ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q89WW0 | MTAFHSVAVIGAGAWGTALAMVAARAGRSVTLWARNAEHATRIASTRDNPRLPGVRLAPDIVVTSELALAARADMLLIATPAQHLRGAVNMLASHIARPTPVVACAKGIEHGTHKFMTEVIAEAALHAQPAILSGPSFADDVARGLPTAVTLAAKEEELASSLVQALGSPTFRPYHSTDVRGVEIGGAAKNVLAIAAGIVVGRNLGASALAALTTRGFSELARLGRACGARPETLSGLSGLGDLLLSCSTAQSRNFALGIALGRGEAAPAGKLAEGAFTAPVLVELAAARNVDMPVSQAVAAILDNKLTIDAAIEGLLTRPFKAEE | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 33282
Sequence Length: 326
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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C0QYQ8 | MINVGIIGAGGWGLALANIFSEKHNVKVWVHSESSYKLLSTSYRNDNYLENIQLNKSIKFTTDVGEAVNDSEIVIIVTPSFAFADACINIEPYISNDQILVSATKGLDRKTGKTMSEVARSIISGDLSILTLSGPSHAEEAAKGVPTAVVVGGEKGVSEYVRDTLTVPPKFRIYNSTDQKGVEIGGALKNIIAIAGGIVDGLKLGDNTKAALITRGLHEIVRFALSKGARIDTMYGLSGIGDLIVTCSSGLSRNNRLGRELAKGKKYQDVIAENHGQVAEGVYATTAAYEYAQKNNIYMPITEAIYNILFNDANIQDTLTELMSKDAKSEGFF | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35835
Sequence Length: 333
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q5ZT56 | MNKKTIAMLGAGSWGTAVAIHLAKIGHKTLLWSHNPQHVALMAEQHSNPAYLPGIPFPENLIPSDNLIECVQSADYVIIAVPSHAFAEIINKIPKPTQGLAWLTKGVDPASHELLSQLVASRFGVDFPIAVISGPSFAKEVARFLPTALTLASNNTNYQKKMHQLFHHDNIRVYLSDDLIGVQLCGAVKNILAIACGISDGLGYGANAKAALITRGLAEMTRLGLSMGARQDTFLGLAGVGDLVLTCTDDQSRNRRFGLLLGREVPIPEAEHQIGQVVEGKHNAAQICAIANKNKVEMPICEQINALLHGIVHAQEAVNNLMSRPAKEE | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35410
Sequence Length: 329
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
P90551 | MSTKQHSAKDELLYLNKAVVFGSGAFGTALAMVLSKKCREVCVWHMNEEEVRLVNEKRENVLFLKGVQLASNITFTSDVEKAYNGAEIILFVIPTQFLRGFFEKSGGNLIAYAKEKQVPVLVCTKGIERSTLKFPAEIIGEFLPSPLLSVLAGPSFAIEVATGVFTCVSIASADINVARRLQRIMSTGDRSFVCWATTDTVGCEVASAVKNVLAIGSGVANGLGMGLNARAALIMRGLLEIRDLTAALGGDGSAVFGLAGLGDLQLTCSSELSRNFTVGKKLGKGLPIEEIQRTSKAVAEGVATADPLMRLAKQLKVKMPLCHQIYEIVYKKKNPRDALADLLSCGLQDEGLPPLFKRSASTPSKL | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 39272
Sequence Length: 366
Subcellular Location: Glycosome
EC: 1.1.1.8
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Q6AFK3 | MIGAGSWGTTFAKILADGGNDVVVWARRPELAREIDEGKRNSDYLQGINLPRSLRATSHLGEAMRGAEQVFVSLPSQTLRSNLDAMIPYLGPATVVISLMKGVEKGTGLRMSEVIAQGLPIDPEQIAVVSGPNLALEIAREQPTAAVVSSVSPATAVAVATSATNRYFRSFVNTDVIGTEFGGVLKNLIAVAIGIVDGVGYGENTKASIITRGLVEMTDFAVAYGADPQTLSGLAGLGDLIATCESPLSRNNTAGRLLGQGYSFTDVVKQMDQAAEGLASVTPILSLAEARGVEMPIVRQVSQVLAGTLAPKDIAPHLTTDDEPQGERTRGERTTDDGQGQGRTSVWGSLKRAFDQLRDGGGSSRRDRP | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 38846
Sequence Length: 369
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
Q4FPT7 | MDKQLLIFDFDGTLIDSVPDLADAVNAMLTTLGKAPYPIDTIRNWVGNGSRMLVERALVGKIEVSEGELAKETIDHAEQVFFDAYSKMGGSKTVAYPNVDSGLKKLKAAGFKLALVTNKPIRFVPKILQFFGWHDIFSEVLGGDSLPTKKPDPAPLLHVCEVLNINPAQAVMIGDSINDILAGQNANMDTLGLSYGYNYGQDIRQLNPTEAFDDFSALVDYLLKAYPANN | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 25142
Sequence Length: 230
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
Q98ML8 | MSRPIIVFDLDGTLIDTAPDLLDSLNHSLAASELTAVDEAGFRRFVGHGGRVMIERAHAAQQRSLDVAEHDRLLKLFLDHYTDNIPGKSRPYPGVIEAIARFEKAGYLLAICTNKYEANSLALIEALGLTRHFAAIAGQDTFAFRKPDPRHLTETIRLAGGDAHRALMVGDSQTDIDTAKAAGIPVVAVDFGYTDRHVREFEPSAVISHFDALTVELAERLIRAAGH | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24821
Sequence Length: 227
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
O33512 | MAPALIFDLDGTLIDSAPAIHKVSNDVLRARGYAPLGLDQIRSFVGQGAPHLVRCLLTTAGEDPEGPLFDAIYADLVSRYETDVEGNTLYPGVITALQRLREMGCPMAITTNKPYKPALAAIAHVGLTDYFQLVIGGDSLPTRKPNPEMVNEARRVLRRPHALYIGDSEIDAQTAQNAGLPFVIYTEGYRKTPLDALPHAAKFHDFSALPGIVEGWTWS | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress (By similarity).
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 23853
Sequence Length: 219
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
Q2RPW9 | MPKAVIFDLDGTLVHSLPGLTDALNKTLAEDDLAPLDEAAVKRMVGEGAGLLVARAFAAYGLGRADDADDTATQARLARFLAHYAPDPLAGASVYPGALALLGALAARGIRLGVCTNKPEGPARALLEGLGLADPIMDVVGGDTLAQRKPDPAPLRALLDSLGVEADQALMVGDSPTDVATAKAAGVPVVVMSYGYSREPVASLGALAVFDDFASLGDWLGFPQPGGDRLGATPALSENPA | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24507
Sequence Length: 241
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
Q55039 | MQAIIFDFDGTLVDSLPTVVAIANAHAPDFGYDPIDERDYAQLRQWSSRTIVRRAGLSPWQQARLLQRVQRQLGDCLPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFSVVQAGTPILSKRRALSQLVAREGWQPAAVMYVGDETRDVEAARQVGLIAVAVTWGFNDRQSLVAACPDWLLETPSDLLQAVTQLMRQ | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 23556
Sequence Length: 212
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
Q3SGR5 | MKSFPLPIKAVVIDLDGTLLNTAPDLAHAAELMMAELGRPCPSLETISTYIGNGVSRLVKRVLTGEMDAEPDPALFAQAIASYQKHYGEHVSLHSRPFDGVVEGLQAFKAMGLHMACITNKAEQFTVPLLKGTGLYDYFELILSGDTLPKRKPDPLPLLHACEVFGVAPAELLLIGDSLNDTQAARAAGCPVFCVPYGYNRGRPVTELDLDAVVPSLAEAALMVTKA | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24331
Sequence Length: 227
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
Q9KNV6 | MKSIKLIAFDLDGTLLDSVPDLAVAADQAARAVGYPAVSEAQVRDYVGNGADVLIARALSQSLTINPELSPELRAQARHLFDEFYEQTGHKLSHLYPNVKTTLLELHQAGFILALVTNKPSKFVPDVLEQHGIAHFFSDVIGGDTFPNKKPDPMALNWLLEKHQLSAEQMLMVGDSKNDILAAKNAGCYSFGLTYGYNHGEPIANAEPDFVSDDIGTLLEVVLVSA | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24560
Sequence Length: 226
Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
|
Q7NJF7 | MALLVMVRHGQSIWNLENRFTGWTDVPLTEKGRAEARACGELIYCVPFAVAFTSKLTRAQDTLRLILEAADQPDVPVIEDQALNERHYGELQGLNKAETAAKYGEETVRQWRRSLEGRPPGGESLKDTALRSLRYFYEKIVPELEAGKNVLVSAHGNTIRAILMELDHLSPEQVEKVEIEYCVPVAFEHQADGTFSQVLMPRCDIIRPPQPPARSIARL | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 24664
Sequence Length: 219
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
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Q82TU0 | MKKLVLLRHGESIWNQENRFTGWTDVDLTPKGLKEAEEAGRLLRENGFSFDIAYTSLLKRAIRTLWIALDEMDQMWTPIELNWRLNERHYGALQGLNKAETAKQYGDEQVLVWRRSYDIRPPSITINDERYPGFDLRYRNMSSGDIPLAESLKDTVARFLPYWNQSIAPQIKAEKKVIIAAHGNSLRALIKHLDNISDQDILNCNIPTGIPLVYELDDDLKPLNSYYLGDAGQIGEAISAVANQGKSGA | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28317
Sequence Length: 249
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
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Q11SV1 | MPILVIVRHGQSEWNLKNLFTGWSDVELTPTGEHEAEYAGIVLRPYHFDIAFTSVLKRAIHTLSIILNQTGATIPIIENEALNERNYGDLQGLNKAEVGEKYGAQQLIAWRRSYTEVPPGGESLENTCQRVIPYYQEKIEPELKDGRNVLIVAHGNSLRALMMHLEKISPEDIAHVDLATGAPRLYEFSSKLDLNSVSYIKLPETPLDVSTLL | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 23920
Sequence Length: 213
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
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Q727C0 | MARLILLRHGQSAWNLENRFTGWTDVDLSPAGEAEALAAARLIRDEGLDFSVCHTSMLTRAIRTLHLVQQELDRLWTPVRKHWRLNERHYGALQGLDKRETAARHGEDQVFVWRRSYDVPPPVIAPDDPKHPVHDPRYADVPPDVLPCGESLEATVARVLPYWYDAIAPDLMAGRDVLVAAHGNSLRALVMHLDGLDREDVSRLDIPTGLPRLYELDAALRPVSYRYLGDPAEAEERARAVAAQGRLEKN | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28208
Sequence Length: 250
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
P96121 | MKLVLIRHGESEWNRLNLFTGWTDVPLTPRGESEAQEGGRVLQEAGFDFDLCYTSFLKRAIRTLNFVLQALDREWLPVHKSWKLNERHYGDLQGLNKTETAQKYGEQQVRVWRRSFDVAPPPLTVGDARCPHTQASYRGVCASGRTPVLPFTESLKDTVARVVPYFEEEIKPQMISGQRVLIVAHGNSLRALMKHIESLDETQIMEVNLPTGVPLVYEFEADFTLCGKRFLGNEADVAARAQAVADQGKSN | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28358
Sequence Length: 251
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
Q83HD5 | MDNLVLLRHGNSLWNQENLFTGWVDVRLSELGEKEAKTAGQLLREANRYPDVLFTSLLTRSIQTAHIALMEIDRVWLPTFRSWRLNERHYGSLQGKNKAQVLEEFGEEQFNSWRRGYDTPPPPLHSQADDPRYEEPPPLSESLKDVQNRLLPYWQGVILPHLVAGKVVLVVAHGNSLRALVKHLECISDTDVCQLNIPTGIPLVYSIDPSGCATHPGRYLP | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 25123
Sequence Length: 221
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
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P37689 | MLVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIRAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAVEGGKLSDIAPTMLSLMGMEIPQEMTGKPLFIVE | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA).
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 56194
Sequence Length: 514
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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A5FJ26 | MNKKVILMILDGWGKSPDPKVSAIDNANVPFINSLYKNYPSAQLRTDGLNVGLPEGQMGNSEVGHMNLGAGRIVYQDLAKINLAVAHKTLAKEQVLIDAFTYAKENNKKVHFLGLVSDGGVHSHTSHLRGLIDASQEYGLDQVYVHAFTDGRDVDPKSGAKYIHDLQDYIKDTPVKIASIVGRYYAMDRDKRWERVKLAYDLVVNGVGTPSTNPVSSVLESYEKDVTDEFIEPVVIVDENAKPLATIVEGDVVIFFNFRTDRGRELTEALSQHDFHEQNMHKLNLYYVTLTNYDETYQNVKVVYNKDNITETLGEVLEKAGKKQIRIAETEKYPHVTFFFSGGREIPFEGESRILRNSPKVATYDLQPEMSAYELADALVPELNKGEVDFVCLNFANGDMVGHTGIMEAAIKACEAVDACAKKVIDAALANDYTTIVIADHGNCETMINPDGSPNTAHTTNPVPIILVDKQLKNIQDGVLGDIAPTILELMGVQQPNAMTCHSLL | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 55874
Sequence Length: 505
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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A6H1H2 | MNKKVILMILDGWGKSPDPKVSAIDNANIPFINSLYKNYPSAQLRTDGLNVGLPEGQMGNSEVGHMNLGAGRIVYQDLAKINLAVQNKTLSQEKALKEAFQYAKENNKPIHFLGLLSDGGVHSHTSHLRGLLDAAQNFGLKKTFIHAFTDGRDVDPKSAIATIENLNKYIHNTPAKLASVIGRYYAMDRDKRWERIKLAYDLLVNGKGKPSQDAVLSISNSYQNNITDEFIEPIIMTDDNNNPIATIQEDDVVIFFNFRTDRGRELTEALSQQDFHEQNMHKLNLYYVTLTNYDETYKNVKVIYNKDNITQTLGEVLEKAGKKQIRIAETEKYPHVTFFFSGGREQPFLGESRILKNSPKVATYDLQPEMSAYELTEALIPEIEKTEADFICLNFANGDMVGHTGIMSAAIKACQAVNKCVEKVITAALAHNYTTIVIADHGNCETMINPDGTPNTAHTTNPVPIILVDKELKTIHDGVLGDIAPTILDLMGIKKPEVMTRNSLL | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 56282
Sequence Length: 505
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
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Q6CZD8 | MLSSSSLYAAIDLGSNSFHMLVTRETAGSIQTLAKIKRKVRLAAGLDKQNRLSQEAMQRGWQCLQLFSERLQDIPQDQVRVVATATLRLATNADEFLQRAQEILGLPIQVISGEEEARLIYQGVAHTTGGPDARLVVDIGGGSTELATGIGAKTTQLISLPMGCVTWLDRYFSDRNLEAGNFERAENAAREMLRPVAASLREQGWQICVGASGTVQALQEIMVAQGMDEYITLPKLRQLKEHAIQCDKLEELEIDGLTLERALVFPSGLAILLAIFQELDIKTMTLAGGALREGLVYGMLHLPVDQDIRHRTLATLQRRYLLDTEQAKRVSTLADNFLQQVARDWQLDSRCRELLRSACMVHEIGLSIDFRQSPQHAAYLIRHSDLPGFTPAQKKLLATLLQNQINPIDLMPLSQQNALPVNQAQHLCRLLRLAIIFASRRRDDTLPAVRLRVEGEALRLILPAGWLAQHPLRAEMLEQESRWQSYVHWPLMLEEAPA | Function: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.
Catalytic Activity: guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine 3',5'-bis(diphosphate) + H(+) + phosphate
Sequence Mass (Da): 55719
Sequence Length: 498
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 2/2.
EC: 3.6.1.40
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Q15N19 | MITSTRLPQNHPEELYAAVDLGSNSFHLVIVRVVAGSVQIIGKVKQKVRLAAGLDDNMMLDNESLERGWRCLETFAERLQDIPRDNIRVVATATLRLAKNADVFTVKAQQILDHTLSVISGEEEARQIYLGVAYTSANQGNSLVIDIGGASTEIIIGNDMTPIHLVSLNMGCVTFKERHFAGDVLSEENFAAAIDAAKAMVDAVADKFVCFDWQQCLGASGTPQAITEILVAQGISDAIRLDYLYNLRQQCIDCSTLDNLIIDGLDESRRIIFPSGLAILIALFESLSIRDMQISGGALREGLIYGMLENMQQNDRRMQTIHQHMQHFHIDSEQAERVTEVALTLFKQLSEQTDVDGIDGEAMLVAAAMLHETGLHIEYKLHHKHGAYILGHVPMVGYTNLQRDGIKTLVLNHRQQISPEVFDQNHSETRGIMRSLVRVLRLACILSIRRKDNLLPQFCLEVEENDWRLVFPEGWLKAHPLIDAELANEKWQQHKMGWHLTCE | Function: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.
Catalytic Activity: guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine 3',5'-bis(diphosphate) + H(+) + phosphate
Sequence Mass (Da): 56404
Sequence Length: 503
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 2/2.
EC: 3.6.1.40
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Q3IDD5 | MGQLKPQKNVYAVIDLGSNSFHMLIAKSIAGGLQTIGRVKRKVRLAAGLDIDNVLSSEAMHRGWECLALFAERLQDIPKQNITIVATATLRLASNADVFKAQAEKILGHKVNVISGELEARTIYKGVAHTSSCTGSQLVIDIGGASTEVIIGKNFDALLYKSLNIGCVTYLERYFKDCKLSNANFNTAIKAARTVIDEIASEYKVKGWQIASGASGTVQAIQEIMIAQNLDELLTLEKLYTIKKQSIAYKTIAALDLPGLSEDRRLVFVSGLAILIALFESLEIEKMGLAGGALREGVLYSMLPELHNSDIRKRTIDGFIDRYHVDQKQASRVASLVLNLASEVNESWPIKALNGLPLLTAVAQLHEIGLLIEYKQYHKHSAYILKNTEMPGFSQSEHKVIVAVAKGHRSDLQKGYFDSLGANSVLAQYLVRLIRIAVILCMRRQDDVLPEFAITVKDDVLNLQFENDWLKNHPLMASELQQESKQQAKLGWKLIVN | Function: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.
Catalytic Activity: guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine 3',5'-bis(diphosphate) + H(+) + phosphate
Sequence Mass (Da): 54968
Sequence Length: 497
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 2/2.
EC: 3.6.1.40
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Q9BZJ8 | MESSPIPQSSGNSSTLGRVPQTPGPSTASGVPEVGLRDVASESVALFFMLLLDLTAVAGNAAVMAVIAKTPALRKFVFVFHLCLVDLLAALTLMPLAMLSSSALFDHALFGEVACRLYLFLSVCFVSLAILSVSAINVERYYYVVHPMRYEVRMTLGLVASVLVGVWVKALAMASVPVLGRVSWEEGAPSVPPGCSLQWSHSAYCQLFVVVFAVLYFLLPLLLILVVYCSMFRVARVAAMQHGPLPTWMETPRQRSESLSSRSTMVTSSGAPQTTPHRTFGGGKAAVVLLAVGGQFLLCWLPYFSFHLYVALSAQPISTGQVESVVTWIGYFCFTSNPFFYGCLNRQIRGELSKQFVCFFKPAPEEELRLPSREGSIEENFLQFLQGTGCPSESWVSRPLPSPKQEPPAVDFRIPGQIAEETSEFLEQQLTSDIIMSDSYLRPAASPRLES | Function: Orphan G-protein coupled receptor. Constitutively activates the G(s)-alpha/cAMP signaling pathway . Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization . May be involved in the regulation of food intake and body weight (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49292
Sequence Length: 451
Subcellular Location: Cell membrane
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Q8C010 | MESSPIPQSSGNSSTLGRALQTPGPSTASGVPELGLRDVASESVALFFMLLLDLTAVAGNAAVMAVIAKTPALRKFVFVFHLCLVDLLAALTLMPLAMLSSSALFDHALFGEVACRLYLFLSVCFVSLAILSVSAINVERYYYVVHPMRYEVRMTLGLVASVLVGVWVKALAMASVPVLGRVYWEEGAPSVNPGCSLQWSHSAYCQLFVVVFAVLYFLLPLILIFVVYCSMFRVARVAAMQHGPLPTWMETPRQRSESLSSRSTMVTSSGAHQTTPHRTFGGGKAAVVLLAVGGQFLLCWLPYFSFHLYVALSAQPISAGQVENVVTWIGYFCFTSNPFFYGCLNRQIRGELSKQFVCFFKAAPEEELRLPSREGSIEENFLQFLQGTSENWVSRPLPSPKREPPPVVDFRIPGQIAEETSEFLEQQLTSDIIMSDSYLRPAPSPRLES | Function: Orphan G-protein coupled receptor. Constitutively activates the G(s)-alpha/cAMP signaling pathway (By similarity). Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization (By similarity). May be involved in the regulation of food intake and body weight .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49382
Sequence Length: 449
Subcellular Location: Cell membrane
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Q9BZJ7 | MANSTGLNASEVAGSLGLILAAVVEVGALLGNGALLVVVLRTPGLRDALYLAHLCVVDLLAAASIMPLGLLAAPPPGLGRVRLGPAPCRAARFLSAALLPACTLGVAALGLARYRLIVHPLRPGSRPPPVLVLTAVWAAAGLLGALSLLGTPPAPPPAPARCSVLAGGLGPFRPLWALLAFALPALLLLGAYGGIFVVARRAALRPPRPARGSRLHSDSLDSRLSILPPLRPRLPGGKAALAPALAVGQFAACWLPYGCACLAPAARAAEAEAAVTWVAYSAFAAHPFLYGLLQRPVRLALGRLSRRALPGPVRACTPQAWHPRALLQCLQRPPEGPAVGPSEAPEQTPELAGGRSPAYQGPPESSLS | Function: Orphan G-protein coupled receptor. Constitutively activates the G(q/11)/inositol phosphate and the G(s)-alpha/cAMP signaling pathways . Has spontaneous activity for beta-arrestin recruitment . Shows a reciprocal modulation of signaling functions with the melatonin receptor MTNR1B most likely through receptor heteromerization .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37614
Sequence Length: 368
Domain: Lacks the conserved DRY and BBXXB motifs. The restoration of these motifs affects its constitutive activity.
Subcellular Location: Cell membrane
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Q9BZJ6 | MVFSAVLTAFHTGTSNTTFVVYENTYMNITLPPPFQHPDLSPLLRYSFETMAPTGLSSLTVNSTAVPTTPAAFKSLNLPLQITLSAIMIFILFVSFLGNLVVCLMVYQKAAMRSAINILLASLAFADMLLAVLNMPFALVTILTTRWIFGKFFCRVSAMFFWLFVIEGVAILLIISIDRFLIIVQRQDKLNPYRAKVLIAVSWATSFCVAFPLAVGNPDLQIPSRAPQCVFGYTTNPGYQAYVILISLISFFIPFLVILYSFMGILNTLRHNALRIHSYPEGICLSQASKLGLMSLQRPFQMSIDMGFKTRAFTTILILFAVFIVCWAPFTTYSLVATFSKHFYYQHNFFEISTWLLWLCYLKSALNPLIYYWRIKKFHDACLDMMPKSFKFLPQLPGHTKRRIRPSAVYVCGEHRTVV | Function: Orphan receptor. May play a role in brain function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47578
Sequence Length: 419
Subcellular Location: Cell membrane
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Q6YNI2 | MNASAAALNESQVVAVAAEGAAAAATAAGAPDTGEWGPPAASAALGGGGGPNGSLELSSQLPAGPSGLLLSAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLVGSLATADLLAGCGLILHFVFQYVVPSETVSLLMVGFLVASFAASVSSLLAITVDRYLSLYNALTYYSRRTLLGVHLLLAATWTVSLGLGLLPVLGWNCLADRTSCSVVRPLTRSHVALLSTSFFVVFGIMLHLYVRICQVVWRHAHQIALQQHCLAPPHLAATRKGVGTLAVVLGTFGASWLPFAIYCVVGSQEDPAIYTYATLLPATYNSMINPIIYAFRNQEIQRALWLLFCGCFQSKVPFRSRSPSEV | Function: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38085
Sequence Length: 363
Subcellular Location: Cell membrane
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P51651 | MNASAAALNESQVVAVAAEGAAAAATAAGTPDTSEWGPPAASAALGGGGGPNGSLELSSQLPAGPSGLLLSAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLVGSLATADLLAGCGLILHFVFQYVVPSETVSLLMVGFLVASFAASVSSLLAITVDRYLSLYNALTYYSRRTLLGVHLLLAATWTVSLGLGLLPVLGWNCLADRASCSVVRPLTRSHVALLSTSFFVVFGIMLHLYVRICQVVWRHAHQIALQQHCLAPPHLAATRKGVGTLAVVLGTFGASWLPFAIYCVVGSQEDPAIYTYATLLPATYNSMINPIIYAFRNQEIQRALWLLFCGCFQSKVPFRSRSPSEV | Function: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Promotes neurite outgrowth and blocks myelin inhibition in neurons.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38115
Sequence Length: 363
Subcellular Location: Cell membrane
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Q6X632 | MNTSAPLQNVPNATLLNMPPLHGGNSTSLQEGLRDFIHTATLVTCTFLLAIIFCLGSYGNFIVFLSFFDPSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHLTSSGFVIMSLKMVAVIALHRLRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMSSLMDGEGKAILSLYVVDFTFCVAVVSVSYIMIAQTLRKNAQVKKCPPVITVDASRPQPFMGASVKGNGDPIQCTMPALYRNQNYNKLQHSQTHGYTKNINQMPIPSASRLQLVSAINFSTAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFTLIFFKSGLNPFIYSRNSAGLRRKVLWCLRYTGLGFLCCKQKTRLRAMGKGNLEINRNKSSHHETNSAYMLSPKPQRKFVDQACGPSHSKESAASPKVSAGHQPCGQSSSTPINTRIEPYYSIYNSSPSQQESGPANLPPVNSFGFASSYIAMHYYTTNDLMQEYDSTSAKQIPIPSV | Function: G protein-coupled receptor that is activated by the chemokine CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it stimulates inositol trisphosphate production and calcium mobilization upon activation. Together with CCL5/RANTES, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin secretion by pancreatic islet cells through activation of this receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59531
Sequence Length: 540
Subcellular Location: Cell membrane
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Q96P69 | MGPGEALLAGLLVMVLAVALLSNALVLLCCAYSAELRTRASGVLLVNLSLGHLLLAALDMPFTLLGVMRGRTPSAPGACQVIGFLDTFLASNAALSVAALSADQWLAVGFPLRYAGRLRPRYAGLLLGCAWGQSLAFSGAALGCSWLGYSSAFASCSLRLPPEPERPRFAAFTATLHAVGFVLPLAVLCLTSLQVHRVARRHCQRMDTVTMKALALLADLHPSVRQRCLIQQKRRRHRATRKIGIAIATFLICFAPYVMTRLAELVPFVTVNAQWGILSKCLTYSKAVADPFTYSLLRRPFRQVLAGMVHRLLKRTPRPASTHDSSLDVAGMVHQLLKRTPRPASTHNGSVDTENDSCLQQTH | Function: Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39332
Sequence Length: 363
Subcellular Location: Cell membrane
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Q96P67 | MNNNTTCIQPSMISSMALPIIYILLCIVGVFGNTLSQWIFLTKIGKKTSTHIYLSHLVTANLLVCSAMPFMSIYFLKGFQWEYQSAQCRVVNFLGTLSMHASMFVSLLILSWIAISRYATLMQKDSSQETTSCYEKIFYGHLLKKFRQPNFARKLCIYIWGVVLGIIIPVTVYYSVIEATEGEESLCYNRQMELGAMISQIAGLIGTTFIGFSFLVVLTSYYSFVSHLRKIRTCTSIMEKDLTYSSVKRHLLVIQILLIVCFLPYSIFKPIFYVLHQRDNCQQLNYLIETKNILTCLASARSSTDPIIFLLLDKTFKKTLYNLFTKSNSAHMQSYG | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38409
Sequence Length: 336
Subcellular Location: Cell membrane
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Q9NYM4 | MVPHLLLLCLLPLVRATEPHEGRADEQSAEAALAVPNASHFFSWNNYTFSDWQNFVGRRRYGAESQNPTVKALLIVAYSFIIVFSLFGNVLVCHVIFKNQRMHSATSLFIVNLAVADIMITLLNTPFTLVRFVNSTWIFGKGMCHVSRFAQYCSLHVSALTLTAIAVDRHQVIMHPLKPRISITKGVIYIAVIWTMATFFSLPHAICQKLFTFKYSEDIVRSLCLPDFPEPADLFWKYLDLATFILLYILPLLIISVAYARVAKKLWLCNMIGDVTTEQYFALRRKKKKTIKMLMLVVVLFALCWFPLNCYVLLLSSKVIRTNNALYFAFHWFAMSSTCYNPFIYCWLNENFRIELKALLSMCQRPPKPQEDRPPSPVPSFRVAWTEKNDGQRAPLANNLLPTSQLQSGKTDLSSVEPIVTMS | Function: G-protein coupled receptor for PEN, a neuropeptide produced from the precursor protein, proSAAS (encoded by PCSK1N). Acts through a G(i)- and G(q)-alpha-alpha-mediated pathway in response to PEN . Plays a role in food intake and body weight regulation. May contribute to the regulation of anxiety-related behaviors (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48339
Sequence Length: 423
Subcellular Location: Cell membrane
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P30731 | MKVPPVLLLFLLSSVRATEQPQVVTEHPSMEAALTGPNASSHFWANYTFSDWQNFVGRRRYGAESQNPTVKALLIVAYSFTIVFSLFGNVLVCHVIFKNQRMHSATSLFIVNLAVADIMITLLNTPFTLVRFVNSTWVFGKGMCHVSRFAQYCSLHVSALTLTAIAVDRHQVIMHPLKPRISITKGVIYIAVIWVMATFFSLPHAICQKLFTFKYSEDIVRSLCLPDFPEPADLFWKYLDLATFILLYLLPLFIISVAYARVAKKLWLCNTIGDVTTEQYLALRRKKKTTVKMLVLVVVLFALCWFPLNCYVLLLSSKAIHTNNALYFAFHWFAMSSTCYNPFIYCWLNENFRVELKALLSMCQRPPKPQEDRLPSPVPSFRVAWTEKSHGRRAPLPNHHLPSSQIQSGKTDLSSVEPVVAMS | Function: G-protein coupled receptor for PEN, a neuropeptide produced from the precursor protein, proSAAS (encoded by PCSK1N). Acts through a G(i)- and G(q)-alpha-alpha-mediated pathway in response to PEN . Plays a role in food intake and body weight regulation . May contribute to the regulation of anxiety-related behaviors .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48137
Sequence Length: 423
Subcellular Location: Cell membrane
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Q8SSH7 | MERGMESEAFYGLSARGWDGSEVSLGSFRGCVIMIANVASSCKFAESNYKSFAGLLDKFYRKGLRILLFPCNQYLGQESRPIEEIRGEVSKKYSDRFVVFDKVDVFGKGAHPVFRHLVNTKNGKGRLGNFIKWNFTKFLVDRKGCVVKRFGPSDIVKEDDENLLRSIEDGENGMQNS | Function: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Catalytic Activity: a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O
Sequence Mass (Da): 20029
Sequence Length: 177
Subcellular Location: Cytoplasm
EC: 1.11.1.12
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C0HLL8 | TELSGAPLDLYQYRGQVLLIPQFTGLLYQKSQQEGDVVDGLPSHQFHQY | Function: Glutathione peroxidase which may protect the cell from oxidative damage.
Catalytic Activity: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Sequence Mass (Da): 5579
Sequence Length: 49
EC: 1.11.1.9
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G9JJU2 | MSLENGTDVSFEEFRGKVVLVINVATYUGLTVPSYTQMNALAEFYVDQDFVILGFPCNQFEMLEPAANAEIMNGIRYVRPGDGFEPLMTLFEKTEVNGATEDPLFTFLKSACESTYTEFYSSLFYEPIRIGDIQWNFEKFLIGKDGKPYTRYHPDVVDPEALKDDINTLLSA | Function: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione (By similarity). May defend against reactive oxygen species that accumulate during the immune response.
Catalytic Activity: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Sequence Mass (Da): 19557
Sequence Length: 172
EC: 1.11.1.9
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Q9CX99 | MESVALYSFQATESDELAFNKGDTLKILNMEDDQNWYKAELRGAEGFVPKNYIRVKPHPWYSGRISRQLAEETLMKRNHLGAFLIRESESSPGEFSVSVNYGDQVQHFKVLREASGKYFLWEEKFNSLNELVDFYRTTTIAKRRQIFLCDEQPLIKPSRACFAQAQFDFSAQDPSQLSLRRGDIVEVVEREDPHWWRGRAGGRLGFFPRSYVQPVHL | Function: Couples signals from receptor and cytoplasmic tyrosine kinases to the Ras signaling pathway. Plays a role in the inner ear and in hearing.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25277
Sequence Length: 217
Subcellular Location: Membrane
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Q932F1 | MQILLVEDDNTLFQELKKELEQWDFNVAGIEDFGKVMDTFESFNPEIVILDVQLPKYDGFYWCRKMREVSNVPILFLSSRDNPMDQVMSMELGADDYMQKPFYTNVLIAKLQAIYRRVYEFTAEEKRTLTWQDAVVDLSKDSIQKGDDTIFLSKTEMIILEILITKKNQIVSRDTIITALWDDEAFVSDNTLTVNVSRLRKKLSEISMDSAIETKVGKGYMAHE | Function: Member of the two-component regulatory system GraR/GraS involved in resistance against cationic antimicrobial peptides (CAMPs). Upon phosphorylation by GraS, functions as a transcription regulator by direct binding to promoter regions of target genes such as adhesins, exoproteins, transporters, toxins, and proteins involved in cell wall synthesis. Down-regulates the expression of many genes involved in RNA and amino acid synthesis or glycolysis.
PTM: Phosphorylated by GraS. Phosphorylated by Stk1; phosphorylation increases the DNA-binding activity of GraR.
Sequence Mass (Da): 26039
Sequence Length: 224
Subcellular Location: Cytoplasm
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P50972 | MSLFDGKKVIIIGDRDGIPGPAIAECLKGTAAEVVYSATECFVUTAAGAMDLENQNRVKGFADQFGAENLVVLVGAAEAESAGLAAETVTAGDPTFAGPLAGVQLGLRVFHAVEPEFKDAVDSAVYDEQIGMMEMVLDVDSIIAEMKSIREQFGKFND | Function: In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination.
Catalytic Activity: [thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) = [thioredoxin]-dithiol + glycine + H(+) + phosphate
Sequence Mass (Da): 16656
Sequence Length: 158
EC: 1.21.4.2
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Q75JT4 | MKILLYIAIILSFFSLITISSECKIAVLLSGSPNDLGYNYLMNEARVKAESELKLDFSIYYENLEESMEEAEKAFQDALHKGANLIVVGSFVHVGLGLKYAALTKDQDIYWIIRGNKRPNPDLPHVVILNFNSFELHYLLGYFSGLMTKTGIVGFVAPGPDVNTISTDNSFYLGAKYARPNITFLNVYVQSWYNPNVSYSAAKMLIKNGADLIGMSQDDMSCQKAMMDSGLIGIGATGYPTHLLFGGNVGVSYITNWTNLYVKYAQHVLNDDWPDYSSYFTNLSREDSIFIDDYSYKVPIDIQNLVNDEIQRLKNTSYIPYRSDPYLAQLGIPFDSKGLLVEDQFRANKKLLKGDSISKVIDFGQYSIPIEFIDYPNSLKYGVTIVSGVCIFICLVCMTLVVVFKKARVIKSSSPAFLLLILLGCCIIFAACILFAQSPTNQTCSARIWLLSLGYTLFLGNLLVKNWRIWLLFDNPKLKKRAITNWKLYPWVFAILAIDVMILAIWQGLGNINAESRIGYDSLTQYQYKNVCSSDDQGSIALYLLLVFHGLVLLVACFISFKIKVVDIEEFNESKPITTSVYIITFCLFIVIPLMVSPQSLTSQTTIICVCAIVTTLISMLLLFGSKFYKMATQGLAINETFATSTKSSSKSSKSSYGKDNPNPNAINFGEDDTSDETSEEKHKSPKQKSVNFSNKSNSHLAVFTSDEETSKTSKLSIDFENSSKDISIDQLQQQKQQPINTNGDLENKSNDKIDDDNDNSSVLSKRISNQQNGETEIDSNNV | Function: May act during the development and be a negative regulator.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87581
Sequence Length: 783
Subcellular Location: Cell membrane
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Q09630 | MDKKWSLEQRWLHLLNQQFLDCLNHLFNHYRRLSTFQKPPSIIRHMFSVLALAIQILANVNVVAQTTEAVDLAPPPKVRQIRIPGDILIGGVFPVHSKSLNGDEPCGEIAETRGVHRVEAMLYALDQINSQNDFLRGYKLGALILDSCSNPAYALNQSLDFVRDMIGSSEASDYVCLDGSDPNLKKQSQKKNVAAVVGGSYSSVSVQLANLLRLFRIAQVSPASTNADLSDKNRFEYFARTVPSDDYQAMAMVEIAVKFKWSYVSLVYSADEYGELGADAFKKEARKKGICIALEERIQNKKESFTESINNLVQKLQPEKNVGATVVVLFVGTEYIPDILRYTAERMKLTSGAKKRIIWLASESWDRNNDKYTAGDNRLAAQGAIVLMLASQKVPSFEEYFMSLHPGTEAFERNKWLRELWQVKYKCEFDTPPGSTASRCEDIKQSTEGFNADDKVQFVIDAVYAIAHGLQSMKQAICPDDAIENHWISRYSKQPEICHAMQNIDGSDFYQNYLLKVNFTGKTISIFSSFRLSPFSDIVGKRFRFSPQGDGPASYTILTYKPKSMDKKRRMTDDESSPSDYVEIGHWSENNLTIYEKNLWWDPDHTPVSVCSLPCKIGFRKQLIKDEQCCWACSKCEDYEYLINETHCVGCEQGWWPTKDRKGCFDLSLSQLKYMRWRSMYSLVPTILAVFGIIATLFVIVVYVIYNETPVVKASGRELSYILLISMIMCYCMTFVLLSKPSAIVCAIKRTGIGFAFSCLYSAMFVKTNRIFRIFSTRSAQRPRFISPISQVVMTAMLAGVQLIGSLIWLSVVPPGWRHHYPTRDQVVLTCNVPDHHFLYSLAYDGFLIVLCTTYAVKTRKVPENFNETKFIGFSMYTTCVVWLSWIFFFFGTGSDFQIQTSSLCISISMSANVALACIFSPKLWIILFEKHKNVRKQEGESMLNKSSRSLGNCSSRLCANSIDEPNQYTALLTDSTRRRSSRKTSQPTSTSSAHDTFL | Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 113276
Sequence Length: 999
Subcellular Location: Cell membrane
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Q8IUY3 | MTALSRSEATEEGGNQQMHRKTASLNSPVSCKEKPDRVEEPPDYSLHWPEGLKGEEIKKCGREGITLNKYNQQYHKLFKDVPLEEVVLKVCSCALQRDFLLQGRLYISPNWLCFHASLFGKDIKVVIPVVSVQMIKKHKMARLLPNGLAITTNTSQKYIFVSLLSRDSVYDLLRRVCTHLQPSSKKSLSVREFSGEPESLEVLIPEMKWRKVCPSSRSLSLPDNIPCIPPSSVDSTDSFFPSRKPPMSEKSRAQVASENGGRWAWPMPGWGPACPKKMPNCSPTAKNAVYEEDELEEEPRSTGELRLWDYRLLKVFFVLICFLVMSSSYLAFRISRLEQQLCSLSWDDPVPGHR | Function: Participates in the organization of endoplasmic reticulum-plasma membrane contact sites (EPCS) with pleiotropic functions including STIM1 recruitment and calcium homeostasis. Constitutive tether that co-localize with ESYT2/3 tethers at endoplasmic reticulum-plasma membrane contact sites in a phosphatidylinositol lipid-dependent manner. Pre-marks the subset of phosphtidylinositol 4,5-biphosphate (PI(4,5)P2)-enriched EPCS destined for the store operated calcium entry pathway (SOCE).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40249
Sequence Length: 354
Domain: GRAM domain is required for specific location to endoplasmic reticulum-plasma membrane contact sites (EPCS). Mediates interaction to phosphatidylinositol lipids and binding to plasma membrane.
Subcellular Location: Endoplasmic reticulum membrane
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Q3V3G7 | MQMKMMFFCLSDWQSNQQMHGKMAPLKSHVPCTEKPGKVQEPPDDGSLHWSEGSKGEDIKKYSREGTLRSKYNQQYHKLFKDIPLEEVVLKVCSCALQRDLLLHGRLYISPNWLCFHASLFGKDIKVVIPVVSVQLIKKHKMARLLPNGLAITTNTSQKYVFVSLLSRDSVYDMLRRVCTHLQPSSKKSLSIRKFPEEAECESPEVLIPEMKWRKACSAPASLSLPDSISCISQIPTDSTDSCFPSRKPPGSEAVCEKDALEEEPSTDQELRLWDSRLLKVIFVMICFLVLSSSYLAFRISRLEQQLCSLSWGSPLPRDR | Function: Participates in the organization ofendoplasmic reticulum-plasma membrane contact sites (EPCS) with pleiotropic functions including STIM1 recruitment and calcium homeostasis. Constitutive tether that co-localize with ESYT2/3 tethers at endoplasmic reticulum-plasma membrane contact sites in a phosphatidylinositol lipid-dependent manner. Pre-marks the subset of phosphtidylinositol 4,5-biphosphate (PI(4,5)P2)-enriched EPCS destined for the store operated calcium entry pathway (SOCE).
PTM: Phosphorylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36441
Sequence Length: 320
Domain: GRAM domain is required for specific location to endoplasmic reticulum-plasma membrane contact sites (EPCS). Mediates interaction to phosphatidylinositol lipids and binding to plasma membrane.
Subcellular Location: Endoplasmic reticulum membrane
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Q14416 | MGSLLALLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPTVCNGREVVDSTTSSL | Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95568
Sequence Length: 872
Subcellular Location: Cell membrane
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P21729 | MAPNNCSHLNLDVDPFLSCNDTFNQSLSPPKMDNWFHPGFIYVIPAVYGLIIVIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLVTCAPVDASKYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAALIWIVSMLLAIPEAVFSDLHPFHVKDTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLAIISVYYYFIARNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLMNRSHSTGRSTTCMTSFKSTNPSATFSLINRNICHEGYV | Function: Receptor for gastrin-releasing peptide (GRP) . Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation . Contributes to the regulation of food intake . Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain . Contributes primarily to nonhistaminergic itch sensation . In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear . In another study, shown to contribute to disinhibition of glutamatergic cells in the auditory cortex via signaling on vasoactive intestinal peptide-expressing cells which leads to enhanced auditory fear memories . Contributes to the induction of sighing through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43215
Sequence Length: 384
Subcellular Location: Cell membrane
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A8ETJ2 | MFGKSIEAYTKACEVIPGGVDSPVRAFKSVGGTPPFIKKGKGAYLYDVDGNKYVDFVQSWGPLIFGHCDKDIEKVVIKTAKKGLSFGAPTKLETKLASEIVEMYDNIDKVRFVSSGTEATMSAIRLARGVTGKNDIVKFEGCYHGHSDSLLVQAGSGLATFGSPSSPGVPSDLTKHTLLCEYNNIKNLEKCFADSSDIACIIIEPIAGNMGLVPASEEFLKACRELCDKHGALLIFDEVMSGFRASLTGASGIVKTKADIITFGKVIGAGMPVGAFAASKEIMSNLSPEGKIYQAGTLSGNPVAMAAGLKSLRKLKANPDIYDELNKKALRLVNGLKKIANKYEIPFQVDTRGSMFGFFFCEKEPKNFKDVGLCDFKRFATFHHEMLKKGFYFACSQYETGFICTKITNKDIDACLKAANEVMKNL | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46184
Sequence Length: 426
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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O29027 | MKLDKSRKLYAEALNLMPGGVSSPVRAFKPHPFYTARGKGSKIYDVDGNAYIDYCMAYGPLVLGHANEVVKNALAEQLERGWLYGTPIELEIEYAKLIQKYFPSMEMLRFVNTGSEATMAALRVARGFTGRDKIVKVEGSFHGAHDAVLVKAGSGATTHGIPNSAGVPADFVKNTLQVPFNDIEALSEILEKNEVAALILEPVMGNSSLILPEKDYLKEVRKVTAENDVLLIFDEVITGFRVSMGGAQEYYGVKPDLTTLGKIAGGGLPIGIFGGRKEIMERVAPSGDVYQAGTFSGNPLSLTAGYATVKFMEENGVIEKVNSLTEKLVSGIADVLEDKKAECEVGSLASMFCIYFGPTPRNYAEALQLNKERFMEFFWRMLENGVFLPPSQYETCFVSFAHTEEDVEKTVEAVSESL | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 45754
Sequence Length: 418
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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P30949 | MRSYEKSKTAFKEAQKLMPGGVNSPVRAFKSVDMDPIFMERGKGSKIFDIDGNEYIDYVLSWGPLILGHTNDRVVESLKKVAEYGTSFGAPTEVENELAKLVIDRVPSVEIVRMVSSGTEATMSALRLARGYTGRNKILKFEGCYHGHGDSLLIKAGSGVATLGLPDSPGVPEGIAKNTITVPYNDLESVKLAFQQFGEDIAGVIVEPVAGNMGVVPPQEGFLQGLRDITEQYGSLLIFDEVMTGFRVDYNCAQGYFGVTPDLTCLGKVIGGGLPVGAYGGKAEIMEQIAPSGPIYQAGTLSGNPLAMTAGLETLKQLTPESYKNFIKKGDRLEEGISKTAGAHGIPHTFNRAGSMIGFFFTNEPVINYETAKSSDLKLFASYYKGMANEGVFLPPSQFEGLFLSTAHTDEDIENTIQAAEKVFAEISRR | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46449
Sequence Length: 430
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
|
P56115 | MELLHSINDFNEAKQVIAGGVNSPVRAFKSVKGTPPFILKGKGAYLYDVDNNHYIDFVQSWGPLIFGHADEEIEENIINALKKGTSFGAPTELETTLAKEIISCYEGLDKVRLVSSGTEATMSAIRLARAYSQKDDLIKFEGCYHGHSDSLLVKAGSGCATFGSPSSLGVPNDFSKHTLVARYNDLNSTEECFKKGNVGCVIIEPIAGNMGLVPAQKEFLLGLKALCEKYQAVLILDEVMSGFRASLSGSQEFYGVVPDLVTFGKVIGAGLPLACFGGRAEIMDLLSPIGSVYQAGTLSGNPLAVCAGLSALYKIKRDKTLYTRLDALAIRLTQGLQKSAQNYNIALETLNMGSMFGFFFNENAVHDFDDALKSDTEMFAKFHQKMLFKGVYLACSSFETGFICEPMTEEMIDLTIAKADESFDEIIKGV | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46727
Sequence Length: 430
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
|
B4U8M6 | MTNKEAFELAKKYMPGGVSSPVRAFKSVGAEPIVVNRGFGAFVEDIEGKKYIDYMLSFGPLILGHRSEIVVSKIMEALDKGNSFGITNMYEIELSELIIKASKVIDKVRFVSSGTEAVMSAIRLARGITNKPYIIKFDGCYHGFSDSVLVGAGSGVATLGIPGTPGIPKEFAALTIVLDYNDENALEEAFIKYKNQIAAVLVEPVAGNMGVVLPKESWLKKLRDITKENDALLIFDEVITGFRLALGGAAEYFGIEPDIVCYGKIIGGGMPIGAYGAKNHIMERVAPEGPIYQAGTLSGNPISVASGLAILKTLIKDIAIYDRLSELRAYLTYTLSKMLSEKGIPHRINEIASMFTIFFTDKDVIDFKSAKTSDTALFGKFFRNALKEGVLMPPSQFEAWFLSTAHTKDVVDTTLEKLKKAIDLL | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46312
Sequence Length: 425
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
|
A9GDD3 | MTNATSAPPARADRAPASKALFDRAAAVLPGGVNSPVRAFRAVGGDPLFIARAQGARLFDADGAEYIDYVGSWGPAILGHAHPAVIEAVREAALGGLSFGAPTELEVRFAEKIRELYPSIDMLRCVSSGTEATMSAIRVARGFTRRDAIIKFEGCYHGHADHLLVKAGSGLATFGAPDSAGVPESIARTTLSLPYNDPAALEAAFAARGGDIAAVILEPVVGNMGCVPPEPGFLALVIDLCRKHGALSIFDEVMTGCRLARGGAQERFGLRPDLTTLGKIVGGGMPLAAYGGRADVMRVVSPLGPVYQAGTLSGNPLAVTAGLATLDRLTPALYERLEELGASLEEGLRAAAEGAGAAACVQRVGSMITLFFTKGPVRSWADAATSDTKRFSAFHAAMLARGIYWPPSQYEAAFLSGAHSEEDIERTIAACREALAA | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 45491
Sequence Length: 437
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
|
P45621 | MAVSAITGARLTLGMSLSSSTRSRTVAMAVSIDPKTDNKLTLTKSEEAFAAAKELMPGGVNSPVRAFKSVGGQPIVIDSVKGSRMWDIDGNEYIDYVGSWGPAIIGHADDQVLAALGETMKKGTSFGAPCLLENTLAELVIDAVPSIEMVRFVNSGTEACMGALRLARAYTGREKIIKFEGCYHGHADPFLVKAGSGVATLGLPDSPGVPKAATFETLTAPYNDTEAIEKLFEANKGEIAAVFLEPVVGNAGFIVPKPDFHSFLRKITKENNTLLVFDEVMTGFRLSYGGAQEYFGITPDITTLGKIIGGGLPVGAYGGRRDIMEKVAPAGPMYQAGTLSGNPLAMTAGIETLQRIKEPGTYEYLDKITGELVEGIIEAGKRAGHAICGGHIRGMFGFFFTEGPVYNFADAKKSDTAKFARFFWGMLAEGVYLAPSQFEAGFTSLAHTSDDIKKTIAAAEKVFREI | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 49646
Sequence Length: 466
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Plastid
EC: 5.4.3.8
|
Q8F4D5 | MKTKELTQSKIEEVSLEILLRHAVKAKHGLEKESMRVNPDGTLSGTTHPIHLGSSLTNHYIKTDFAEPQLEYATHPRPKVEANIRELQDLHIFTIRKLENELIWPFSMPPVLPEEENEIPLGQYGTSHSGRWKTIYRHGLGLRYGRRMQTISGVHYNFSFSKVFLRQFLGKEISNFTKEEISSLYLHVIRNFLRRVHFLTYLTGSSPVFDFTFLPNPGSLKFEKHKNFTLYSTYATSLRMSEIGYTSKVQDTLGIHYNSLEEYVDRMCYAVHTPYPKYVSFSENKDAQLNPNYLQIENEFYSPIRPKQVPKGDERPLDALLQRGIEYIEIRSLDIDPYSPVGVCRSNLAFTQLILLDSLLKVSPSISEEENFSLKENLNSVIWEGRNPELKINVNGSKRNFQEAGAEYSESLRHYAKILDLHTGRRTYQEAIDFQIKKWKNPDKTPSGKLLSEILKRNIEFREKGIELAQENKRMFSYLEYSPGTLMKMEKETIRSFQEKEELEKQEIQTQYPTVKLCNH | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 60577
Sequence Length: 520
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
|
Q9ZNX6 | MTTIFRLASSSSPSLRHDATPHNFHIRKTSISNTFSFSSKNSLSFKRILTSGGSRRFIVAASPPTEDAVVATEPLTKQDLIDYLASGCKTKDKWRIGTEHEKFGFELGSLRPMKYEQISELLNGIAERFDWDKVMEGDNIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGIGFQPKWERKDIPMMPKGRYEIMKKYMPKVGSLGLDMMFRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTDGKPNGFVSMRSHIWTDTDKDRTGMLPFVFDDSFGFEQYVDFALDVPMYFVYRKKKYIDCTGMTFRDFLAGKLPCIPGELPTLNDWENHLTTIFPEVRLKRYLEMRGADGGPWRRLCALPAFWVGILYDEVSLQRVLDMTADWTLEEREMLRNKVTVTGLKTPFRDGLLKHVAEEVLELAKDGLERRGFKESGFLNAVAEVVRTGVTPAERLLELYHGKWEQSVDHVFDELLY | PTM: The Cys-172-Cys-392 disulfide bridge is known to modulate the enzyme activity according to the redox status. The oxidized form constitutes the active enzyme (By similarity).
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 57677
Sequence Length: 508
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
Subcellular Location: Plastid
EC: 6.3.2.2
|
P97494 | MGLLSQGSPLSWEETQRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDHENRKVQLLLNGGDVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTVEANMRKRRKEATSVLGEHQALCTITSFPRLGCPGFTLPEHRPNPEEGGASKSLFFPDEAINKHPRFGTLTRNIRHRRGEKVVINVPIFKDKNTPSPFVETFPEDAEASKASQPDHIYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLEPLKNNRFRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLEEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDIGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVLQGMFYFRKDICKGGNAVVDGCSKAQSSSEPAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEINYSLIWKCNQIADELCECPELLGSGFRKAKYSGGKSDPSA | Function: Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 72571
Sequence Length: 637
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
|
Q8X0X0 | MGLLALGTALDWPDAKQQAHLVRAWGIKQLLEIWNKAKGKERDAMLWGDEIEYLVVNYSKDEPKVLLSLRQADILKALADSKTLKVTGDCAPGTEANADAGNVTLPVFHPEFGRFMLEATPGKPWGIDFKDLLTVEADMKLRRCIAKDHMLSNEHPITLTTFPRIGSPGVFTEPSYPVSGPKLRSQFVPDEIANPHIRFPTLAANIRSRRGRKVQVNVPVFRDENTPWPWKDPTVNYDLHNWPEDDDVRNGAAPDNFIHMDAMAFGMGSCCLQITFQAKNITEGRKMYDQLSPLGPILLALTAATPVYKGFIADTDVRWNQISRAVDDRTPEELGEKPLKNDRWRIPKSRYASNSTYISTDSRLRPEYMDPNLVIDPEIKQQLLDGGMDDRLATHFAHLFIRDPIVIFNEDLQELDLTKTDHFENIQSTNWQHMRFKPPPADNSIGWRVEFRPMEIQITDFENAAFSVFIVLITRAILSFDLNFYIPIVKVDENMETAHARNANLEKKFWFRKNPFPVRTTRRGGSASRSASGTSTPNSGSSRPATPPLGPVEDEYRLMSVNEVINGTAYAKATSKEVTEDAEEGEEFPGLIPLVESYLDSVNMDVATRCGLARYLDLIRKRASGELWTAAKWIREFIAKHPGYKKDSVVSEEITKDLVGAVIEIGEREKRGLGIDDLIGQVPDLEKLFGGFLKGKSPCGGGQAALEQKLKDDDAKVNGVKRKFNEEQ | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 81879
Sequence Length: 728
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
|
Q9NFN6 | MGLLTLGTPLPWNETVPYVDYIKEHGIAQFIALYHRLKGREGDQLKWGDEIEYTIVKFDDDAKRVRVSLRAEELLHQLQAGEELNALLGNENCCLWRPEFASYMIEGTPGAPYGGLLACFNVVESNMISRRAEVTRLLENGESIMSISFPALGTPDFTSPPYEPRPDDINSFGCSLFFPDEVIYGGHPRFRNLVRNIRQRRGEKVAINVPIYKDINTPSPYQEDFTKAKDGGQAARAAKSDHIYMDHMGFGMGCCCLQVTFQAVNIDEARWLYDQLTPITPVLLALSAATPVFRSRLADVDSRWDVISASVDDRTAEERGLVPLKNNKFVLEKSRYDTTDCYIYPCSESYNDIPLQYDDKIYKQLIDGGIDDLLAQHIAHMFIRDPLQVFRERIEQDDTKSTEHFETVQSSNWMNMRFKPPPPDSEIGWRVEFRPSEVQLTDFENAAYCCFVVLLTRVMISFRITLILPISALTENMKRAQRRNAVLEQKLLFRKGIATCNSPPCARGAGCTLESDDVVEMTVNEIINGNGNDFPGLIPLMRQYLDSADVDVDSRCTVSQYLSFIQKRASGELQTLAAWMREFISEHPEYKHDSYVGDRIIYDMLKEMDRISKGEISCPKLLGDYCTKTDSRIPMAVRRAEEKLIVSTKKQS | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 74212
Sequence Length: 652
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
|
Q9HTY6 | MSDLLSRRLALLGAAANLPLLTECLHGIERECLRVDSDGKLALTPHPRALGSTLTHPQITTDYSEALLEFITPTETDVADTLGDLERIHRFASSKLDGEYLWSPSMPCELPDEESIPIARYGSSMIGRLKYVYRKGLALRYGKTMQCIAGIHYNFSLPERLWPLLRQAEGSELSERDYQSAAYIALIRNFRRYSWLLMYLFGASPALDAGFLRGRPSQLERLDEHTLYLPYATSLRMSDLGYQNNAQAGLTPCYNDLQSYIDSLRQAVSTPYPPYEKVGTKQDGEWVQLNTNILQIENEYYSSIRPKRVTYTGERPVQALAARGVQYVEVRCLDINPFLPLGIDLDEARFLDAFLLFCAFSDSPLLNGECSDATDNFLAVVKEGRRPGLQLQRRGQPVELQVWANELLERIADTAALLDRARGGEAHAAALAAQRAKVADAELTPSAQVLKVMRERGESFEAFSLRQSREHAEYFRQHPLAAEEQARFEKMASDSLAEQTELERDQDGDFDTFVAAYQASILGLISN | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 59224
Sequence Length: 527
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
|
Q83AL0 | MNLKVGVLMDPIANIAIHKDTTFAMLLALQARQHEVYYLEPADIFLRNEKILGSMRRLQVADDPSQWFNLSESEIKPLHALDVLLMRKDPPFNMSYVYLTYLLELAEKQGLFVVNKPASLRDANEKLFTGWFPHCTPKTLVTSRKAILQEFIREQKEVVIKPLGAMAGESIFYLTVNDPNIPVVIETMTANGHQLVMAQRFIPEVKSGDKRIILIDGEPIPYTLARIPPKGDFRGNLARGAKGEGRELTDRDRWICEQVGPTLRKKGLWFVGLDIIGDYLTEINVTSPTGVRELQAQFDVDIAGQFIAFLETKYATTTDIE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 36319
Sequence Length: 321
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
|
Q54E83 | MEEKLNDLKEQGIDWAFANGLIMIKKPTEEEAKNNVVNVTHVPFSLYPSKMNKKLFNEACKLAEDYNLLVHNISKDYDFLQNTLKDVFDDFTQMLLNIQRKVVKEGIKQKISLGIFRSDYMFHNKIEGEEERIYQVELNTISSSLAVVSNRVFNLHKYLIGRNDLNDNGYDLLNHPTNQSDKEISDSIALAHKLYNKEKSSVVLMIIQEGERNIYDQKGLEFQLWSNHSIKLIRRTMKEINQCAKLDEENGSVLIVDGMEISVAYYRAGYTPNDYTSSGGDEWKARLLIERSLAIKCPTIAHHLVGVKKIQQVLAQPGVLEKFINNDKESLQRVKRSFTGLYSLSKEDIDMSVVKEAIESPQNYVMKPQREGGGNNIYNDQVAIALKSMSSEELSSYILMDKIMSKSFKTHVVRDRQLLEIEGLYELGIYSVFISNGDDDIVLNKQAGILLRTKTANSDEVGVAAGFGLLDSPILE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 54140
Sequence Length: 476
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
|
P04425 | MIKLGIVMDPIANINIKKDSSFAMLLEAQRRGYELHYMEMGDLYLINGEARAHTRTLNVKQNYEEWFSFVGEQDLPLADLDVILMRKDPPFDTEFIYATYILERAEEKGTLIVNKPQSLRDCNEKLFTAWFSDLTPETLVTRNKAQLKAFWEKHSDIILKPLDGMGGASIFRVKEGDPNLGVIAETLTEHGTRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARIPQGGETRGNLAAGGRGEPRPLTESDWKIARQIGPTLKEKGLIFVGLDIIGDRLTEINVTSPTCIREIEAEFPVSITGMLMDAIEARLQQQ | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 35561
Sequence Length: 316
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
|
Q7NF44 | MKILFIVDPLETLKPGHDTSVALMQAAARRGHSVWAAEVGDLQVHHHRAAAQVRTLTIHPGRTPFYTVEAVGFYPLSEADVIWMRKDPPVTSAYLWATQVLDLVNAGRGDGRTTFVLNRPSGLRNDNEKLYALHFPDLVPETRVCTHRQDILDFVDIHGRAVIKPLDGKGGEGIFLLARADRNLNAIIEASTAYGTRHVMVQRYLEESRQGDKRIVLLAGEPIGALLRVPREDDVRGNMAAGGRVVKTTLTERDREICRVVGPRLVADGHYFVGIDVIGAYLTEINVTSPTGICEIDVLDGVVLEDEIVDWLVEYTRPALARNL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 35906
Sequence Length: 324
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
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P48637 | MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSALLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVFLGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKILSNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFEDISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQLAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSRFVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVVQCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner . Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes . Participates in ophthalmate biosynthesis in hepatocytes (By similarity).
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 52385
Sequence Length: 474
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
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Q9JYJ3 | MMKVLFIADPMASFKTYKDTTYAMMREMAKRGWRLFHTLSGELSVNGGLVTAQASAFEFLGAKNDDDHAWFKSADKVQTALEAFDAVIMRTDPPFDMQYLYATQLLTLAEQQGAKVFNSGQAMRDFNEKLAILNFSRFIAPTLVTTRSADVRTFLKEHGDIIIKPLDGMGGMGIFRLTEKDPNIGSILETLMQLDSRTIMAQRYIPEIVHGDKRILIIGGEVVPYALARIPQNGETRGNLAAGGRGVAQELGGRDREIAETLAPELKRRGILLAGLDVIGSNLTEVNVTSPTGFQEIMKQKGFDVAAMFADAVAAWSVR | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 35146
Sequence Length: 319
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
|
Q7M7H8 | MIKLGIVMDPISSINIKKDTSFAMLLEAQRRSWELHYMEMSDLYLHQGEARARTRLLQVENHPQQWYQFDREQDLALETLDVILMRKDPPFDTEYIYATYILERAEEKGTLIVNKPQSLRDCNEKLFTAWFPELTPDTLVTRNAAHLREFHQKHGDVIFKPLDGMGGASIFRLKKDDPNVGVIIETLTEHGNRFCMAQNFLPAIKEGDKRVLIVDGEPVPYCLARIPAQGETRGNLAAGGRGEARPLSESDWAIARAVAPTLQEKGLIFVGLDIIGDKLTEINVTSPTCAREIEAAFPDISITGMLMNAIEERLEK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 35765
Sequence Length: 316
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
|
Q7TUK9 | MRQLFVLDPLQCIQPAKDSSAALMQAAQRASIEVWACTPADLQARGDQLSAIAVPVVAEPWISTGEPRSLPLTDFACIWMRKDPPVDEGYLYATHLLELAERAGVCVLNRPAALRAWNEKLGALRFNNLMAPTLVASRVSELAAFAREQEEVVLKPLGGRAGQGLVRVAGAAPGLEALLELVTDQEQLPVMVQRFLPAVIEGDKRILLVDGEPLGAVNRRPKAGDFRSNLAMGGRPEPTELDSRELQICAELAPVLREQGLFFVGIDVIDGLLSEINVTSPTGIREVERLKGVPLADQVIARLLVSLG | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Mass (Da): 33316
Sequence Length: 308
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
|
P41441 | MNYRYRAMTQDGQKLQGIIDANDERQARLRLREEGLFLLDIRPQKSSGVKTRRPRISHSELTLFTRQLATLSAAALPLEESLAVIGQQSSNKRLGDVLNQVRSAILEGHPLSDALQHFPTLFDSLYRTLVKAGEKSGLLAPVLEKLADYNENRQKIRSKLIQSLIYPCMLTTVAIGVVIILLTAVVPKITEQFVHMKQQLPLSTRILLGLSDTLQRTGPTLLATVFIVAVGFWLWLKRGNNRHRFHAMLLRVALIGPLICAINSARYLRTLSILQSSGVPLLDGMNLSTESLNNLEIRQRLANAAENVRQGNSIHLSLEQTAIFPPMMLYMVASGEKSGQLGTLMVRAADNQETLQQNRIALTLSIFEPALIITMALIVLFIVVSVLQPLLQLNSMIN | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44339
Sequence Length: 398
Subcellular Location: Cell inner membrane
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P15745 | MALFRYQALDEQGKPRRGVQQADSARHARQLLREKGWLALDIDPAAGGGRPSRFMRRTSARDLALVTRQLATLVAAAIPLEKALDAVAQQSEKPQLKTLIAGVRGKVLEGHSLAEAMRGHPGCFDALYCAMVAAGEASGHRLLQAMIYPIVLTLVAVSVIVILLSTVVPKVVEQFIHLKQALPFSTRLLMAMSDMLRAAGPWLLLAILLLILLLRYLLRQPAKRLAWHRLLLRLPLIGRVARSVNSARYARTLSILNASAVPLLLAMRISADVLSNAWAKRQLEAASDAVREGVSLHRALEMTQLFPPMMRYMVASGERSGELNSMLERAADNQDRDLSAQIQLALSLFEPLLVVAMAGMVLFIVLAILQPILQLNTLMSM | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41873
Sequence Length: 381
Subcellular Location: Cell inner membrane
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P31705 | MAQYHYQALDAQGKKCRGTQEADSARQARQLLRERGLVPLSVDENRGDQQKSGSTGLSLRRKIRLSTSDLALLTRQLATLVAASMPLEEALDAVAKQSEKPHLSQLMAAVRSKVMEGHSLADAMKCFPGSFERLYCAMVAAGETSGHLDAVLNRLADYTEQRQQMRSRIQQAMIYPCVLTVVAIAVVSILLSVVVPKVVEQFIHMKQALPLSTRVLMGMSDAVRTFGPWMLLALLAGFMAFRVMLRQEKRRVSFHRRLLHLPLIGRIARGLNTARYARTLSILNASAVPLLQAMRISGDVMSNDYARHRLSLATDAVREGVSLHKALEQTALFPPMMRHMIASGERSGELDSMLERAADNQDREFSSQMTLALGLFEPLLVVSMAAVVLFIVLAILQPILQLNTLMSS | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45162
Sequence Length: 408
Subcellular Location: Cell inner membrane
|
Q00513 | MAAFEYLALDPSGRQQKGVLEADSARQVRQLLRERQLAPLDVKPTRTREQSGQGGRLTFARGLSARDLALVTRQLATLVQAALPIEEALRAAAAQSTSQRIQSMLLAVRAKVLEGHSLAGSLREFPTAFPELYRATVAAGEHAGHLGPVLEQLADYTEQRQQSRQKIQLALLYPVILMVASLAIVGFLLGYVVPDVVRVFIDSGQTLPLLTRVLIGVSDWVKAWGALAFVAAIGGVIGFRYALRKDAFRERWHGFLLRVPLVGRLVRSTDTARFASTLAILTRSGVPLVEALAIAAEVIANRIIRNEVVKAAQKVREGASLTRSLEATGQFPPMMLHMIASGERSGELDQMLARTARNQENDLAAQIGLMVGLFEPFMLIFMGAVVLVIVLAILLPILSLNQLVG | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44062
Sequence Length: 405
Subcellular Location: Cell inner membrane
|
P45780 | MAAFEYKALDAKGRHKKGVIEGDNARQVRQRLKEQSLVPMEVVETQVKAARSRSQGFAFKRGISTPDLALITRQLATLVQSGMPLEECLRAVAEQSEKPRIRTMLVAVRAKVTEGYTLSDSLGDYPHVFDELFRSMVAAGEKSGHLDSVLERLADYAENRQKMRSKLQQAMIYPVVLVVFAVGIVAFLLAAVVPKIVGQFVQMGQALPASTQFLLDASDFLQHWGISLLVGLLMLIYLVRWLLTKPDIRLRWDRRVISLPVIGKIARGLNTARFARTLSICTSSAIPILDGMRVAVDVMTNQFVKQQVLAAAENVREGSSLRKALEQTKLFPPMMLHMIASGEQSGELEGMLTRAADNQDNSFESTVNIALGIFTPALIALMAGMVLFIVMATLMPILEMNNLMSR | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44931
Sequence Length: 406
Subcellular Location: Cell inner membrane
|
P31744 | MPLYRYKALDAHGEMLDGQMEAANDAEVALRLQEQGHLPVETRLATGENGSPSLRMLLRKKPFDNAALVQFTQQLATLIGAGQPLDRALSILMDLPEDDKSRRVIADIRDTVRGGAPLSVALERQHGLFSKLYINMVRAGEAGGSMQDTLQRLADYLERSRALKGKVINALIYPAILLAVVGCALLFLLGYVVPQFAQMYESLDVALPWFTQAVLSVGLLVRDWWLVLVVIPGVLGLWLDRKRRNAAFRAALDAWLLRQKVIGSLIARLETARLTRTLGTLLRNGVPLLAAIGIARNVMSNTALVEDVAAAADDVKNGHGLSMSLARGKRFPRLALQMIQVGEESGALDTMLLKTADTFELETAQAIDRALAALVPLITLVLASVVGLVIISVLVPLYDLTNAIG | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44024
Sequence Length: 405
Subcellular Location: Cell inner membrane
|
P31733 | MQKRRQSGFTLLEVMVVIVILGILASLVVPNLMGNKEKADQQKAVSDIVALENALDMYKLDNNRYPTTEQGLDALVNKPTAAPEPRSYRDGGYIKRLPQDPWGNPYQMLSPGQFGKIDIFSMGLDGEAGTDDDIGNWNLKDFQ | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth.
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15902
Sequence Length: 143
Subcellular Location: Cell inner membrane
|
P31585 | MERRQRGFTLLEIMVVIVILGVLASLVVPNLMGNKEKADKQKAVSDIVALESQLDMYKLDNSRYPTTEQGLGALVKKPTTPPEPRNYPQDGYIRRLPQDPWGAEYQLVSPGRHGKIDVFSYGPDGMPDTDDDIGNWNVGNGAHNNGGNGNGNP | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth.
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16789
Sequence Length: 153
Subcellular Location: Cell inner membrane
|
A0A0H3HDD6 | MRRQSQRGFTLLEIMVVIVIMGILASLVVPNLMGNKDKADRQKVVSDIVALESALDMYKLDNSRYPTTEQGLQALITKPSVPPEARYYPQDGYIRRLPQDPWGGDYQLVSPGQHGQIDIFSSGQDGVPGTDDDIGNWTLSKK | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm . Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth .
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15792
Sequence Length: 142
Subcellular Location: Cell inner membrane
|
P31586 | MQQSQRGCGQNSYGQSGYRQRGFTLLEIMVVIVILGVLASLVVPNLMGNKEKADRQKAVSDIVSLESALDMYKLDNNRYPSTEQGLKALVTKPTVQPEPRNYPADGYIRRLPQDPWGTDYQLLNPGQHGKLDIFSLGPDGMPGTEDDIGNWNLDKK | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth.
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17352
Sequence Length: 156
Subcellular Location: Cell inner membrane
|
Q00514 | MQRRQQSGFTLIEIMVVVVILGILAALVVPQVMSRPDQAKVTVAKGDIKAIAAALDMYKLDNFAYPSTQQGLEALVKKPTGNPQPKNWNKDGYLKKLPVDPWGNPYQYLAPGTKGPFDLYSLGADGKEGGSDNDADIGNWDN | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm . Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth . Type II pseudopilus confers increased bacterial adhesive capabilities .
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15449
Sequence Length: 142
Subcellular Location: Cell inner membrane
|
P45773 | MKKMRKQTGFTLLEVMVVVVILGILASFVVPNLLGNKEKADQQKAVTDIVALENALDMYKLDNSVYPTTDQGLEALVTKPTNPEPRNYREGGYIKRLPKDPWGNDYQYLSPGDKGTIDVFTLGADGQEGGEGTGADIGNWNIQDFQ | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm . Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth (By similarity).
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16080
Sequence Length: 146
Subcellular Location: Cell inner membrane
|
P31734 | MIKRSITRSPSRAGQAGMSLLEIIIVIVLIGAVLTLVGSRVLGGADRGKANLAKSQIQTLAGKIENFQLDTGKLPSKLDDLVTQPGGSSGWLGPYAKPVELNDPWGHTIEYRVPGDGQAFDLISLGKDGRPGGSSYDSDIKYQ | Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm . Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus . Further polymerization triggers pseudopilus growth .
PTM: Cleaved by the prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15148
Sequence Length: 143
Subcellular Location: Cell inner membrane
|
P31735 | MRRHRQSGFTLLEVLLVAMLMGLVATAVTLSMGGARGDRELDKQARRFMATLQQAQEYSVMDGRLVGLRIEDHGWQFMQRAAKDRKWQALTGDKILGQVQLPDTMLLAIELEGFSWRTESDEKTERGRDEKERTPQVLIFPGGELSPFVLTLTQQDEDVRYLRTVKADEFGRLRLLQDEEEEE | Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
PTM: Cleaved by prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21070
Sequence Length: 183
Subcellular Location: Cell inner membrane
|
P24687 | MRQRGFTLLEIMLVVLLAGVAATLVMMAIPAPKQQDSGWQIARFKAQLQYAVEDSQMNDHILGIYIQPHRWQYALLQRQVVENSPEEQQRLRYVWIPWQPYRMSVPSELPDSFHIELSTQVGAAGDGTGFSPGNGDPHVLILPGGEVTPFRLTLRNGNDSAWLQVDTNGQVHTSPEAEQKG | Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
PTM: Cleaved by prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20288
Sequence Length: 181
Subcellular Location: Cell inner membrane
|
P41443 | MNQQRGFTLLEMMLVLALVAITASVVLFTYGREDVASTRARETAARFTAALELAIDRATLSGQPVGIHFSDSAWRIMVPGKTPSAWRWVPLQEDAADESQNDWDEELSIHLQPFKPDDSNQPQVVILADGQITPFSLLMANAGTGEPLLTLVCSGSWPLDQTLARDTRP | Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
PTM: Cleaved by prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18565
Sequence Length: 169
Subcellular Location: Cell inner membrane
|
A0A0H3H546 | MRQRGFTVLEMMLVVLLMGSAASLVIMSFPAMQQDTAERQLQRFQAQLEFAMDSGMQNDRLLGIQIRPNGWQFQVLQSQAAETRSSVAHSDRWQGYVWQIWQPRQAALGGQVPDNQPLTLRLPPPQEWPPTAEPAADPDILLLPGGEITPFTLIFGEKDDRSEVWLRVDESGAIATSAKGGAP | Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm . Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates (By similarity).
PTM: Cleaved by prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20341
Sequence Length: 183
Subcellular Location: Cell inner membrane
|
P15747 | MRQRGFTLLEMMLILLLMGVSAGMVLLAFPASRDDSAAQTLARFEAQLRFVQQRGLQTGQFFGVSVHPDRWQFLVLEARDGADPAPADDGWSGYRWLPLRAGRVATSGSIAGGKLNLAFAQGEAWTPGDNPDVLIFPGGEMTPFRLTLGEAPGIAFNARGESLPEPQEAQ | Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
PTM: Cleaved by prepilin peptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18403
Sequence Length: 170
Subcellular Location: Cell inner membrane
|
Q96324 | MVVKVYGQIKAANPQRVLLCFLEKDIEFEVIHVDLDKLEQKKPQHLLRQPFGQVPAIEDGYLKLFESRAIARYYATKYADQGTDLLGKTLEGRAIVDQWVEVENNYFYAVALPLVMNVVFKPKSGKPCDVALVEELKVKFDKVLDVYENRLATNRYLGGDEFTLADLSHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMELAAY | Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 24637
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9FE46 | MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFADQGTNLLGKSLEHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTHMPAMGYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVLAGH | Function: Involved in the transport and/or accumulation of both anthocyanins and proanthocyanidins (PA)s in the vacuole. Functions in the cytosol to maintain the regular accumulation in the vacuole of PA precursors, such as epicatechin and glycosylated epicatechin.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 24581
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9LZI9 | MAMKLYGDEMSACVARVLLCLHEKNTEFELVPVNLFACHHKLPSFLSMNPFGKVPALQDDDLTLFESRAITAYIAEKHRDKGTDLTRHEDPKEAAIVKLWSEVEAHHFNPAISAVIHQLIVVPLQGESPNAAIVEENLENLGKILDVYEERLGKTKYLAGDTYTLADLHHVPYTYYFMKTIHAGLINDRPNVKAWWEDLCSRPAFLKVSPGLTVAPTTN | Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 24652
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9C6C8 | MADSKMKLHCGFIWGNSAALFCINEKGLDFELVFVDWLAGEAKTKTFLSTLNPFGEVPVLEDGDLKLFEPKAITRYLAEQYKDVGTNLLPDDPKKRAIMSMWMEVDSNQFLPIASTLIKELIINPYQGLATDDTAVQENKEKLSEVLNIYETRLGESPYLAGESFSLADLHHLAPIDYLLNTDEEELKNLIYSRPNVAAWVEKMKMRPAWLKTVVMKNHIVDLMKQRRLPIKLDSSCHESTVVAQKNAIAIENK | Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 28819
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
P48438 | XVAFETVPVDLMKGEHKQPAYLALQPFGTVPAVVDGDYXLLSAVLDVYEAHLHGYLAGDFVSLADLAHLPFTDYLV | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 8268
Sequence Length: 76
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q04522 | MTIKVHGNPRSTATQRVLVALYEKHLEFEFVPIDMGAGGHKQPSYLALNPFGQVPALEDGEIKLFESRAITKYLAYTHDHQNEGTSLIHKEKHEMAAQLVWEEVEAHQFDPVASKLAWELVFKGIFGMQTDTTVVEENEAKLAKVLDVYEARLTESEYLGANDSFTLVDLHHLPLLGYLMGTQVKKLFEERAHVSAWCKKILARPSWEKTLALQKQA | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 24599
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q06718 | MIQFVIPSYQRVGAVSALDMFPTDYEPHIVVREHEEKAYNDAYGSRAKIITIPDGVNGIAGTRKAITDMYAGQRIWMIDDDTTIRMSSMRKRDDRRCVDKVNQLTHEQFYELIQYVEDAMDCGYYHGHARLPIFKITSSWGNYRENSYGFTNTWYDLGKLTTEQIGYGKIDLCEDMYAFLNLINQGYPHLALFKYLVVSGKAQAPGGCSSIRSNSKHNRALEQINREFPEQARWKTSNIEKRKSLGEEDEPLKVLRMCVSRKEKSEAFHKFNAIHPIAVD | Function: Transfers a gentiobiosyl-group on a hydroxymethylcytosine residue in DNA. Is involved in a DNA modification process to protects the phage genome against its own nucleases and the host restriction endonuclease system.
Sequence Mass (Da): 32300
Sequence Length: 280
Pathway: Genetic information processing; DNA modification.
EC: 2.4.1.-
|
Q9Y2Q3 | MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL | Function: Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds . Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB) .
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25497
Sequence Length: 226
Subcellular Location: Peroxisome
EC: 2.5.1.18
|
P24473 | MGPAPRVLELFYDVLSPYSWLGFEVLCRYQHLWNIKLKLRPALLAGIMKDSGNQPPAMVPHKGQYILKEIPLLKQLFQVPMSVPKDFFGEHVKKGTVNAMRFLTAVSMEQPEMLEKVSRELWMRIWSRDEDITESQNILSAAEKAGMATAQAQHLLNKISTELVKSKLRETTGAACKYGAFGLPTTVAHVDGKTYMLFGSDRMELLAYLLGEKWMGPVPPTLNARL | Function: Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25493
Sequence Length: 226
Subcellular Location: Mitochondrion matrix
EC: 2.5.1.18
|
Q18973 | MPNRKVVKFFFDVISPYSYFGFEGITRHRSVWKTPIQMKPFFFAGVVRHTENPGLPLRIPIKEKYMHKDLLFSAQYWGIPFRLPKDYTNMMLNTSSIVPQRILVASQLRDNVLMEDVARGLWHRFYAYGKPIFTKSQVAEVLRDLHVKDVDELVMMSDSAEVKNILRENTDEAIGNGCFGAPWMHITDGHGKVLQTVFGSDRLPQVADFLAEPFKGPMREKKPNA | Function: Has roles in respiratory and lipid metabolism.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25951
Sequence Length: 225
Subcellular Location: Mitochondrion
EC: 2.5.1.18
|
Q6NLB0 | MALSPPKIFVEDRQVPLDATSDPPALFDGTTRLYISYTCPFAQRVWITRNLKGLQDEIKLVPIDLPNRPAWLKEKVNPANKVPALEHNGKITGESLDLIKYVDSNFDGPSLYPEDSAKREFGEELLKYVDETFVKTVFGSFKGDPVKETASAFDHVENALKKFDDGPFFLGELSLVDIAYIPFIERFQVFLDEVFKYEIIIGRPNLAAWIEQMNKMVAYTQTKTDSEYVVNYFKRFM | Function: Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin. In vitro, possesses glutathione-dependent thiol transferase activity toward 2-hydroxyethyl disulfide (HED).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 27167
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9M2W2 | MSVGLKVSAFLHPTLALSSRDVSLSSSSSSLYLDRKILRPGSGRRWCKSRRTEPILAVVESSRVPELDSSSEPVQVFDGSTRLYISYTCPFAQRAWIARNYKGLQNKIELVPIDLKNRPAWYKEKVYSANKVPALEHNNRVLGESLDLIKYIDTNFEGPSLTPDGLEKQVVADELLSYTDSFSKAVRSTLNGTDTNAADVAFDYIEQALSKFNEGPFFLGQFSLVDVAYAPFIERFRLILSDVMNVDITSGRPNLALWIQEMNKIEAYTETRQDPQELVERYKRRVQAEARL | Function: Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin. In vitro, possesses glutathione-dependent thiol transferase activity toward 2-hydroxyethyl disulfide (HED).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 33058
Sequence Length: 292
Subcellular Location: Plastid
EC: 2.5.1.18
|
Q9LZ06 | MAPSFIFVEDRPAPLDATSDPPSLFDGTTRLYTSYVCPFAQRVWITRNFKGLQEKIKLVPLDLGNRPAWYKEKVYPENKVPALEHNGKIIGESLDLIKYLDNTFEGPSLYPEDHAKREFGDELLKYTDTFVKTMYVSLKGDPSKETAPVLDYLENALYKFDDGPFFLGQLSLVDIAYIPFIERFQTVLNELFKCDITAERPKLSAWIEEINKSDGYAQTKMDPKEIVEVFKKKFM | Function: Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 27090
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q8IYK4 | MAARPAATLAWSLLLLSSALLREGCRARFVAERDSEDDGEEPVVFPESPLQSPTVLVAVLARNAAHTLPHFLGCLERLDYPKSRMAIWAATDHNVDNTTEIFREWLKNVQRLYHYVEWRPMDEPESYPDEIGPKHWPTSRFAHVMKLRQAALRTAREKWSDYILFIDVDNFLTNPQTLNLLIAENKTIVAPMLESRGLYSNFWCGITPKGFYKRTPDYVQIREWKRTGCFPVPMVHSTFLIDLRKEASDKLTFYPPHQDYTWTFDDIIVFAFSSRQAGIQMYLCNREHYGYLPIPLKPHQTLQEDIENLIHVQIEAMIDRPPMEPSQYVSVVPKYPDKMGFDEIFMINLKRRKDRRDRMLRTLYEQEIEVKIVEAVDGKALNTSQLKALNIEMLPGYRDPYSSRPLTRGEIGCFLSHYSVWKEVIDRELEKTLVIEDDVRFEHQFKKKLMKLMDNIDQAQLDWELIYIGRKRMQVKEPEKAVPNVANLVEADYSYWTLGYVISLEGAQKLVGANPFGKMLPVDEFLPVMYNKHPVAEYKEYYESRDLKAFSAEPLLIYPTHYTGQPGYLSDTETSTIWDNETVATDWDRTHAWKSRKQSRIYSNAKNTEALPPPTSLDTVPSRDEL | Function: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of collagen.
Catalytic Activity: (5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP
Sequence Mass (Da): 72924
Sequence Length: 626
Subcellular Location: Endoplasmic reticulum lumen
EC: 2.4.1.50
|
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