ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q52309 | MKYKVLTLCLSAALFAPIAPTMASTDNQADMVLDQVLVLSRHNLRTPIVNTGILTEVTDKKWPDWDAKSGYLTTQGGALEVYMGHYFREWIDQNKLLADELCPTSNEDIYLYTNSLQRTIATAQFFAAGAFPGCKVNIHHQPEIGKMDPVFNPIITNGSPEFKQKALAAMDDYLKGLSLKAGYEELDTVLNIKDSQKCKTDKLCNLDSQKNSFIIEADKEPGVSGPLKIANSAVDAIDLQYYEGFPADQVAWGLVDTPEKWKKLNTLKNAYQETLFTPKIIAKNVAHPILNYIDKGFVSVDKGETAKFIFLVGHDSNIAS... | Catalytic Activity: alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate
Sequence Mass (Da): 46941
Sequence Length: 417
Subcellular Location: Periplasm
EC: 3.1.3.10
|
A0A5Q0QNJ2 | MVWDFVLSLFHSLLAAFQTLTSWLTGSFLFNNKMAPAPNPAPVTFILPDLEKTFNSLPDDGLNPHHDVACAESREWFAKYNKKVLGAQMQEFFRRCKFELITSYTYPYVDKEGLRATMDWHNILWFFDEVTDTETGKDAHKSAIITIRTLREPDFDDGSSLCRMVRDFRLSHLSRAGPECTRRFLEHCDVAFHAGAVEAELREKGEVLSIEGYLKLRRETSGARTCFDMAEYLMDIDLPQDMYDDPVFQKGYIAALDLIFLANDLYSYNMEQAKGHNGANVLTVVMKETKLNLQSAADYVGVLCEKLIKQFQEAKSTLEN... | Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to viridiflorene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene
Sequence Mass (Da): 44434
Sequence Length: 389
Domain: The DDXXD motif is important for the catalytic activity, presumably through bindi... |
A0A5Q0QU70 | MNASPFLNESSPTRPTSFVLPDLVSHCKFPLSYHPNGDEIAQESVDWLDSSCPDLTAKQRRALRVLQSGELTAYCYNQATSPERLRVVSDFLTYLFHLDNISDGMMTRETDVLADVVMNAFWFTDKYMPTRGPGKEQLDEELNPGKLARDFWSRAIADCGVGVQARFKETMGLFFEAVNIQARMRDEDTIPDLESYIDVRRDTSGCKPSWVLIEYALGIDLPDHVVDHPIMQALNQGTNDLVTWSNDIFSYNVEQSRGDTHNMIVILMEYHGHTLQSAVDYVGELCAQTIDTFCENKERLPSWGPEIDDMVARYVKGLQD... | Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-muurolene, gamma-muurolene, germacrene, delta-cadinene, delta-cadinol and cubenol.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate
Sequence Mass (Da): 40819
... |
Q8K209 | MAVQVLRQMVYFLLSLFSLVQGAHSGSPREDFRFCGQRNQTQQSTLHYDQSSEPHIFVWNTEETLTIRAPFLAAPDIPRFFPEPRGLYHFCLYWSRHTGRLHLRYGKHDYLLSSQASRLLCFQKQEQSLKQGAPLIATSVSSWQIPQNTSLPGAPSFIFSFHNAPHKVSHNASVDMCDLKKELQQLSRYLQHPQKAAKRPTAAFISQQLQSLESKLTSVSFLGDTLSFEEDRVNATVWKLPPTAGLEDLHIHSQKEEEQSEVQAYSLLLPRAVFQQTRGRRRDDAKRLLVVDFSSQALFQDKNSSQVLGEKVLGIVVQNT... | Function: Receptor involved in cell adhesion and probably in cell-cell interactions. Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial base... |
Q8IZP9 | MVFSVRQCGHVGRTEEVLLTFKIFLVIICLHVVLVTSLEEDTDNSSLSPPPAKLSVVSFAPSSNGTPEVETTSLNDVTLSLLPSNETEKTKITIVKTFNASGVKPQRNICNLSSICNDSAFFRGEIMFQYDKESTVPQNQHITNGTLTGVLSLSELKRSELNKTLQTLSETYFIMCATAEAQSTLNCTFTIKLNNTMNACAVIAALERVKIRPMEHCCCSVRIPCPSSPEELEKLQCDLQDPIVCLADHPRGPPFSSSQSIPVVPRATVLSQVPKATSFAEPPDYSPVTHNVPSPIGEIQPLSPQPSAPIASSPAIDMPP... | Function: Orphan receptor. Could be involved in a signal transduction pathway controlling epididymal function and male fertility. May regulate fluid exchange within epididymis.
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit.
Location Topology: Multi-pass membran... |
Q8CJ12 | MLFSGGQYSPVGRPEEVLLIYKIFLVIICFHVILVTSLKENGNSSLLSPSAESSLVSLIPYSNGTPDAASEVLSTLNKTEKSKITIVKTFNASGVKSQRNICNLSSLCNDSVFFRGEIVFQHDEDHNVTQNQDTANGTFAGVLSLSELKRSELNKTLQTLSETYFIVCATAEAQSTVNCTFTVKLNETMNVCAMMVTFQTVQIRPMEQCCCSPRTPCPSSPEELEKLQCELQDPIVCLADQPHGPPLSSSSKPVVPQATIISHVASDFSLAEPLDHALMTPSTPSLTQESNLPSPQPTIPLASSPATDLPVQSVVVSSLP... | Function: Orphan receptor. Could be involved in a signal transduction pathway controlling epididymal function and male fertility. May regulate fluid exchange within epididymis.
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit.
Location Topology: Multi-pass membran... |
Q86Y34 | MATPRGLGALLLLLLLPTSGQEKPTEGPRNTCLGSNNMYDIFNLNDKALCFTKCRQSGSDSCNVENLQRYWLNYEAHLMKEGLTQKVNTPFLKALVQNLSTNTAEDFYFSLEPSQVPRQVMKDEDKPPDRVRLPKSLFRSLPGNRSVVRLAVTILDIGPGTLFKGPRLGLGDGSGVLNNRLVGLSVGQMHVTKLAEPLEIVFSHQRPPPNMTLTCVFWDVTKGTTGDWSSEGCSTEVRPEGTVCCCDHLTFFALLLRPTLDQSTVHILTRISQAGCGVSMIFLAFTIILYAFLRLSRERFKSEDAPKIHVALGGSLFLLN... | Function: Orphan receptor that regulates migration of lymphatic endothelial cells in vitro via the small GTPases RhoA and CDC42 . Regulates B-cell development (By similarity). Seems to signal through G-alpha(q)-proteins .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60861
Sequence Length: 549
Subc... |
Q8R0T6 | MATARSLGLLFFLLLTSDEETTEEPRNVCRRLQEGHEYDTFDLNDTAQCFTKCGQSEHSPCDVGNLQRYWLNYESYLLENSMETVDMPFVKALIQNISTDVSEDLLYSLMLSQIPRQVMQGEDEPADGVRLPKSLFGALPGNRSAVRLAITVLDIGAGNVFKGPKLLEDKGSSVLNNRMVGLSVGQMHATGLSEPVEITFSHERQPPNVILTCVFWDMAKGDWDSHGCSTVPGDGRTVCRCDHLTFFALLLRPILDLATAQTLTRISQAGSAVSMIFLAFTMVLYVAFRFSLQRFKSEDAPKIHMALSISLFLLNLTFLI... | Function: Orphan receptor that regulates migration of lymphatic endothelial cells via the small GTPases RhoA and CDC42 (By similarity). Regulates B-cell development . Seems to signal through G-alpha(q)-proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60072
Sequence Length: 54... |
Q8IZF4 | MDHCGALFLCLCLLTLQNATTETWEELLSYMENMQVSRGRSSVFSSRQLHQLEQMLLNTSFPGYNLTLQTPTIQSLAFKLSCDFSGLSLTSATLKRVPQAGGQHARGQHAMQFPAELTRDACKTRPRELRLICIYFSNTHFFKDENNSSLLNNYVLGAQLSHGHVNNLRDPVNISFWHNQSLEGYTLTCVFWKEGARKQPWGGWSPEGCRTEQPSHSQVLCRCNHLTYFAVLMQLSPALVPAELLAPLTYISLVGCSISIVASLITVLLHFHFRKQSDSLTRIHMNLHASVLLLNIAFLLSPAFAMSPVPGSACTALAAA... | Function: Adhesion G protein-coupled receptor (GPCR). Transduces intracellular signals through coupling to guanine nucleotide-binding protein G(s) subunit alpha and activation of adenylate cyclase pathway. Isoform 1, but not isoform 2, is constitutively active, as evidenced by elevated basal cAMP levels, and responds t... |
Q3V3Z3 | MDPHGALFFYLCLLAAQVVLVETLSDLLVLMKRLEQPVGRGLSSRARHIHSLEQKLLNASFGGHNLTLQTNSIQSLVFKLSCDFPGLSLSSTTLTNVSQVRAPHAMQFPAELTKGACVTSRPAELRLICIYFFTAHLFQDDRNSSLLNNYVLGAQLDHRPVNNLQKPVNISFWHNRSLEGYTVSCVFWKEGASKSSWGAWSPEGCYTEQPSATQVLCHCNHLTYFAVLMQLSGDPVPAELQVPLEYISFVGCSISIVASLLTILLYAQSRKQSDSTTRIHMNLNGSVLLLNVTFLLSSQMTLPTMPRPVCKVLAAVLHYA... | Function: Adhesion G protein-coupled receptor (GPCR). Transduces intracellular signals through coupling to guanine nucleotide-binding protein G(s) subunit alpha and activation of adenylate cyclase pathway . Isoform 1, but not isoform 2, is constitutively active, as evidenced by elevated basal cAMP levels, and responds ... |
Q96K78 | MASCRAWNLRVLVAVVCGLLTGIILGLGIWRIVIRIQRGKSTSSSSTPTEFCRNGGTWENGRCICTEEWKGLRCTIANFCENSTYMGFTFARIPVGRYGPSLQTCGKDTPNAGNPMAVRLCSLSLYGEIELQKVTIGNCNENLETLEKQVKDVTAPLNNISSEVQILTSDANKLTAENITSATRVVGQIFNTSRNASPEAKKVAIVTVSQLLDASEDAFQRVAATANDDALTTLIEQMETYSLSLGNQSVVEPNIAIQSANFSSENAVGPSNVRFSVQKGASSSLVSSSTFIHTNVDGLNPDAQTELQVLLNMTKNYTKT... | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88909
Sequence Length: 797
Subcellular Location: Membrane
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Q8BM96 | MRSCRSCNVRVLVAIVCGLLTGIVLGLGIWRMVIRINRGIFVPVPSIPVQFCRNGGTWQNGRCICTEEWKGLRCTIANFCENSTDGEFTFGSIPVGRYGPSLQTCEPGTLNAGSPKATRLCNVSEFGNIELQNVTKGSCNINLQTLEIQINNQTASAENISREAQVLTADASKLTAQNITSATTVVGQIFGKANNESQAKKTAIATVSQILDASEDVFQKAAEMDNSKSFSNLIKQMENYSYSQGDQTVVEPNIAIQSVTRDDNSGPSVLFSVQKGSSNSLVSGRILINKTANGLNPDGQTELQILLNTGENRKSCGFMV... | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87684
Sequence Length: 785
Subcellular Location: Membrane
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Q7AKI6 | MSLDSLKSAVPDYAKDLKLNLGSVIGNSDLPAQQLWGTVLATAIASRSPIVLRELEPEAKANLSPEAYSAAKSAAAVMAMNNVFYRTRHLLSDHEYGTLRAGLRMNVIGNPGVDKVDFELWSFAVSAINGCGMCLDSHEQVLRKAGVDRETIQEAFKIAAVVEAVGVTLDAEAVLAAE | Function: Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-ca... |
P65689 | MLNVGATAPDFTLRDQNQQLVTLRGYRGAKNVLLVFFPLAFTGICQGELDQLRDHLPEFENDDSAALAISVGPPPTHKIWATQSGFTFPLLSDFWPHGAVSQAYGVFNEQAGIANRGTFVVDRSGIIRFAEMKQPGEVRDQRLWTDALAALTA | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May represent an important antioxidant defense against cytotoxic peroxides, especially ... |
P82955 | MLDQNIXTQLXAYLER | Cofactor: Binds 1 FAD per subunit.
Function: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein (By similarity).
Sequence Mass (Da): 1931
Sequence Lengt... |
P35340 | MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSDKVTFKEDNSLPVRKPSFLITNPGSNQGPRFAGSPLGHEFTSLVLALLWTGGHPSKEAQSLLEQIRHIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQNEITDRNVMGVPAVFVNGKEFGQGRMTLTEIVAKIDTGAEKRAAEELNKRDAYDVLIVGSGPAGAAAAIYSARKGIRTGLMGERFGGQILDTVDIENYISVPKTEGQKLAGALKVHVDEYDVDVIDSQSASKLIPAAVEGGLHQIETASGAVLKARSIIV... | Cofactor: Binds 1 FAD per subunit.
Function: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.
Sequence Mass (Da): 56177
Sequence Length: 521
EC: 1.8.... |
Q9I6Z2 | MLDANLKTQLKAYLEKVSQPFEIVASLDDSDKSRELLGLLQDIVGLTDKITLKTDGSDARKPSFSLNRPGADIGLRFAGIPMGHEFTSLVLALLQVGGHPSKLDADVIEQVKGIEGTFEFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALFQDEVEARQIMSVPSIYLNGEVFGQGRMGVEEILAKIDTGAAARDAEKLTARDAFDVLVVGGGPAGAAAAIYAARKGIRTGVAAERFGGQVLDTMAIENFISVQETEGPKLARALEEHVRHYEVDIMNLQRASKLVPAKNAGELHEVRFESGGSLKAKTLILA... | Cofactor: Binds 1 FAD per subunit.
Function: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein (By similarity).
Sequence Mass (Da): 55836
Sequence Leng... |
C5M5S1 | MNTISPVVIEPRHGGEHHSVNVKYGIIIFAISVIHILFFLLVKFIEINRWKSNGRFNKSLWKLNNTPTWMLITLWILIIFFIGGANITEFSEEYITIAKRYGRIAYCLLPLNIYLILRPTNCVYLKPGYYLENLSLHKWLSRLISICTLIHAIGYFYKWNKEGKILIKSFRFLNFLGIVVFVMFAVLIIVSIRILRRKYYSLFYIIHNITAWSMVVLIIFHARPGVTIFGIICLILMCYQLLYLRFYKSYPVNNLKIVDIPMSTLQIIKIPKPSNFPTWLPGSHVRLNYTTSNIKSWINSSHPFTIANIPEDGVNYLSLV... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63696
Sequence Length: 551
Subcellular Location: Membrane
EC: 1.16.1.-
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C4Y9R6 | MTTSKIGVRHAGHGHTVNIKYGYIIFGVSVLYALLLASAHFLELRQWRRQKRPSRSSVWARINNAPFWVHTLLWAAIVVGLAFTNVHDLSQNWTVVVKRLGRLAFCLVPLDLALALRPCLLGQSYLELMPLHKWLSRLIILAGVVHGIGFFVKWTIHHQLGKAKRWANLAGIIVALFSVLLVIVSSRPVRRRFYSYFYAFHNFTVALFVLLMIWHARPGVSDFVLLSVALLLFQGASRVYNGYSVPGLTIVDADAASLRLLRLQKPNSFPSVWQPGSHIRVGLPLSSWQSWVFPAHLYTLCSSPANDTLNLVVKKGRRFE... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57083
Sequence Length: 513
Subcellular Location: Membrane
EC: 1.16.1.-
|
Q6BM09 | MNELESFSPRHEGHHHAANIKYGYIVLGFSVVHIIGILICKSVFKLRWTTSTKGIDFVKSPLFISIIAWTLILIGLGVFHVQLPENYVTSIKRFGRMSYALLPFDIFLVLRPNSIGLRYLELMDLHKWMSRVIIAGAIIHGVGYFIKWILEGSLFTKSVRLWNFLGIVVFMLNLILIIISLRYFRRRIYQYFYVVHNITVWLFVGLICLHARPGVGKYAIACASLLGLQIFERYAKSHSISDLKVISYEGSNLIVVRIQRDSKIADWPSGSHIRLTYPLTNYRSWIFPTHPYTIASLESDEMLDLIISKSNRFILHPQMP... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58691
Sequence Length: 512
Subcellular Location: Membrane
EC: 1.16.1.-
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Q6CIY2 | MDASSLVKRGSSTHYANLPYGYYVLGVIVFYTIFLIVMRWLIPSRYTKVSPWKNKLLQSIRTASPCFHMPLLLLLVFVPFIHKYSLVAYISLYLKRLGRLSYVLVILNVLLTLRPANPILGYHYLDLIPLHKWLSRFVTVIGIIHGIGFIVKWSLDPKVSMISKATKLFNFIGVIAFVPLFILMFASVRIWRRYSYRSFYVIHQLGQWAMVFLVPIHARPRVTVPYFFILLALYIWRGISYIYYSTTVNVTQRVKDDTSLTYVKLDRSAIRDWLPGSHLRLSKYKKKNPLYWLMPTQPYTIASLPDESQIDLIIRENLTP... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58953
Sequence Length: 508
Subcellular Location: Membrane
EC: 1.16.1.-
|
C5E398 | MAMTLLPRHGKTHLANIPYGYYTATVSLIFIILLIGARKLIPVRQRNRSKWAKWALSSARGGSPLLYLVVLFVALLVPFVHHYSLLGYVGLYLKRLGRLSYVLATLNLFLTLRPNFLLPGYVYLDLIPLHKWLSRSLCLLALVHGVGFLVKWALDSQVSFVAKAFYNIPNLAGLVVGALMAFMVLLSVRPVRRFSYRSFYLTHIIGAWVFVFLTAYHARPGVFVPYTLLNAGLFVFYILSKTVPARGVELVSKSTDDVNNCLTRIVLPRKAMPEHFAPGSHLRISPYRRVNPLYYMLPSHPYTVASMPEDKDVELIVREH... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59726
Sequence Length: 533
Subcellular Location: Membrane
EC: 1.16.1.-
|
A5DE11 | MHNHPRHEGHLHTVNVKYGYVVFLLSIVHIVVVATVPRLRKVGSSSTRRSLPWLPQIVIWAILLAILGVWNIHEWSEHYNVSIKRFGRMAYCLLPFDILLAYKYWPLENYLQNLNLHKWMSRIIVVCSMIHGIGYFVKWFVEGTFFHHLFKIDNLLGVVVFAAAVVLLVVSVALFRRQSYRLFYVSHNITIGMFVVLILFHARPPVTLFVAICGLLLAILFFIKFQTYSATPVSLKEVPNSSLVLVSFPWPDHIATSFKPGSHVRINHSNRSWKSWVFASHPFTSATLPGTSETLDLVVKKGTFIFAKDTQYNLSSPYTS... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54837
Sequence Length: 482
Subcellular Location: Membrane
EC: 1.16.1.-
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A3LN69 | MSWYSVDSEIESLERRHAGHHHTVNIKYGYVILALSIVHMVLSISGKKLYFKNWAETGRASSWWRSVVSIPFWVSTLVWLAIFAFLSIFHIEELSENYTTAVKRLGRMAYCLVPFTIFISLRPPNTVGYQSGYYLEKLNLHKWISRLIFATAIGHGLGFLYKWTKEGALAEKIFKFDNFLGVTVFALMPVLIFASVNVMRRRNYRLFYILHNVTLWMFVVLIAFHARPGVPLLAVINLALLGYQIYQRFFKSYYLHDISVVESPYSKMQIIRIPRPETFPSYLPGSHIRLGYSATNISAWLYATHPFTIASTNDDSESTL... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59993
Sequence Length: 524
Subcellular Location: Membrane
EC: 1.16.1.-
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A7TQE6 | MDELVKRHGSTHFANINYGYYILFLSIIYIILLFCLRNYAKITTRSTRFFKKLYSLNPFIHLSILLIAIFIPFYQPHLNKLTVYYKRLGRLSYTLIPLNLFLTLKPNWFLPSQCTYTDFIPIHKWLSRFITFIAILHSILFLSHWSSSSDENVSIAIKLQNPKNVLGLIMLIPSLLLICLSIGPFRRFSYTSFYIIHNISNVMLIFLTPIHARPGVAIPYLIINSILLLAIAFNKIFFIKKSELLAKETLPNYDNNSSLVTIRLPRSALPETFTPACHIRISPYQFFNPLYWLLPSHPYTVVSLPSDDSVDLVLTENIKK... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59833
Sequence Length: 519
Subcellular Location: Membrane
EC: 1.16.1.-
|
Q6C188 | MLEKRHGDHHNANIKYGTFVLVISLLVVCYIAVRNLTQPEVRARTKRDLRLPLWLSVLLWTALVIGMGVIHVEELNEAAKRFGRLCYALLPLIVFLAIRPSPLPRTFYLKLLPLHKWLGRLATLVGVVHGVLYTVHFVKKNEFYKVFKFDNFLGVIILAVFLVMVVTSLPFFRKRMYSLFYTIHYLSAWFVAIATIFHARPGVGWLFFWVALFMGSSLLYRVLASSTVQIESTEAMGPDLHRVTFPRSILPEFFVPASHIRVSRTLRNPLSWISSTHPYTISSLPSDDHVELIVRPTKFSLAHAASGTQFAVYGPFESLP... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58630
Sequence Length: 525
Subcellular Location: Membrane
EC: 1.16.1.-
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P53109 | MKESPLITLVKRHSETHFANIKYGYYVLIISLVYLIGLALLRAFGRRTPSRSSSAFKNKIIYRLYDIDPAIHLGILFFAVLIPFYYHYSLTTQSTVYLKRLGRLSYALIPLNLFLTLRPNWFLRKNCTYTDFIPFHKWFSRIITVIGLLHGIFFIIKWAIDDNVSLKQKLILKTFNFAGFIISILVLFLLICSIGPMRRYNYRLFYIVHNLVNVAFILLTPIHSRPGVKFPFLLLNCTLLFIHIINRIVFAKSLMILNKNANYSKTNLVHVRLPRAILPDYFEPGSHIRISPYRRINPLYWLLPSHPYTIASLAEDNSID... | Function: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65840
Sequence Length: 570
Subcellular Location: Membrane
EC: 1.16.1.-
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P23180 | MLRSNLCRGSRILARLTTTPRTYTSAATAAAANRGHIIKTYFNRDSTTITFSMEESSKPVSVCFNNVFLRDASHSAKLVTTGELYHNEKLTAPQDIQISEDGKSLVVKWKDGGHHQFPLQFFIDYKGSSFVSPATRKQESRYRPQLWNKRILKDNVKDLLSVSYNEFIDPKDDSKLFQTLVNLQKFGIAFISGTPSSSSEGLTIQKICERIGPIRSTVHGEGTFDVNASQATSVNAHYANKDLPLHTDLPFLENVPGFQILQSLPATEGEDPNTRPMNYFVDAFYATRNVRESDFEAYEALQIVPVNYIYENGDKRYYQS... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Sequence Mass (Da): 53135
Sequence Length: 465
Subcellular Location: Mitochondrion
EC: 1.14.11.-
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P32858 | MQTMGGEHLLLSQLKGSFFLLLLAYFFRGRSPYYARCYRRLAVTPGAITIAIAIATDSIPALAKSKVLVSVCSHTDPCTASCNLIPFPRPFSNSLTRFLFCLGSARFCISFPCFGLSI | Function: Involved in selective mitochondria autophagy (mitophagy).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12936
Sequence Length: 118
Subcellular Location: Mitochondrion membrane
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O14862 | MESKYKEILLLTGLDNITDEELDRFKFFLSDEFNIATGKLHTANRIQVATLMIQNAGAVSAVMKTIRIFQKLNYMLLAKRLQEEKEKVDKQYKSVTKPKPLSQAEMSPAASAAIRNDVAKQRAAPKVSPHVKPEQKQMVAQQESIREGFQKRCLPVMVLKAKKPFTFETQEGKQEMFHATVATEKEFFFVKVFNTLLKDKFIPKRIIIIARYYRHSGFLEVNSASRVLDAESDQKVNVPLNIIRKAGETPKINTLQTQPLGTIVNGLFVVQKVTEKKKNILFDLSDNTGKMEVLGVRNEDTMKCKEGDKVRLTFFTLSKN... | Function: Sensor component of the AIM2 inflammasome, which mediates inflammasome activation in response to the presence of double-stranded DNA (dsDNA) in the cytosol, leading to subsequent pyroptosis . Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-asso... |
P82809 | XXXXXXXXXXXDGHCIPALGFGTYKPIEVPKSKAMEAANLAIGVGYRHIDTAYAYQIEEEIGQAIQSNIKAGIVKREDMFITTKLWCTCFQPELVRPSLEKXXXKLQLEHVDLFIMHYPVPMKAGDNDFPLDEQGKLLLDTVDFCATWEALEKXXDAGLVKSIGVSNFNMRQLERILNKPGLKYKPVCNQVECHVYNNQSKLLDYCKSKDIVLVAFGALGTQRYKEWVDQDSPVLLNDPVLCGGAKXXXRSPALIALRYLVQRGVVPLAQSFYESEMKENLQVFEFQLSPEDMKILDGLNKNFRYLPAQFFADHPEYPFS... | Function: Catalyzes the dehydrogenation of morphine to morphinone. The enzyme also exhibits significant activity for a variety of cyclic and alicyclic alcohols. In addition to xenobiotics, the enzyme catalyzes the dehydrogenation of 17-beta-hydroxysteroids with much higher affinities than morphine. Uses both NAD and NA... |
Q1XAA8 | MDPKGWRVELNDGHFIHALGFGTYAPNEVPKSKAVEATKSAIDAGFRHIDCAHLYDNEKEVGLAIRSKIQDGTVKREDIFCTSKLWATSLRLQLVRPALEKSLKNLQLDYVDLYIIHFPVAVKPGEEHLPQDEQGRMIFDTVDLCATWEAMEKCKDAGLTKSIGVSNFNRRQLEMILNKPGLKHKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQREHWIDQSSPVLLEDPVLCAMAKKYKRTPALIALRYQLQRGVVVLAKSYNEKRIKENVQAFGFQLTSEDMKVLDGLNRNLRYVTLEMFAGHPEYPFSD... | Function: NADP-dependent oxidoreductase that has 20-alpha-hydroxysteroid dehydrogenase activity.
Sequence Mass (Da): 36672
Sequence Length: 322
Subcellular Location: Cytoplasm
EC: 1.1.1.-
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P51857 | MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLKDALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEY... | Function: Catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of bile acid intermediates and steroid hormones carrying a delta(4)-3-one structure to yield an A/B cis-ring junction. This cis-configuration is crucial for bile acid biosynthesis and plays important roles in steroid metabolism. C... |
Q9LYU8 | MAATRVRCCHSNAAFTRLPLTRHRNSPTLPISLNRVDFPTLKKLSLPIGDGSSIRKVSGSGSRNIVRAVLEEKKTEAITEVDEKGITCVMKFGGSSVASAERMKEVADLILTFPEESPVIVLSAMGKTTNNLLLAGEKAVSCGVSNASEIEELSIIKELHIRTVKELNIDPSVILTYLEELEQLLKGIAMMKELTLRTRDYLVSFGECLSTRIFAAYLNTIGVKARQYDAFEIGFITTDDFTNGDILEATYPAVAKRLYDDWMHDPAVPIVTGFLGKGWKTGAVTTLGRGGSDLTATTIGKALGLKEIQVWKDVDGVLTC... | Function: Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Mass (Da): 62298
Sequence Length: 569
Pathway: Amino-acid biosynthesis; L-lysine biosynthesi... |
Q04795 | MKIIVQKFGGTSVKDDKGRKLALGHIKEAISEGYKVVVVVSAMGRKGDPYATDSLLGLLYGDQSAISPREQDLLLSCGETISSVVFTSMLLDNGVKAAALTGAQAGFLTNDQHTNAKIIEMKPERLFSVLANHDAVVVAGFQGATEKGDTTTIGRGGSDTSAAALGAAVDAEYIDIFTDVEGVMTADPRVVENAKPLPVVTYTEICNLAYQGAKVISPRAVEIAMQAKVPIRVRSTYSNDKGTLVTSHHSSKVGSDVFERLITGIAHVKDVTQFKVPAKIGQYNVQTEVFKAMANAGISVDFFNITPSEIVYTVAGNKTE... | Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-asparta... |
Q9VLL3 | MGKAQSKRSIDITTDPKKVGEGDEVAGKVEKIDVDQKTDAPAVNGDAATPKEGGDEAAAVEKKETEEHSENDKDLTTEKSAAVAEGGDAVAETAKGEEGSPKEAAAGEDITPLADESIKSKSKKDKVKKKWSFRSISFGKKDKQKPAKSEEATSPTSGTTSPTTAEAEAAPAGDAAVAEPSVATNGEAEKPAETATATSEPASKDEKPAENGSATEQEKQANGETEKAAPAPSTVEEAAKPKPAEEPATVTATESNTTATEEVPVKESQPEPEVVTNGHGAGEALTNGSSNGLAESPVTETAPVADNIPSNVDDEPPHQN... | Function: Scaffolding protein involved in the regulation of PKA signaling and anchoring to the actin cytoskeleton integrating signals propagated by cAMP, diacylglycerol and calcium . Contributes to the maintenance and regulation of cytoskeletal structures in germline via PKA-mediated signaling . As part of ethanol resp... |
O23653 | MASLQLYGVKTPGLALSSKRLEFASKGACFSVTLPSSSAVFRDVEHSCRNIGLRVSCEALRVDLLQRKEPETCDSSGTGKELTCVMKFGGSSVESAERMKEVANLILSFPDERPVIVLSAMGKTTNKLLKAGEKAVTCGVTNVESIEELSFIKELHLRTAHELGVETTVIEKHLEGLHQLLKGISMMKELTLRTRDYLVSFGECMSTRLFSAYLNKIGHKARQYDAFEIGFITTDDFTNADILEATYPAVSKTLVGDWSKENAVPVVTGYLGKGWRSCAITTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDPNI... | Function: Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Mass (Da): 59605
Sequence Length: 544
Pathway: Amino-acid biosynthesis; L-lysine biosynthesi... |
Q4P6L3 | MAAPGTPLSSSATQAISVSTVDAPSDPLLSSQSAQLDGHSSWDTHMGGSNGIGSRAPSRANTPGQDQMPLTIHSAAQRGDLPAIMRLVDSGRATVHDRDDDNITPLHWAAINAQLATCRYLLDHGAQVDALGGDLIASPLQWAARNGHVYVLELLCSRGADPTITDSQGFNALHLTVHSSAVMPLVFMLQQPSLDSPEGLDSTDSQGHTALMWAAYQGDAISVDILLKHGADVHKRDGAGLTAMHWAVVKGNRLCIRLLADAKADLLAKEDSGKTPRDMAIELKSIGAYRKALADIGLEEDGRRKQRTFGASTDRTARLA... | Function: Palmitoyltransferase specific for casein kinase 1.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90932
Sequence Length: 844
Domain: The DHHC domain is required for palmitoyltransferas... |
Q6C520 | MSTDAELQTISGLSVASKSAPSTQTEGVTASGKVESTTNAEEATSDVEEEENPLVVAARDGNTAEVKRLCESGSYSVLDTAEDGVTALHWAAVNNRISTCQYLVEQGAVVDAKGGQLNGTPLHWACRRGLVYIVHYLIQNGADPLRSDVQGYNALHLATHSSNVMLLVYLLHQGLPVDCQDPNGRTALHWAAYQGDALSVDVLLRWGSDVKITDTQGFLPLHWGIVNGSRNSLARLIEEGSDMYAKSSDGKTPHVMAAEMNTTAQLEGALDDCGRFPDGSQKTKYFDARTTNLLCFFTPFILILLGLVLCTFCGPIFGII... | Function: Palmitoyltransferase specific for casein kinase 1.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77430
Sequence Length: 702
Domain: The DHHC domain is required for palmitoyltransferas... |
P39010 | MVNELENVPRASTLTNEEQTVDPSNNDSQEDISLGDSNEITSLASLKAIRSGNEEESGNEQVNHNDEAEEDPLLTRYHTACQRGDLATVKEMIHGKLLEVNNDGDSTEHITGLHWASINNRLSVVDFLVSQGADVNARAGALHATPLHWAARYGYVYIVDFLLKHGADPTMTDDQGFNLLHLSVNSSNIMLVLYVLFNVVSKGLLDIDCRDPKGRTSLLWAAYQGDSLTVAELLKFGASIKIADTEGFTPLHWGTVKGQPHVLKYLIQDGADFFQKTDTGKDCFAIAQEMNTVYSLREALTHSGFDYHGYPIKKWFKKSQ... | Function: Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis... |
Q9SAR5 | MASNSEKNPLLSDEKPKSTEENKSSKPESASGSSTSSAMPGLNFNAFDFSNMASILNDPSIREMAEQIAKDPAFNQLAEQLQRSIPNAGQEGGFPNFDPQQYVNTMQQVMHNPEFKTMAEKLGTALVQDPQMSPFLDAFSNPETAEHFTERMARMKEDPELKPILDEIDAGGPSAMMKYWNDPEVLKKLGEAMGMPVAGLPDQTVSAEPEVAEEGEEEESIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTP... | Function: Exhibits chaperone activity toward chloroplast outer envelope membrane, mitochondrion outer membrane, endoplasmic reticulum membrane and peroxisomal proteins, by recruiting specific proteins containing a single transmembrane associated with an AKR2A-binding sequence (ABS) and subsequently binding glycolipids ... |
Q12013 | MTSMSIIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKDGDLKVVKDVVESGAVDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNQAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNNDNVDIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLFKKSSHAQFTIFLSPFLLMVYIYLISLVL... | Function: May be involved in constitutive endocytosis of a-factor receptor STE3.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85236
Sequence Length: 749
Domain: The DHHC domain is required for... |
Q0PGJ6 | MANAITFFKLNTGAKFPSVGLGTWQASPGLVGDAVAAAVKIGYRHIDCAQIYGNEKEIGAVLKKLFEDRVVKREDLFITSKLWCTDHDPQDVPEALNRTLKDLQLEYVDLYLIHWPARIKKGSVGIKPENLLPVDIPSTWKAMEALYDSGKARAIGVSNFSTKKLADLLELARVPPAVNQVECHPSWRQTKLQEFCKSKGVHLSAYSPLGSPGTTWLKSDVLKNPILNMVAEKLGKSPAQVALRWGLQMGHSVLPKSTNEGRIKENFNVFDWSIPDYMFAKFAEIEQARLVTGSFLVHETLSPYKSIEELWDGEI | Function: Oxidoreductase acting on a broad range of substrates: reduces ketosteroids, aromatic aldehydes, ketones, sugars and other aliphatic aldehydes, and oxidizes hydroxysteroids . Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes . No a... |
P77256 | MKKIPLGTTDITLSRMGLGTWAIGGGPAWNGDLDRQICIDTILEAHRCGINLIDTAPGYNFGNSEVIVGQALKKLPREQVVVETKCGIVWERKGSLFNKVGDRQLYKNLSPESIREEVAASLQRLGIDYIDIYMTHWQSVPPFFTPIAETVAVLNELKSEGKIRAIGAANVDADHIREYLQYGELDIIQAKYSILDRAMENELLPLCRDNGIVVQVYSPLEQGLLTGTITRDYVPGGARANKVWFQRENMLKVIDMLEQWQPLCARYQCTIPTLALAWILKQSDLISILSGATAPEQVRENVAALNINLSDADATLMREM... | Function: Catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro . It is not known if this activity has physiological significance . Cannot use NADPH as a cosubstrate . Seems to play some role in intestinal colonization .
Catalytic Activity: hydroxyacetone + NAD(+) = H(+) + methylglyoxal + NAD... |
P74308 | MQSFNRINSMKYFPLSNGEQIPALGLGTWKSSPQVVGQAVEQALDLGYRHLDCAAIYGNEAEIGATLANAFTKGVVKREELWITSKLWSNAHHPDAVLPALEKTLQDLGLDYLDLYLIHWPVVIQPDVGFPESGDQLLPFTPASLEGTWQALEKAVDLGLCHHIGVSNFSLKKLEMVLSMARIPPAVNQVELHPYLQQSDLLTFANSQNILLTAYSPLGSGDRPAAFQQAAEPKLLTDPVINGIAAEQGCSAAQVLLAWAIQRGTVTIPKSVNPERLEQNLRAADITLTDSEMAKIALLDRHYRYVSGDFWTMPGSPYTL... | Function: Aldo/keto reductase with broad substrate spectrum. Catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols. Highest enzymatic efficiency is observed with 4-oxonon-2-enal (4-ONE) and 4-hydroxynon-2-enal (4-HNE), that are li... |
P30907 | NPHYVDKDRDLDIACRRIAWGKFMNSGQTCVAPDYILCDPSIQSQVVEKLKKSLKEFYGEDAKKSRDYGRIINSRHFQRVMGLLEGQKVAYGGTGDATTRYIAPTILTDVDPESPVMQEEVFGPVLPIMCVRSLEEAIQFITQREKPLALYVFSPNDKVIKKMIAETSSGGVTANDVVVHISVHSLPYGGVGDSGMGSYHGRKSFETFSHRRSCLVRPLLNEETLKARYPRARPICPDT | Function: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (By similarity). Preferen... |
P30838 | MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTI... | Function: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids . Preferentially oxidizes... |
P51648 | MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTD... | Function: Catalyzes the oxidation of medium and long chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length . Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid .
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Q1JPA0 | MDPFADTLQRLREAFVSGRTRPAEFRDAQLKGLSRFLRENKQLLQEALAQDLHKSAFEAEVSEISISQNEINLALRNLRTWMKDEKVSKNLATQLDSAFIRKEPFGLVLILSPWNYPLNLSLGPLVGALAAGNCVVLKPSEISKNTEKVLAEVLPRYLDQSCFAVVLGGPQETGRLLEHKFDYIFFTGNPQVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAFFRCFNAGQTCVAPDYVLCSPEMQAQLVPALQSAITRFYGDDPQSSPNLGRIISQKHFQRLRGLLSCGRVVIGGQSDECDLYIAPTV... | Function: Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde. Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor. May have a protective role against the cytot... |
P43353 | MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTV... | Function: Oxidizes medium and long chain saturated and unsaturated aldehydes . Metabolizes also benzaldehyde . Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde . May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor . May have a protective role against the c... |
Q80VQ0 | MDSFEDKLQQLREAFKEGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFEAEVSEIAISQAEVDLALRNLRSWMKDEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPINLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFTVVLGGRQETGQLLEHKFDYIFFTGNAYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQIVANRVAWFRYFNAGQTCVAPDYILCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTV... | Function: Oxidizes medium and long chain saturated and unsaturated aldehydes . Metabolizes also benzaldehyde (By similarity). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (By similarity). May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor (By similari... |
P48448 | MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSVP... | Function: Oxidizes medium and long chain aldehydes into non-toxic fatty acids.
PTM: Geranylgeranylation is important for localization to lipid droplets and enzyme activity.
Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 42635
Sequence Length: 385
Pathway: Alcohol meta... |
Q2UPB0 | MAMDKKGDLEWMPPRPEPVHWRNRQRSLAYSVTLTLVALFFTFALRPEAFPSFLVRKGLHKSPLEQVLTRVPLTDGHNDFAIWTRAFYQNHIYRANFTDHDELYGQVDFPRLRKGRLGAQFWSVYVECARNPNEPGVQYEIVRDTFQQIDLVHRMINHFPDFLVPASSVADVHHNFYHSPGRISSLLGIEGLHQIGGSASVLRMYHELGVRYASLTHTCHNEYADSEAPEEPRHGGLSTAGEAIVAEMNRMGMIVDLSHTSLATQRAVFNVTRAPVMYSHSSAYALCPHSRNVPDDLLQMLKENDGIVMISLYPEYTNCQ... | Function: Dipeptidase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor ... |
P30145 | MIRLVTMGKSSEAGVSSFQALTMSLSGRIGVGNVAGTATGIAYGGPGAVFWMWVITFIGAATAYVESTWRKFIKRNKTDNTVAVRRSTLKKALAGNGLRCSRAAIILSMAVLMPGIQANSIADSFSNAFGIPKLVTGIFVIAVLGFTIFGGVKRIAKTAEIVVPFMAVGYLFVAIAIIAANIEKVPDVFGLIFKSAFGADQVFGGILGSAVMWGVKRGLYANEAGQGTGAHPAAAAEVSHPAKQGLVQAFSIYLDVFLVVTATALMILFTGQYNVINEKTGETIVEHLKGVEPGAGYTQAAVDTLFPGFGSAFIAIALFF... | Function: Mediates the active transport of alanine, driven by either an H(+) or Na(+) gradient.
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47804
Sequence Length: 445
Subcellular Location: Cell membrane
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Q07159 | MNQEQFDKIKNGKGFIAALDQSGGSTPKALKDYGVEENEYSNDEEMFNLVHDMRTRIITSPAFNGEKILGAILFEQTMDREVEGKYTGSYLADKGIVPFLKVDKGLAEEADGVQLMKPIPDLDKLLDRANERGIFGTKMRSNILENNKEAIEKVVKQQFEVAKEIIAAGLVPIIEPEVNINAKDKEAIEANLAEAIKAELDNLKKDQYVMLKLTIPTKVNAYSELIEHPQVIRVVALSGGYSRDEANKILKQNDGLIASFSRALVSDLNAQQSDAEFNEKLQEAIDTIFDASVNKA | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 32851
Sequence Length: 296
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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Q8CMY5 | MNKEQLEKMTHGKGFIAALDQSGGSTPKALKEYGVNEDQYSNEDEMFQLVHDMRTRVVTSPSFSPDKILGAILFEQTMDREVEGKYTGDYLADKGVVPFLKVDKGLAEEKNGVQLMKPIDDLDETLDRANERHIFGTKMRSNILELNEQGIKDVVEQQFEFAKKIIAKGLVPIIEPEVNINAKDKSEIEKVLKAEIKKGLDSLNDDQLVMLKLTIPTEANLYKDLADHPNVVRVVVLSGGYSRDEANKLLKDNDELIASFSRALASDLRASQSQEEFDKALGDAVDSIYDASVNKN | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 33052
Sequence Length: 296
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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P58315 | MANLTEKFLRIFARRGKSIILAYDHGIEHGPADFMDNPDSADPEYILRLARDAGFDGVVFQRGIAEKYYDGSVPLILKLNGKTTLYNGEPVSVANCSVEEAVSLGASAVGYTIYPGSGFEWKMFEELARIKRDAVKFDLPLVVWSYPRGGKVVNETAPEIVAYAARIALELGADAMKIKYTGDPKTFSWAVKVAGKVPVLMSGGPKTKTEEDFLKQVEGVLEAGALGIAVGRNVWQRRDALKFARALAELVYGGKKLAEPLNV | Function: Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 28705
Sequence Length: 263
Subcel... |
Q8P5Z7 | MSIEQLAETAQAMVAPGKGIIAIDESTSTIAKRFSGVGIENTEENRRAYRELLLTTPKLSDYISGAILFDETIRQKTKDGVPFAKYMADHGIIPGIKVDKGAQPLAGMPGELVTEGLDGLRARLEEYYTLGARFAKWRAVINIGEDIPSGTCIEANAHALARYAALCQEQGLVPMVEPEVIMDGDHDIETCYEVTEATLRSLFGALYEQNVVLEGTILKASMVISGKGCEEQASVEEVAESTVMCLKSTVPAILPGIVFLSGGQTDEQSTAHLNEMHQLGNLPWPLSFSYGRAMQQAALKLWSKDMTGNYAKAQQIIYER... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 36276
Sequence Length: 334
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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Q9PF52 | MSIEQLAETAQAMVASGKGIIAIDESAGTIAKRFSSVGIENIEENRRAYRELLLTTPKLSDYISGAILFDETIRQSTKAGVPFPKYMADHGIIPGIKVDKGAYPLAGCPGELVTEGLDGLRARLEEYYKLGARFAKWRAVINIGDDIPSGMCIDANVHALARYAALCQEQGLVPMVEPEVIMDGNHDISAAYEVTEATLRSLFNALYEQNVVLEGTILKASMVIPGTDCEEQASIDEVAESTVMCLKSTVPAILPGIVFLSGGQTDAQSTAHLNAMNQLDPLPWPLSFSYGRAMQQAALKLWSQDMKGNFAKAQQVVYER... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 36131
Sequence Length: 334
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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P56109 | MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQTSEGAIKYMGIDMAVGMVKTMCERYPHIPVALHLDHGTTFESCEKAVKAGFTSVMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGIEDNISVDEKDAVLVNPKEAEQFVKESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGASAIPDNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAFIAEVRKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI | Cofactor: Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the re... |
P91759 | HNMFLEGTLLKPNMVTAGQGCPKKYTPEDIARATVTALNRTVPAAVAGITFLSGGQSEEDATINLNAINQFPGRKPWPLTFSYGRALQASVLKAWGGKDEL | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 10831
Sequence Length: 101
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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Q27744 | MNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSNHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENV... | Function: Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate . Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related a... |
O13933 | MLVLKIVLFLSLVIWFNLKKRTDKKRIIVLVLGDIARSPRMQYHAVSFAKLGWKVDLLGYQHPGSSVGLFESHENIRFYPIPSLPAYLQPKNRLQFLFLGPLKVLHQFLALNWALFVRKPASFLFIQNPPCIPVFFIAQCLHILRGTKFIIDWHNFGYSILALKLGKQHTFVKLLKIYEKYMARGAYAHLTVSKRMKDVLQTWGMNPCYVCYDRPPNHFTPIKNEQKKQMSIKKIPCEYNPSSTKLLITSTSWTPDEDIYILWEALNEYDKTLDTPKLLVLITGKGPMKEEFSQYIKKHPLHKVRFCMPWLSIEDYPQVM... | Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER (By similarity).
Catalytic Activity: GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodol... |
Q6C3K2 | MKAWHWSVTLVVIYLAIPVILYLLTRKDDRKPLSDIRKRKRTIVLVLGDLGRSPRMLYHARSLARSGHKVDLCGYDGAKPFDEILNNDLIKIHHIPLILNTRKLPFVVFGILKVIRQHWLLISLLYKLRGADYLLVQNPPSIPTLGVVRFYNLFLSTRTKVVLDWHNFGYTILALKLPETHPMVKFAKFYEGFFGGRAFVHLCVTVLMGQAMRKTFGMSGRRIVPLHDRPAFHFKPLSESEKLDVLRDFKETLYDDMTADHKIIVSSTSYTPDENFNILLDALALYDESKLDLPPLRVIITGKGPMMPEFLAKVEKLQLK... | Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER (By similarity).
Catalytic Activity: GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodol... |
P16661 | MFLEIPRWLLALIILYLSIPLVVYYVIPYLFYGNKSTKKRIIIFVLGDVGHSPRICYHAISFSKLGWQVELCGYVEDTLPKIISSDPNITVHHMSNLKRKGGGTSVIFMVKKVLFQVLSIFKLLWELRGSDYILVQNPPSIPILPIAVLYKLTGCKLIIDWHNLAYSILQLKFKGNFYHPLVLISYMVEMIFSKFADYNLTVTEAMRKYLIQSFHLNPKRCAVLYDRPASQFQPLAGDISRQKALTTKAFIKNYIRDDFDTEKGDKIIVTSTSFTPDEDIGILLGALKIYENSYVKFDSSLPKILCFITGKGPLKEKYMK... | Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Catalytic Activity: GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodolichol = beta-D-M... |
Q59LF2 | MSKRQENKKIAFIHPDLGIGGAERLVVDAAVGLQDFGHDIIIYTSHCDLTHCFEEVSSGQLKVSVHGDSLPTNLFGKLHIFFAILRQFYLVCWLIFTGTIKNYDYFIVDQLSFCIPLLKMFCNSNCQVLFYCHFPDQLLVRRTSFLKKLYRVPFDAIEEYTTGSSDQIVVNSNFTKQIFHDTFKKLNHIDPQVVYPCVDTETIVDTNASSNSEVSKFFKDSPFFLSINRFERSKNIELAIKSFARMNKLMVTKAIKSFARMNKLMVTNKKPRLVIAGGYDSRVAENVEYLAELSTLCDELNLINFTIRGKLIMMPPSVDV... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
Q7KWM5 | MVKDEKELNIAILHPDLGIGGAERLIVDLALGLKSVGNNRITMYTSRHDPKRCFKETSNGELDVHVTGGYFPRHIFNRFMVICAIIRNLLAALYIIFFSGQKYDVIVLDQISASIPLFKLFTNSKVLFYCHFPDKLLTSRTSLIKRLYRIPIDLFEEFTTGCADQVLVNSNFTSSIYKQSFKHLKNSPSVLYPIINTNEFDKTKQSHNFSNQPIENNLINPIKLDDKKFFLSINRYERKKDLKLALDAFSVFISNSESGGSGKGKDEIYLVFAGGYDTGLKENVEHLQELKDKAKEYGLENRVIFLITINEEQKQWLLLN... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
Q9H553 | MAEEQGRERDSVPKPSVLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFAESRELPVRCAGDWLPRGLGWGGRGAAVCAYVRMVFLALYVLFLADEEFDVVVCDQVSACIPVFRLARRRKKILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKETFKSLSHIDPDVLYPSLNVTSFDSVVPEKLDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSQDWERVHLIVAGGYDERVLENVEHYQELKKMVQQSDLGQYVTFLRSFSDKQKISLLHSCTCVLY... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
Q9DBE8 | MAENLYRARSRVYSPSVLFLHPDMGIGGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIETRELSVQCAGDWLPRSLGWGGRGAAICSYVRMVFLALYVLFLSGEEFDVVVCDQVSACIPVFKLARRRKRVLFYCHFPDLLLTQRNSALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHRNPDVLYPSLNIGSFDLAIPEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEWDKVHLFMAGGYDDRIPENVEHYKELKKMVQESDLERHVTFLRSFSDRQKISLLHGCLCVLY... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
Q8X0H8 | MAAGVDEKDKKTIVFLHPDLGIGGAERLVVDAAVGLQNRGHKVVIFTSHCDPRHCFDEARDGTLDVRVRGNSIIPPSLLGRFSILCAILRQLHLILQITLLTSELRTLSPSAFFVDQLSAGLPLLKLLVPTSPIFFYCHFPDLLLVQGRQTWYKRLYRLPFDTWEEWSMGFADSIAVNSSFTKGIVSHTWPSLASKRSLEVVHPCIDVRSTSDSSQNPNDDDKDVLPWTKTGIILSINRFERKKDIALAIKAFASLSPEQRGKAKLIIAGGYDNRVHENVSYHMDLVDLAEGAPYHLKTATAKTVVSALNTSPDVEVLFL... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
O94738 | MTSKSLNVAFIHPDLGIGGAERLVVDAAVGIQKKGHQVIFYTSHHDPNHCFEETRDGTLKVQVRGDWLPRTIFGRFYILCAILRQFVLVASLILWERHSYDIFFVDQLSACVPLLKWFTTAKILFYCHFPDKLLTQRNSTIKKLYRAPVDKMEELTTGMSDLIAVNSGFTAGMFKKSFPSVHQTPQILYPPINFDAYDRPVDRNDPTVKILETDKRVLLSINRFERKKNVELALRAFAALKIKNMVPKDVFANYRLVLAGGYDKRVRENVEYLEELDQLATEEFGLQTFTIHPSSAAADVPADAQVVFLCSFNDAQRTFL... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
Q96WW6 | MSQENSVHRSSTKKTPIKIAFIHPDLGIGGAERLVVDAAVGLQSLGKEVVVFTSHCDKKHCFEEIRDGTIKVKVYGDWLPSSIFGRLSIFCSSLRQVYLTMILLTNYMHFDAIIVDQLSTCVPFLLLASQMILFYCHFPDKYLAKRGGILKKLYRIPFDTVEAESVRLADRIVVNSKFTASVFKKAFPKIRKPLRIVHPCVDIEAASKPLEFQLPEKILQRKLLISVNRFERKKDIRLAIDAFSALRDLSANRFPEYLLLVAGGYDIRVSENRRYLKELQEFCEQKDLSYTTVKDNWDNITVAPSTNVLFLLSVPSKVRD... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
Q6C3V7 | MRVAFIHPDLGIGGAERWVVDAAVGLQNLGHEVDIYTSYCNKSHCFDEVRDGLLKVTVLGDTICPHTIKGKFAIFCATFRQLHLAYELKKGPGSKVDVFVVDQLSACVPLLKLWFPKARVLFYGHFPDQLLVQNRNQMSLVKKAYRYPFDKFEEITTASADRLVVNSHFTKDMFEKTFPATKNPLVIYPCVDTDIKEQQQGLDRDMITAASQYTFLLSINRFERKKNILLAIEAFGEAQKKSSNLKLAVAGGYDFRVNENVEYLQELILACEKLKLSHISITADKYAKLLEKDTPAAVWTSIFKNDVIFFPSASNSFKNT... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
P43636 | MIEKDKRTIAFIHPDLGIGGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCFEEVKNGQLKVEVYGDFLPTNFLGRFFIVFATIRQLYLVIQLILQKKVNAYQLIIIDQLSTCIPLLHIFSSATLMFYCHFPDQLLAQRAGLLKKIYRLPFDLIEQFSVSAADTVVVNSNFTKNTFHQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFKTVFNEGDRFYLSINRFEKKKDVALAIKAFALSEDQINDNVKLVICGGYDERVAENVEYLKELQSLADEYELSHTTIYYQEIKRVSDLESFKTNNSKIIFLTSISSSLKEL... | Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)... |
O82244 | MAGASSPASLRASRSRRLGKETNRSDLFKKPAVPFAFALILADAILVALIIAYVPYTKIDWDAYMSQVSGFLGGERDYGNLKGDTGPLVYPAGFLYVYSAVQNLTGGEVYPAQILFGVLYIVNLGIVLIIYVKTDVVPWWALSLLCLSKRIHSIFVLRLFNDCFAMTLLHASMALFLYRKWHLGMLVFSGAVSVKMNVLLYAPTLLLLLLKAMNIIGVVSALAGAALVQILVGLPFLITYPVSYIANAFDLGRVFIHFWSVNFKFVPERVFVSKEFAVCLLIAHLFLLVAFANYKWCKHEGGIIGFMRSRHFFLTLPSSL... | Function: Required for N-linked oligosaccharide assembly. Adds the sixth mannose residue in an alpha-1,3 linkage onto the dolichol-PP-oligosaccharide precursor dolichol-PP-Man(5)GlcNAc(2).
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1... |
Q751K5 | MSAAVPTTRAGTPPTLQCGWRSACGKLLDIANYVIFSPEASAVVMPVLVAWECVLLKLIVKHVPYTEIDYLAYMEQIWQINNGERDYSKIEGGTGPLVYPAGHVLIHRLLERATDGLQNVARGQDIFTWLYLLTLVLQFGVYRMLRLPPWCIVLACLSKRLHSVYVLRLFNDGWTTLMMVVAVFLLLLAARHPRLCLPAALVYSAAVSIKMNALLYLPGVLVALFLLTRGHLLALALCGAVAVAWQVLVAADFLSTHPAEYFATAFDFRRQFMYRWSVNWQLVGEQVFSHPTFHRCLLLSHIAILMLFFFTRYAAPRQPN... | Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolic... |
Q4WVG2 | MQLHRINTMDLKHSLRDLCMNPRHTSWAAPLLILGDAVLCALIIWRVPYTEIDWTTYMQQISLYISGERDYTLIKGSTGPLVYPAAHVYIYNILYHLTDEGRDIFLGQILFAILYLATLTVAMTCYRQAGAPPYLLVPLVLSKRLHSVFMLRLFNDGIAAFAMWVSIFLFMNKKLAAGVIVWSTGVAIKMTLLLLAPAIAMVLVLSLSFGPSIRLGFLAVLIQVLFGIPFLRNNPAGYVSRAFELTRQFMFKWTVNWRFVGEELFLSRKFSLALLALHLLLLGLFVATVWLEPSGSNLPSFLQRLIQRRYRTASLSKSFV... | Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolic... |
Q8L8W0 | MSSTAASSTVGGGGSSEISGVKKTSKRPKYSRFTQQELPACKPILTPRWVILTFLVAGVVFIPLGVICLFASQGVVEIVDRYDTDCIPTSSRNNMVAYIQGEGDKICKRTITVTKAMKHPVYVYYQLENFYQNHRRYVKSRNDAQLRSPKEEHDVKTCAPEDNVGGEPIVPCGLVAWSLFNDTYSFSRNSQQLLVNKKGISWKSDRENKFGKNVFPKNFQKGAPIGGGTLNISKPLSEQEDLIVWMRTAALPTFRKLYGKIETDLHAGDTITVLLQNNYNTYSFNGQKKLVLSTTSWLGGRNDFLGIAYLTVGSICLFLA... | Function: Required for the lipid transport activity of the ALA/ALIS P4-ATPase complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38909
Sequence Length: 350
Subcellular Location: Golgi apparatus membrane
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P43633 | MLLHFDIVIQLLSSHTLKSHQVEPPMDFETSFEEFVEDKRFIALEVSDNDDDCDTDLTADTADELESSAILKMRESDASLNVTTGNNTSRKTTSNSKKRWSLLSNHSAVSSSKSKKRWSVLSSSFTSESHKDRESRNVLQQKRKSLQSYSSLDTVASNSSISASSSLKRSSTGLSLRQLFTKIGINDDISQPGIGIPQGKENLPPTMGKKNSSIASTSSENRLRTPLKPLVNHSKRPTSQPQQQQPLYNASLSSRRSSISSTVSSSSSSKWRFWKRNKNQTPALLQPDHHSLKTFPAVNRRDSMTPVEPRNMVKHKTSFS... | Function: Serine/threonine haspin-like protein kinase involved in cell cycle regulation.
PTM: Periodically phosphorylated during the cell cycle with a phosphorylation peak during mitosis and hyperphosphorylated after DNA damage.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequ... |
P32789 | MNFDAVADQQMTDRRYFALEVAESDDADSSLNSSSMGSPAVDVGRKVYKITSHKGSAEDESQSFFTSSDSPTSKTRPVGKTIENDDYYGKRSSTGSSLKQLFNKININDTAHSSNKENVSQSVLSENKLLSPSKRLSKQGLTKVTNSKFRTPLRPISNQSTLSRDEPVKDFRSLKFRSGSDFKCWGDEKTSSHVHSSSVNSVNSFTSTTSSSKWKFWKNDNLLSRSLSSRSVNDQDPNFVQPKPTNSLQKKSSISSFHNSIFGGGKHTEKKRNSGFIMPDHQSTKELNHKHSSSNLSFRSLKHKTSHSSLNKLKVRRKGN... | Function: Serine/threonine haspin-like protein kinase involved in cell cycle regulation.
PTM: Periodically phosphorylated during the cell cycle with a phosphorylation peak during mitosis and hyperphosphorylated after DNA damage.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequ... |
P9WJW2 | MHDDFERCYRAIQSKDARFDGWFVVAVLTTGVYCRPSCPVRPPFARNVRFLPTAAAAQGEGFRACKRCRPDASPGSPEWNVRSDVVARAMRLIADGTVDRDGVSGLAAQLGYTIRQLERLLQAVVGAGPLALARAQRMQTARVLIETTNLPFGDVAFAAGFSSIRQFNDTVRLACDGTPTALRARAAARFESATASAGTVSLRLPVRAPFAFEGVFGHLAATAVPGCEEVRDGAYRRTLRLPWGNGIVSLTPAPDHVRCLLVLDDFRDLMTATARCRRLLDLDADPEAIVEALGADPDLRAVVGKAPGQRIPRTVDEAEF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the Sp diastereomer of DNA methylphosphotriester lesions by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. Also catalyzes t... |
Q13686 | MGKMAAAVGSVATLATEPGEDAFRKLFRFYRQSRPGTADLEGVIDFSAAHAARGKGPGAQKVIKSQLNVSSVSEQNAYRAGLQPVSKWQAYGLKGYPGFIFIPNPFLPGYQWHWVKQCLKLYSQKPNVCNLDKHMSKEETQDLWEQSKEFLRYKEATKRRPRSLLEKLRWVTVGYHYNWDSKKYSADHYTPFPSDLGFLSEQVAAACGFEDFRAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLQRDEAPTAMFMHSGDIMIMSGFSRLLNHAVPRVLPNPEGEGLPHCLEAPLPAVLPRDSMVE... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA . Requires molecular oxygen, alpha-ketoglutarate and iron . A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their d... |
P0CB42 | MGKMAAAVASLATLAAEPREDAFRKLFRFYRQSRPGTADLGAVIDFSEAHLARSPKPGVPQVVRFPLNVSSVTERDAERVGLEPVSKWRAYGLEGYPGFIFIPNPFLPGCQRHWVKQCLKLYSQKPNVCNLDKHMTKEETQGLWEQSKEVLRSKEVTKRRPRSLLERLRWVTLGYHYNWDSKKYSADHYTPFPSDLAFLSEQVATACGFQGFQAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLKRDEAPTAMFMHSGDIMVMSGFSRLLNHAVPRVLPHPDGECLPHCLETPLPAVLPSNSLVE... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA . Requires molecular oxygen, alpha-ketoglutarate and iron . A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their d... |
Q9I0R2 | MFENFSPSTMLAIKKYAYWLWLLLALSMPFNYWMAQDSAHPAFWAFSLVIAVFGIGPLLDMLFGRDPANPDEETQTPQLLGQGYYVLLTLATVPVLIGTLVWAAGVFVAFQEWGWLGRLGWILSMGTVMGAVGIVVAHELIHKDSALEQAAGGILLAAVCYAGFKVEHVRGHHVHVSTPEDASSARFGQSVYQFLPHAYKYNFLNAWRLEAVRLRKKGLPVFGWQNELIWWYLLSLALLVGFGWAFGWLGMVFFLGQAFVAVTLLEIINYVEHYGLHRRKGEDGRYERTNHTHSWNSNFVFTNLVLFHLQRHSDHHAFAK... | Cofactor: Binds 2 Fe(3+) ions per subunit.
Function: Catalyzes the hydroxylation of n-alkanes in the presence of a NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases C16-C24 hydrocarbons.
Catalytic Activity: 2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin]
Loc... |
Q0VTH3 | MFENTNPDVMLKMKKYGYLAFWAIMVPLVPFSAFVGVESGTQDYWAWFMYAFIFGIIPVLDYLVGKDPTNPSEDVQVPTMSEEVFYRVSAIAMGFVWIAVLFYAGHIFMNNGYGLLGKIGWIVSIGTVGGIIAINLGHELIHKDPKVENWMGGLLLSSVTYAGFKVEHVRGHHVHVSTPDDASSSRYNQSLYNFLPKAFVHNFINAWSLEKKYLERKGKKNISVHNELIWWYSISALFAATFGLLWGWQGVVFFLGQSFFAALALEIINYIEHYGLHRRVNDKGRFERVTPAHSWNSNFLLTNLALFQLQRHSDHHAYAK... | Cofactor: Binds 2 Fe(3+) ions per subunit.
Function: Catalyzes the hydroxylation of n-alkanes in the presence of a NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases C8-C16 hydrocarbons.
Catalytic Activity: 2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin]
Loca... |
Q9SIE0 | MTNPLNSTAANRSNQPSSDGISDGQITNEEAESLINKKNCSGHKLKEVTDSDTFSDNGKDDSDTKKRFHYHQDQRRMSLTSIVAVESPSSSNAPSRKTIDLGHGSDLIYIQRFLPFQQSWTFFDYLDKHIPWTRPTIRVFGRSCLQPRDTCYVASSGLTALVYSGYRPTSYSWDDFPPLKEILDAIYKVLPGSRFNSLLLNRYKGASDYVAWHADDEKIYGPTPEIASVSFGCERDFVLKKKKDEESSQGKTGDSGPAKKRLKRSSREDQQSLTLKHGSLLVMRGYTQRDWIHSVPKRAKAEGTRINLTFRLVL | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that repairs alkylated DNA containing 1-methyladenine and 1-ethenoadenine by oxidative demethylation. Accepts double-stranded and single-stranded substrates, with a preference for dsDNA over ssDNA. Confers resistance to methylating agents such as methylmet... |
Q58DM4 | MDRFLVKGAVGSLKRRMEQEQTGGGPAGLAEEEGNSKKNPRRAAPGNGVDSAGLTWGRIRAEGLNCDYTILFGKAEADEIFQELEKEVEYFTGALARVQVFGKWHSVPRKQATYGDTGLTYTFSGLTLSPKPWIPVLERVRDRVSLVTGQTFNFVLINRYKDGQDHIGEHRDDERELALGSPIASVSFGACRDFVFRHKDSRGKHPSRRLEVVRLQLAHGSLLMMNHPTNTHWYHSLPVRKKVLAPRVNLTFRKILPTTKRTTLLTASASVGSFALHS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that repairs alkylated nucleic acid bases by direct reversal oxidative dealkylation. Can process both double-stranded (ds) and single-stranded (ss) DNA substrates, with a strong preference for dsDNA (By similarity). Uses molecular oxygen, 2-oxoglutarate an... |
A4VP33 | MRTLTIEPLTKEAFAPFGDVIETEGSDYFMINNGSTRRYHKLATVETAAPEDQAIISIFAAEALEMPLVIRMLERHPLGSQAFIPLLGHPFLVVVAPLGDAPVPGHVRAFRSNGRQGVNYHRGVWHHPVLTIEKRDEFLVVDRSGSGNNCDEYFFTEDQQLLLDPQQVSR | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 19069
Sequence Length: 170
Pathway: Nitrogen meta... |
P32459 | MVTVVAETLTKESFEEYGTIISPDEEISRMQNLEKGANQGTAIKLLQVSQVENKSTSKVPNWNLFRCFPQPHLNRVFTQGSNQAISHSIKVLEKHPCSTQTFVPMGRTSAEVAYLVVVAKEIGNKPDLSTLRAFTCLGNQAVTYGLGTWHAPMIVLGKEEHLDFSVLIYESLDPDRPEKDCVEEHYSDGDVCIII | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as secondary nitrogen source when primary sources are limiting.
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 21727... |
Q5WBJ6 | MLDLCITGGRVVLPSGVEETDVGIQAGKIARIGPINKKEARCIMNANGQYVFPGAVDTHVHFSEPGRTEWEGFFTGSRSLAAGGTTTYVEMPLNALPATTNRANLQRKLEAAKGQNYVDYSFYGGLVPTNLHELADLSASGVVAFKCFLSPCGSDIPGDFRNVDLNGLRAGMRLLAEKGQLLCVHAEDPSMISQLEAKLLSPVGADAYVASRPVEAEVKAVCDTLAAARETGCRIHFVHISSAAAIEAIERAKEEGVDVTVESCPHYFLLSAEELAELGPLAKCQPPLRPKQEQAKLWACLLDGQIDWLASDHSPCTPDL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Se... |
Q65LN0 | MNFDSIIKNGLVILENGEQEVEVGIKDGKIAAIGQDLGTSAKIIDAKGSIVSPGMIDAHVHITEPGGGYRDEWEGYDTGTRAAAKGGVTTFIEMPLNQVPATVDEESIQEKFKAGKGKLSVDVASYGGLVPFDLDGGIQELDSNGVVAYKCFLATCGDRSIEGDFMNVDDYSLYEGMKQIAKTGKILSIHAENAAITDKLGEIASKNGETSLRAYVDSRPVFTEVEPIRKIILFAKETGCRVHIVHIACEEGVDEIVKAQQEGVDITCETCTHYLYFYKEELDHIGPVVKCSPPIREQSRLEGMWNRVLNGDISFVTSDH... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Se... |
O32137 | MAYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPLNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFKAFLSKSGTDEFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Se... |
Q9RV76 | MSLDLLLRGAVLVTPEGERRADLGIVGGQIAELTDEIATPAAQTLDVSGLHVFPGVLDDHVHLNEPGRTHWEGFETGTQALAAGGATSFLDMPLNSSPPVLTRERFEDKARLGEEKSLIDFGLWGGLTPLNLDQLDDLAECGVIGLKAFMSHSGLDEFPAADDLTLYEGMRTAKRHGLVVATHAESNEFTRRLTETARAQGKSGVRDYLESRPVVTELEAVQRALLFAQDTGAALHLVHVSSGAAVALAYEGKQKGIDVTIETCPHYLHFTGEDVERVGAALKCAPPLRDPAVQEELWRELLAGHIDTVGSDHSPAPPDM... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Se... |
Q24PT9 | MSHYDLILRNGNVVCPDGVRKADIAVSDGKIVLIAEEIPGDAKEVIDAAGKHVFPGITDGHVHFNDPGRTEWETISTGSSALAAGGGVAYFDMPLNCSPCTLDAVNFNNKLAVAQKDSLVDYGFWGGLTSANLDKLDELAECGVIGFKAFACHSGIDEFPRMDDYTALVGMEKLAKLGLPLMVHCENAEITKELTELSLANNRTGVRDYFAARPPITEIENVSRMITFAEETGCKLIIAHISTAKAVDLVAQARARGVDVYCETIGHYLYLTGDDVERLGTVAKCSPPIRDGENQLQMWGRLFNDNIAFVSSDHSPCDPK... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Se... |
Q9SRM9 | MDLNAQEKKAGFFQRLQDFPSKLKDDVTKRVKNVQKFAKDDPRRIIHSMKVGVALTLVSLLYYVRPLYISFGVTGMWAILTVVVVFEFTVGGTLSKGLNRGFATLIAGALGVGAVHLARFFGHQGEPIVLGILVFSLGAAATFSRFFPRIKQRYDYGALIFILTFSFVAISGYRTDEILIMAYQRLSTILIGGTICILVSIFICPVWAGEDLHKMIANNINKLAKYLEGFEGEYFQPEKISKETSSCVREYKSILTSKSTEDSLANLARWEPGHGRFRLRHPWKKYLKIAGLVRQCAVHLEILNGYVLSNDKAPQEFESK... | Function: Malate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54400
Sequence Length: 488
Subcellular Location: Membrane
|
Q9LS46 | MAAKQGSFRHGILEKRERLLSNNGFSDFRFTDIESNDLLENENCGRRTRLCCCCSCGNLSEKISGVYDDAKDVARKAWEMGVSDPRKIVFSAKIGLALTIVALLIFYQEPNPDLSRYSVWAILTVVVVFEFTIGATLSKGFNRALGTLSAGGLALGMAELSTLFGDWEEIFCTLSIFCIGFLATFMKLYPSMKAYEYGFRVFLLTYCYILISGFRTGQFIEVAISRFLLIALGAGVSLGVNMFIYPIWAGEDLHNLVVKNFMNVATSLEGCVNGYLRCLEYERIPSKILTYQASEDPVYKGYRSAVESTSQEESLMSFAI... | Function: Vacuolar malate channel. Has a higher selectivity for malate than for fumarate. Exhibits also a weak chloride conductance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67046
Sequence Length: 598
Subcellular Location: Vacuole membrane
|
O23086 | MATQEAGKLEWRISVDNGTTERLVPRSGLSKRIFLWLKDLVMKVIMERVAKFMRKAWRIGADDPAKVVHCLKVGLALSLVSIFYYMRPLYDGVGGNAMWAIMTVVVVFESNVGATFCKCVNRVVATILAGSLGIAVHWVATQSGKAEVFVIGCSVFLFAFAATYSRFVPSFKARFDYGAMIFILTFSLVSVGGYRVDKLVELAQQRVSTIAIGTSICIIITVFFCPIWAGSQLHRLIERNLEKLADSLDGCVAEYFKENEVSTNRNEDENTNMKLQGFKCVLNSKGTEEAMPLIRFSGFSFSQANLARWEPAHGSFNFRH... | Function: Malate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55516
Sequence Length: 497
Subcellular Location: Membrane
|
Q3E9Z9 | MSNKVHVGNIEMEEGLSKTKWMVLEPSEKIKKIPKRLWSVGKEDPRRVIHAFKVGHSLTLVSLLYFMENLFKGIGSNAIWAVMTVVAVLLEFFAVEGLTISEKVILSMAARGRESAAEPHERNEAGNVCHSIKFLPKSIARAKQHHVLNQPY | Function: Malate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17103
Sequence Length: 152
Subcellular Location: Membrane
|
O49696 | MSNKVHVGSLEMEEGLSKTKWMVLEPSEKIKKIPKRLWNVGKEDPRRVIHALKVGLSLTLVSLLYLMEPLFKGIGSNAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKVLRAIFIGTAVFIIGAAATYIRFIPYIKKNYDYGVVIFLLTFNLITVSSYRVDSVINIAHDRFYTIAVGCGICLFMSLLVFPIWSGEDLHKTTVGKLQGLSRSIEACVDEYFEEKEKEKTDSKDRIYEGYQAVLDSKSTDETLALYANWEPRHTLRCHRFPCQQYVKVGAVLRQFGYTVVALHGCLQTEIQTPR... | Function: Malate-sensitive anion transporter permeable to chloride, nitrate, sulfate and malate. Involved in dark-, CO(2)-, abscisic acid- and water-deficient-induced stomatal closure. Belongs to the R-type anion channels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62310
Sequence Length: 560
Sub... |
Q9LS23 | MGYKVEARSMEISMEDEDSRKKRKKGLNLPKKMKKILRNLWNVGKEDPRRVIHALKVGVALTLVSLLYLMEPFFEGVGKNALWAVMTVVVVLEFSAGATLRKGLNRGLGTLIAGSLAFFIEWVAIHSGKILGGIFIGTSVFTIGSMITYMRFIPYIKKNYDYGMLVFLLTFNLITVSSYRVDTVIKIAHERLYTIGMGIGICLFMSLLFFPIWSGDDLHKSTITKLQGLSRCIEACVSEYFEEKLKDNETSDSESDDEDLIYNGYNTVLDSKSADEALAMYAKWEPRHTRRCNKFPSQQYIKVGSVLRKFGYTVVALHGC... | Function: Malate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60505
Sequence Length: 539
Subcellular Location: Membrane
|
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