLLISKVFYFFFYSAYGSLYPLLPVYYKQLGMSPSQSGLLVGIRYFIEFCSAPFWGVVADRFRKGKIVLLFSLLCWVLFNLGIGFVKPATLRCLPKIPPTAHPTNVSHPVTVLPMNSSTVAFFSTPPKLLQKRDVQLSETEPNISDIDLVSTALTLTSEPTRRPQTEAITHPVTGLILNTSTVTLPPTGNVTRETTIAVVTTTKSLPSDQVTLVYDQQEVEAIFLIILVVVIIGEFFSASSVTIVDTVTLQYL... | 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
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Q0VA82 | MPLEESGENTPLLRGEIISDGDTDRSRWRSIRVMYFTMFLSSVGFTIVITSIWPYLKKIDESADASFLGWVVAAYSLGQMVASPFFGLWSNHRPRREPLVCSIFINVSANIYYSYVYLPPSHNQIHMLLARTFVGIGAGNVAVVRSYVAGATSLKERTSAMANMSACQALGFILGPALQAVLSFIGETGVSVDVIKLQVNMYTAPALLAACFGVINILLVILVLREHSVDDHGNRIRPINYTPEERVDVPPEVEGDIDHIAVFTSNVLFFIILFIFAVFETISTPLSMDMFAWTRKEAVLYNGIILAAIGFESILVFLVV... | 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 | MAGLRNESEQEPLLGDTPGSREWDILETEEHYKSRWRSIRILYLTMFLSSVGFSVVMMSIWPYLQKIDPTADTSFLGWVIASYSLGQMVASPIFGLWSNYRPRKEPLIVSILISVAANCLYAYLHIPASHNKYYMLVARGLLGIGAGNVAVVRSYTAGATSLQERTSSMANISMCQALGFILGPVFQTCFTFLGEKGVTWDVIKLQINMYTTPVLLSAFLGILNIILILAILREHRVDDSGRQCKSINFEEASTDEAQVPQGNIDQVAVVAINVLFFVTLFIFALFETIITPLTMDMYAWTQEQAVLYNGIILAALGVEA... | 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
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Q6GPQ3 | MASIDDDDDERTPLLQDSHIGELVETQKQLKSRWWSIRVMYLTMFLSSVGFSIVMTSIWPYLQKVDQSADASFLGWVIASFSLGQMVASPLFGLWSNHRPRREPLVVSITILVAASCLYAYVHVPASHNKYYMLLARTFVGFGSGNVAVVRSYVAGATSLSERTGAMANISAFQAMGFILGPAFQAALSVIGETGITINGISLQVNMYTAPALMGALLGIGNIILIFAIFREHRVDDLEKNVSSINSESEVTDVEKANEGPIDQIAVISSNILFFVVLFVFAIFETISTPLTMDMYAWTRTQAVFYNGIILAAVGVESVI... | 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
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A0QYL8 | MSAPQAAIDTDHADRHGPRRAWAAVGVLALVGTLNYVDRFLPSVLAEPIKHDLELSDTAIGVINGFGFLIVYAVMGIAVARVADRGAFGAVVAGCLTLWGTMTMLGGAVQSGFQLALTRVGVAIGEAGSTPAAHAYVARNFVPQRRSAPLAVITIAIPLASTASLLGGGLLAQSLGWRTAFVIMGAVSVVLAPLVLLVVGVRQSLPAAPAVVDKTAGGWWNLLRKPSFLIVVAGTAFISAAGYSLTTFSPAFLMRTRGMSLGEVGVEYGLATGAIGVLGLLIVGRLADRLAERDPRWLLWIVVTLTLVLLPASVLAFVVE... | 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
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E5AE35 | MSTLCAFPVPYSTIEVLNIVLPYRTYSARLLYLHAPLGNHLPFCHRSYNVLHLRQDCDSHMYSAGNDVRLSQEAVTMSDQRSHDTTADQSARDASSLDTRKIHGFPWFLLVISVLSSIFLYALDNTIVADIIPAIANDFSSINDLGWLSVGFVIGGVAVIMPLGKLYGILNTKWLYITSVVLFMAASAVCGAAPDMNAEIVGRVFAGAGGIGMYIGTMILLSINTSDQERPAYLSLVGLVWGIGTVLGPVIGGSFEKVDWRWAFYLNLVIGALLFPVWFFLLPSFHPAKHLSLNKRLSQFDFVGAILSIGAFVTTIMPIN... | 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... |
Q947B7 | MAALLVFFSVSLILLAVLFHKRKSSLSSRKRPPPSPLRLPVIGHFHLIGALSHRSFTSLSKRYGEVMLLHFGSAPVLVASSAAAAREIMKNQDVIFASRPRLSIFDRLMYSGKGVAFAPYGEHWRNARSMCMLQLLSAKRVQSFGGIREEETSAMIEKIRRSKPTTVVNLSEMFMALTNGVIHRAVLGRKGDGGDDFNRILIKVIKLLGSFNVGDYVPWLSWINRINGVDAEVEKVGTKLDGSMEGILRKYRRKKVGDDETNFVDTLLQFQRESKDTDPVEDDVIKALIFDMVSAGTDTTFAALEWTMAELIKNPRTLKT... | 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 Mas... |
Q9SGU9 | MAHFLETQEPLVFSGKKRNDRDDEDGDALVAKKSALAVCDADPAAAIANIRHEFGEHGGVNMSIEASATFTVMEPDTMRRMFTGELGPDNDFYVYSRHFNPTVLNLSRQMAALEGTQAAYCTSSGMSAISSVMLQLCSSGGHVVAASTLYGGTHALLSHFLPRTCNITTSFVDITDHGAVANAIVEGRTQVLYFESVANPTLTVADIPELSRMAHEKGVTVVVDNTFAPMVLSPAKLGADVVVHSISKFISGGADIIAGAVCGSENLVKEMMDLRGGSLMLLGPTMNAKVAFELSERIPHLGLRMREHSHRAQVYAERMR... | 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 (m... |
P32266 | MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPG... | 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 (... |
Q9BQP7 | MKMKLFQTICRQLRSSKFSVESAALVAFSTSSYSCGRKKKVNPYEEVDQEKYSNLVQSVLSSRGVAQTPGSVEEDALLCGPVSKHKLPNQGEDRRVPQNWFPIFNPERSDKPNASDPSVPLKIPLQRNVIPSVTRVLQQTMTKQQVFLLERWKQRMILELGEDGFKEYTSNVFLQGKRFHEALESILSPQETLKERDENLLKSGYIESVQHILKDVSGVRALESAVQHETLNYIGLLDCVAEYQGKLCVIDWKTSEKPKPFIQSTFDNPLQVVAYMGAMNHDTNYSFQVQCGLIVVAYKDGSPAHPHFMDAELCSQYWTK... | 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 (mtDN... |
Q9CXC3 | MKLPLTFCRLLSRLNRFSVKASPPVSFSTFSYLCSQKKKNSYEAVDQAKYSRLVRSVLSRGPAQTPESLFKEDDVLYGPVSKHKAAEPEPQARVPQHCFPIFNEERTGKPHTDASSSPLKIPLQRNSIPSVTRILQQTMPPEQSFFLERWKERMVLELGEDGFAEYTSNVFLQGKQFHKALESILSPQENLTGGEEHPQCGYIESIQHILTEISGVQALESAVQHEALKYVGLLDCVAEYRGKLCVIDWKTSEKPKPLIRNTYDNPLQVVAYMGAVNHDAHYSFQVQCGLIVVAYKDGSPAHPHFMDEELCSKYWAKWLL... | 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 (mtDN... |
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 irrever... |
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 irrever... |
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 rea... |
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 irrever... |
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 rea... |
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 irrever... |
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 irrever... |
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