ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A7HZF9 | MRISIKKILDNESTAGIFLLAAAVFALIFSNVGFLHDIYRHFLELPIVIGVSDYKLDKPLEFWVNDALMAIFFFSIGLELKRERIEGQLRHFSQVFLPSFAAIGGVIFPAVIFAVINFSDSHALRGWAIPTATDIAFAVGVMALLGRRIPTSLKIFVLTLAIMDDLCAIVIIALFYSTALNFTYLGLAFVCFLVLLVMCKLKIPQKIPFVIMSILLWIFVLHSGIHATIAGVAAGFCIPINTSRGNSMLKEMESSLGYFVNYVVLPLFAFANAGVDMRGMQISYLFGPVPLGVMLGLFLGKQLGIFTFSWFLIKMNIVGM... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43589
Sequence Length: 396
Subcellular Location: Cell inner membrane
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A5CM04 | MISPNPALPTPPHAPTAPGRGARLSRFLSRDTTGGILLLIATVLALVIANSPAADLYERVRGFTFGPEALHLDLSVSAWAADGLLAIFFFVVGLELKQEFVAGSLRDPRVAALPIAAAAGRVIVPAGIFTLINLGAGPEALRGWAIPAATDIAFAVAVVAVVGRRLPPVLRTFLLTLAVVDDLLAITIIAVFYTAGIAFVPLLLASVPLAVFGILVQRGVRAWYVLIPLGVAAWALVHASGIHATIAGVALGLLVPAIATARAGVTHRGTAGREERHALTHFFAERWSPISSGIAVPVFAFFSAGVTVGGLEGLTSSLTD... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44506
Sequence Length: 434
Subcellular Location: Cell membrane
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Q1IY26 | MTIRRPGGACLFGLLLAVSPTPFPRRTTLTPIRTLLTPFGEFFKGQASSGLVLILAAVLAFAWANSPWRESYFTLRELPLTLSLGSWTLSHGLYWWVNDLLMALFFLLVGLEIKRELRVGELRHPRQASLALFAALGGMLLPAGLYTLVNAGGPGAAGWGVPMATDIAFALGVLALLGDRVSPGLKVLLAALAILDDLGAVLVIALFYTSGLNLLALGLMGAVWALGLGLNAAGVRHLGPYAVLGAALWLTTLASGLHPTVAGVLLALTIPLGRRAEQEDAEPSPLHRLEHGLHPWSAFLILPLFALFNAGVSVAGGSLD... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44042
Sequence Length: 421
Subcellular Location: Cell membrane
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Q2NDA1 | MVDPIRSPLSRAFAPVRALFVSDASAGILLILVAAAAMIVANSPLAGAYEEMFYGDLAWTPIAKLDDLHLWINDGLMAIFFFVVGLEVKRELICGQLSSPEQRTLPVLAAIAGMAVPAIVYVGVVGTDSALVRGWAIPAATDIAFAMGVLGLLGSRVPASLRLFLLTVAIVDDIGAVLVIAAFYTANLKVMWLVIALGIFGVMVGMNKFGVDRIWPYILVALVLWVAVLFSGVHATIAGVMAALTIPMRRKDGHSLLEKLEHGLAPWSAYLVVPIFGFANAGVNLSGMGLDAVLAPLPLAIAAGLVVGKQLGIFGIIVAA... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42597
Sequence Length: 405
Subcellular Location: Cell inner membrane
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A5FLP0 | MKLTKTFKAFFENEKSGGLLLLFVTVISLWAANSSYSAGYIAFWEKDLAGHSITHWINDGLMTIFFLLIGLELEREIYHGELSNIKNASLPIMAAFGGMLIPAATFLALNFGTSTQNGAGIPMATDIAFAIGILSLLGDKVPASLKVFLTALAVIDDLGAIIVIAVFYTTSIGFVNLAIALGIWVFLFVLNRMKVYNLIPYLIGGVIMWYFMLNSGIHATITGVILAFVIPFGDGGEKSTSYKLQHFLHQPVAFFILPLFAIANTCIAIESNWHIGLNHPNAFGIILGLVIGKPLGILLFSSIGVSAGLCALPKNLKWAH... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41148
Sequence Length: 381
Subcellular Location: Cell inner membrane
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Q7VFN1 | MSEAKITPSRHSYVKDRLQDSLNRFIKHESFGGVLLAFCVGAAMLVANSSYADMYFTFFHSEFGAFFSDSHFKVSLQDFINDVLMSFFFLLVGLEMKREMLYGELAGFKKVSFSFLAAFGGIICPVMIYSYFNSGTAYESGFGVAMSTDTAFALGLIMLLGDRVPKILKIFLVTLAVADDLGAISVIAIFYSDNINMQWIYASLILVAVLIYLNYRDTKYLSLYFLAGILLWFCVHHSGIHVTIAAVILAMAIPGRTRVNKKYFINMLKEFERMKVATNDWNDVVYARESEKVGFWRGSFKNIRSFIFGNQDVEKKIDMA... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56255
Sequence Length: 503
Subcellular Location: Cell inner membrane
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Q6G0H9 | MSALSSNRLPNRASLVTNRAFSALEGFLHVEAFSGIVLLLAAAAALIFANSQYASVYESLWHTPLGFNFGHFTLSWDLHFWVNDALMTVFFLVAGMEIRREIHEGALADFKQAILPIVSAIGGVCFPALIYLSFNFNSEHTHGWAVPTATDIAFALGILALLGKKIPANLHVILLSLAIIDDIIAVLIIAFFYSTNIDPSGLAIAIAGIALVLFFQWIGLASAWLYILPGAIIWWGLMITGVHPSLTGVILGMMTPVFPTRTLVAPLTILSNAMQILQEKNIKTDLHHISTALKKMRKGQRDMIAPVIRVQKTLHPWVAY... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49609
Sequence Length: 458
Subcellular Location: Cell inner membrane
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Q8G5R2 | MATTAGAKKGLWSTIRRIAASDRISGLIMLGFALTGLVLANLPATAHAFETVAETHLFIPYTNLDLPIGHWAQDGLLTIFFLTVGLELKQELTTGSLANPKAAAVPMLCAVGGMIAPPILFLAVTALFSQIGPGEPGTLILTTTGSSIPFSEMSHGWAVPTATDIAFSLAVLALFAKALPGSIRAFLMTLATVDDLLAIILIAVFFSSINAWYWFIGIAVCAAIWAYLVRLKKVPWIAVGIVGILAWIMMFEAGVHPTLAGVLVGLLTPSREMHGELSPRAERYANKLQPFSALLALPIFALFATGVHFESMSPLLLASP... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49613
Sequence Length: 472
Subcellular Location: Cell membrane
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Q8YFI5 | MNHSPQSARPVSIMRRFLDSEAAGGITLMAAAALALIVANSPFAQTYFDALHLYIGPLSLAHWINDALMAIFFLLVGLEIKREMLDGQLASWPNRMLPGIAAAGGVILPAIIFAVLNHDNPAKLRGWAVPSATDIAFALGVLSLLGSRAPSSLKVFLATLAILDDLAAVVIIAIFYTAEISMPYLGAAFITAAVLFVMNRMDVVKLLPYLISAVILWFFVFNSGVHATVAGVVAALMIPLKPAPGRPDDMTSPLHKLEHALAKPVAFIVVPIFGFANAGISFKGLEASVLGDTLTLGILLGLFLGKQFGVFGAAWLAIKT... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78574
Sequence Length: 736
Subcellular Location: Cell inner membrane
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Q9AAZ2 | MLQRVRKLSLLRELLESGAAGGLLLMACAVLALFVANSPLAEGYFHALHVPFAGLDLLHWINDGLMAIFFLFVGLEIKREFLDGQLSTWANRALPCIAAAGGVVVPGLIYASLNAGSPETLRGWAIPTATDIAFALGVLSLLGSRVPTSLKIFLATLAIVDDLVAVLIIAVFYTAELNTAALMGAALVTLVLLGFNRLKVKRLAPYLVMGVALWWLVLLSGVHATIAGVVLAMTIPLHASKAAPDDATSPLHRLEHALSPWVAFLVVPIFGFANAGLSFAGMTPSVLAEPVTLGVALGLFFGKQIGVFGAAWLAIRLGVA... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43454
Sequence Length: 413
Subcellular Location: Cell inner membrane
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A0M0N2 | MGQSVRNQSTIGYIRETATKFLDRETAGGIFLIIATIVALLLANSQWAGAYHHFLGDELLFEFSEHLSFGLTIEEWINDGLMAIFFLVAGLELKREVMVGELSSIKKASAPLLAALGGMAVPALIFISLNLGTENIKGWGIPMATDIAYSLGIIGLLGKNVPRQLKTFLIALAIADDIGAILVIALFYSNELSWIYLGSGMGAFGLLLLMNWTGVKNLIWYIIIGIILWYCFLNSGIHPTIAGVLFAITIPIVPKLDSKILKERTATNVTNLEKTELEKLNPLQDKKQQIILKAIKTDTENSRPPLLKLENSLVDFNAFF... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48576
Sequence Length: 449
Subcellular Location: Cell inner membrane
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P44706 | MTNIQAFMKNFLGASPEWYKLAIVVFLIINPIVFFFISPFIAGWLLVAEFIFTLAMALKCYPLQPGGLLAIEAIIIGMTNAKHVKAEIMANFEVILLLIFMVAGIFFMKQLLLYVFTKLLVKIRSKIALSIAFCFSAAFLSAFLDALTVVAVIISVAMGFYGVYHKVASGNNLIDAVDISDDRKIIEQQHEILEKFRAFLRSLMMHAGVGTALGGVMTVVGEPQNLIIAEQAKWNFMEFFLRMAPVTIPVFICGLLTCFLVEKFKLFGYGEKLPDEVWKILSDLDRTNSEKMSKQDKIKLGMQALIAIWLIVGLAFHLAA... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 3 H(+)(out) + 2 Na(+)(in) = 3 H(+)(in) + 2 Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56540
Sequence Length: 514
Subcellular Location: Cell inner membrane
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P96454 | MTSTTITPHHIGGAWTRTERRRLASVVGAIVILHVLGVALYLGYSGNPAAAGGLAGSGVLAYVLGVRHAFDADHIAAIDDTTRLMLLRGRRPVGVGFFFAMGHSTVVVVLALVVALGASALTTTELEGVQEIGGLVATVVAVTFLSIVAGLNSVVLRNLLCLSRQVRAGSDITGDLESRLSERGLFTRLLGNRWRGLVRSSWHMYPVGLLMGLGLETASEVTLLTLTASAATGGTLSIAAVLSLPLLFAAGMSTFDTADSLFMTRAYSWSYQDPQRRLNFNIATTGATVVIGLFVAGIYVCALLAHLPMFAALSPIGDIS... | Function: Mediates energy-dependent uptake of cobalt ions into the cell. Can also transport nickel ions, but cobalt is the preferred substrate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37187
Sequence Length: 352
Subcellular Location: Cell membrane
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P77567 | MTPILNHYFARINWSGAAAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDNQSPEEKLVIARRGGYCFEQNGVFERVLRELGFNVRSLLGRVVLSNPPALPPRTHRLLLVELEEEKWIADVGFGGQTLTAPIRLVSDLVQTTPHGEYRLLQEGDDWVLQFNHHQHWQSMYRFDLCEQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYENGHAVEQRNLPDVASLYAVMQEQFGLGVDDAKHGFTVDELALVMAAFDTHPEAGK | Function: Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene . N-hy... |
P11067 | MELSVLGQNNGGQHSAGGCSSSSCGSTHDQLSHLPENIRAKVQNHPCYSEEAHHYFARMHVAVAPACNIQCHYCNRKYDCANESRPGVVSEVLTPEQAVKKVKAVAAAIPQMSVLGIAGPGDPLANPKRTLDTFRMLSEQAPDMKLCVSTNGLALPECVEELAKHNIDHVTITINCVDPEIGAKIYPDLLEQQAHPRRQGRKILIEQQQKGLEMLVARGILVKVNSVMIPGVNDEHLKEVSKIVKAKGAFLHNVMPLIAEPEHGTFYGVMGQRSPEPEELQDLQDACAGDMNMMRHCRQCRADAVGMLGEDRGDEFTLDK... | Cofactor: Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two others probably act as substrate.
Function: Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitro... |
Q8KC85 | MTLNIKNHPCFNDSSRHTYGRIHLPVAPKCNIQCNYCNRKFDCMNENRPGITSKVLSPRQALYYLDNALKLSPNISVVGIAGPGDPFANPEETMETLRLVREKYPEMLLCVATNGLDMLPYIEELAELQVSHVTLTINAIDPEIGQEIYAWVRYQKKMYRDRQAAELLLENQLAALQKLKRYGVTAKVNSIIIPGVNDQHVIEVARQVASMGADILNALPYYNTTETVFENIPEPDPMMVRKIQEEAGKLLPQMKHCARCRADAVGIIGEINSDEMMAKLAEAALMPKNPDEHRPYIAVASLEGVLINQHLGEADRFLVY... | Cofactor: Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two others probably act as substrate.
Function: Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitro... |
P27714 | MQPTQYVGIQDIKSLGTLLDKVAEHKGCGTSSEGGKASCGSSDGPADMAPEVWEKVKNHPCYSEEAHHHYARMHVAVAPACNIQCNYCNRKYDCANESRPGVVSEKLTPEQAAKKVFAVASTIPQMTVLGIAGPGDPLANPAKTFKTFELISQTAPDIKLCLSTNGLALPDHIDTIAAFNVDHVTITTNMVDPEIGQHIYPWIYYQNKRWTGIDAARILHERQMLGLEMLTARGILCKVNSVMIPGINDQHLVEVNRAVKSRGAFLHNIMPLISAPEHGTVFGLNGQRGPSAQELKALQDACEGEMNMMRHCRQCRADAV... | Cofactor: Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two others probably act as substrate.
Function: Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitro... |
P10390 | MTSCSSFSGGKACRPADDSALTPLVADKAAAHPCYSRHGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVVKVRQVAQAIPQLSVVGIAGPGDPLANIARTFRTLELIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIYAWLWLDGERYSGREAGEILIARQLEGVRRLTAKGVLVKINSVLIPGINDSGMAGVSRALRASGAFIHNIMPLIARPEHGTVFGLNGQPEPDAETLAATRSRCGEVMPQMTHCHQCRADAIGMLGEDRSQQFTQLPAPESLPAWLPIL... | Cofactor: Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two others probably act as substrate.
Function: Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitro... |
O26739 | MKRIAIYGKGGIGKSTIVSNMAAAYSSEHRVLVIGCDPKADTTRTLYGERLPTVLDVLKENREPDVSEVIHTGFGGVRCVESGGPEPGVGCAGRGVIVAMNLLERLGVFREDIDVVIYDVLGDVVCGGFAVPLREDFADEVYIVTSGEYMSLYAANNIARGIRKLKGKLGGVICNCRGIRDEVEIVSEFASRIGSRLIGAVPRSNLVQESELEARTVIERFPESEQASVYRKLAEDIYRNTEFTVPEPMDQEEFEEFFRKFRVEG | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
PTM: The reversible ADP-ribosylation of Arg-94 inactivates the nitrogenase reductase and regulates ... |
Q9AKT4 | MAKKIKQIAIYGKGGIGKSTTTSNISAALSVAGYKVMQFGCDPKSDSTNTLRGGEYIPTVLDTLRDKQIVRAHDVIFEGFNGIYCVEAGGPAPGVGCAGRGIITSVSLLKQQKVFEELDLDYVIYDVLGDVVCGGFAVPVREGIAEHVFTVTSADFMALYAANNLFKGIHKYSTEGGALLGGVIANSINAPYAKEIVDDFVARTHTQVMEYVPRSVSVTQAELQGKTTIEADPNSKQAQIYKSLAQKIVDHTESKVPVPLETSELREWASNWGKQLVELEAGVLSPAAAGNL | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
PTM: The reversible ADP-ribosylation of Arg-100 inactivates the nitrogenase reductase and regulates... |
Q44290 | MNKVLINDTTLRDGEQAAGVVFTLEEKVAIAKFLDTIGVPELEVGIPAMGEEEMRAICAISNLGLKANLLAWNRAVISDIKASVACGMERVHIAIPVSGIQIAAKFHGQWRVSLQRLKDCISFAVDQGLWVAVGGEDSSRADENFLLDVALYAQEWGASRFRFCDTVGVLDPFTTYGKVKLLVSALTIPVEVHTHNDFGMATANALAGIKAGASSVNTTVIGLGERAGNAALEEVVMAIKRIYGVDMGIDTPRLLELSQLVAAASGANVPPWKAIVGENTFAHESGIHAHGVLQNPDTYEPFAPEEVGWERRLVVGKHSG... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 40851
Sequence Length: 377
EC: 2.3.3.14
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Q00853 | MGINIVDTTLRDGEQKAGIALSVQDKVEIAKIISEMGVHQIEAGIPAMGGDEKISVSKIAALGLPSKIAAWNRMSTKDIDTSIECGVDIVHISSPVSDLQIKTKLEKDRKWVAENLKRTVIYALEKDCEVTVGLEDSSRADLNFLIQLCEMIFALGVKRVRYADTVGIMEPKELYSQIKKIRDKVPIDIEIHVHNDFGMAISNSFAAFKAGAKFADCTITGMGERAGNCDFLKFVKVIQELTGEKIYTGDFEDIIEKENEIKKILRLNW | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 29865
Sequence Length: 269
EC: 2.3.3.14
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Q00852 | MAVVMDGVKKNIIDRTIPNLVKKFQNFNNDDIAYFLKLLHETGIDLFEINRDSMDKIKKFPLNLDYIYRIENIEDYNYLNNYNFKYIILNYKTIYRFLLEDEKIQKNLKEHNIILEIDIEDLDELYLSEDNKIFCIFNIVCLRINNLSKLDFIDEDFRIKDLKSKFNVLVDFCASNKYNMATAIIINAFLNGSDIITTEFNSNDYAAMEEVIIALKSIRNIEIRGDLKLISKLTRIYEKITSERVYSMKPILGEDIFKYESGIHADGIAKNPKNYEPFNPELIGTNRKLYIGKHSGKAALVVKFKELNLNCNNIDMNLFL... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 41578
Sequence Length: 352
EC: 2.3.3.14
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P70728 | MAGSTIINDTHARDGEQTAGVAFTLDEKIAIAQALDEAGVAELEIGIPAMGREERERIRAVASLGLKARLMVWCRMHDTDLKARSTAVAPSLSVPVSDIHITKKLNGSRAWALREIERKVKTARDHGLEVSLGGEDSSRADMDFLIAAATVAQRPRFRFADTLGVLDPFQHARLHLTAAATDPEIGYHAHTPRLANATAWVTLAAVLGGATHVNTTVNGLGERAGNAPLEEVVVSLKVLYGQDCGVDTRALGAISDLVERASNRPVAVNKSIVRDAVFTHEAGIHVDGLLTDRAPTRISTPPRWGASTASCWASIPARGG... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 39701
Sequence Length: 376
EC: 2.3.3.14
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P05342 | MASVIIDDTTLRDGEQSAGVAFNADEKIAIARALAELGVPELEIGIPSMGEEEREVMHAIAGLGLSSRLLAWCRLCDVDLAAARSTGVTMVDLSLPVSDLMLHHKLNRDRDWALREVARLVGEARMAGLEVCLGCEDASRADLEFVVQVGEVAQAAGARRLRFADTVGVMEPFGMLDRFRFLSRRLDMELEVHAHDDFGLATANTLAAVMGGATHINTTVNGLGERAGNAALEECVLALKNLHGIDTGIDTRGIPAISALVERASGRQVAWQKSVVGAGVFTHEAGIHVDGLLKHRRNYEGLNPDELGRSHSLVLGKHSG... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 41653
Sequence Length: 385
EC: 2.3.3.14
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Q01181 | MSRQQPRASFLPESPLAPVALCDTTLRDGEQTAGVAFTRAEKRAIAEALQAAGVAEVEVGVPAMGEEERADIRAVAAVLKTAAPVVWCRLRAEDLAAAQRTGVVRLHIGVPVSERQISAKLGKDAAWVRDKVEKLVRAASWAGHKVSVGAEDASRADPFFLAEIAHVAAEAGAIRFRISDTLGVLDPFAAHELVGRVVTRCPLPVEFHGHNDLGMATANSLAAARAGASHLSVTVNGLGERAGNAALEEVAAALEAAGRATGVALGQLCALSELVARASGRPLSPQKPIVGEGVFTHECGIHVDGLMKDRATYESADLRP... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 40666
Sequence Length: 391
EC: 2.3.3.14
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P54610 | MTVRETRFPSSSATATQPDAVVRFCDTTLRDGEQAPGVAFTAAEKLAIAGALDAIGVHQIEAGIPGMGVTERDVLREILATDPKAEIVGWCRADHRDVEAAASCGLVTAHLTIPVSDLHLKSKLERDRAWARRRVRDCVVDGTDRGMRVSVGFEDASRADDAFVTDLAGELRDVGVTRLRWADTVGLLDPVSAYDRLGRLVRAVPGPWEIHAHDDFGLATANTIAAVQAGFTWVSTTVLGLGERAGNAPIEEVAMALRHLLKLPIDLDTTSFRTLAQLVVGWPLPAGKKAVVGESVFAHESGIHVHGILRHPATYEPFDP... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 43158
Sequence Length: 401
EC: 2.3.3.14
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P05345 | MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQNAPAARLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAAAWKPSALGLERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHS... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Mass (Da): 41190
Sequence Length: 381
EC: 2.3.3.14
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O28435 | MHIPDGYLDLSIAGLFYILSIAVLGYSIYRLRGQKLTSLFGIVAAAIFAAQMLNWPIPGGTSAHFVGGALAGILLGPYAGALAMAVVLTIQCLVFADGGITALGANVWNMAIVNVFVGYYVYRAIERFNRSAAAFIAGWIGITLAAIFAGIEIGISTSFGYGLKVTLPVMGTWHALLGLVEGTITAGVVSYIAAARPDVIEQKAAPGKLALAVIAAMIAVSPLFAYAAELVGYSEPLENAAAMLGLEENPIYEGLLPDYTLPGLDPYAGTLIAGIVGTVIVLALGFALTRYARTA | Function: May be involved in nickel transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30664
Sequence Length: 295
Subcellular Location: Cell membrane
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D5AQY8 | MHIPDGYLSPVTCAVTFAATVPFWYVSMRKLDRDLNGQHLPLVALVAAFSFVIMMFNLPIPGGTTAHAAGIGIAAVLLGPWAAVPAISVALLIQAIFFGDGGITAFGANCLNMAVVGPMVAAAVYALGTRGAAIGSRRRVIMAGLASYAGLNAAALLAAVEFGVQPLFFHDAAGAPLYAPYPLSVAVPAMALTHLTIAGAAEFIVTAGLVAWLQRSNPELLAPRRAPAAPERHLRLWAGIGALVVLCPLGLIAAGTAWGEWGAEDFTSEAGRAAMAGASGGVAPPAGLPGGFARLAELWSAPLPDYAPAFVQNAPLGYVL... | Function: Part of the energy-coupling factor (ECF) transporter complex NikMNQO involved in nickel import. The complex confers nickel uptake upon expression in E.coli; can also transport cobalt with a very low affinity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35244
Sequence Length: 347
Subcell... |
D5AQY6 | MTPAFELQGVQFAYKGVPALNGLDLTLPLGRRTALLGANGSGKSTLLRLLDGLQFPAAGRISAFGTPLTEAMFTDEAAAIAFRRRVGFVFQNPEVQLFCPSVFDELAFGPLQLHWPKERIRARVARAIAQFGLGPLAGRPPHRLSGGEKKRVALASVLILDPEVLLLDEPTAALDPQATDDIAALLETEFGARNPGRTLIFSSHDLDLVARIADHVVVLEAGKVAAAGPAAEVLARTALLRRARLLPGFDGTAP | Function: Part of the energy-coupling factor (ECF) transporter complex NikMNQO involved in nickel import. The complex confers nickel uptake upon expression in E.coli; can also transport cobalt with a very low affinity. Presumably responsible for energy coupling to the transport system.
Location Topology: Peripheral mem... |
D5AQY7 | MTDPSVVHARAPAPDRIGRLGAGVRGLMQHAEEAAGLAQRPGLLQGLDPRAKVAGAFALILAAVATRSLLVLLALFVLATALAAASQISPARLARQVWIVVLGFTGMIALPALILVPGTPVLSLPFGLAITEQGLRAAAFLTGRSETTATLALALVLTTPWPQVLKALRCLGVPRAAVMILGMTHRYIFVLADLALDLFEARRSRLVGRLSPAEARRLATGIAGALFERALALSSEVHLAMLARGWRGEVHLIDDFRFRPRDGGALVLAAAILAGVVWAGSVWP | Function: Part of the energy-coupling factor (ECF) transporter complex NikMNQO involved in nickel import. The complex confers nickel uptake upon expression in E.coli; can also transport cobalt with a very low affinity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29859
Sequence Length: 284
Subcell... |
Q9VFS2 | MAAGVFKSFMRDFFAVKYDEQRNDPQAERLDGNGRLYPNCSSDVWLRSCEREIVDPIEGHHSGHIPKWICGSLLRNGPGSWKVGDMTFGHLFDCSALLHRFAIRNGRVTYQNRFVDTETLRKNRSAQRIVVTEFGTAAVPDPCHSIFDRFAAIFRPDSGTDNSMISIYPFGDQYYTFTETPFMHRINPCTLATEARICTTDFVGVVNHTSHPHVLPSGTVYNLGTTMTRSGPAYTILSFPHGEQMFEDAHVVATLPCRWKLHPGYMHTFGLTDHYFVIVEQPLSVSLTEYIKAQLGGQNLSACLKWFEDRPTLFHLIDRV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the oxidative cleavage at the 15,15'-double bond of carotenoids and the simultaneous all-trans to 11-cis isomerization of one cleavage product. Carotenoids like 11-cis retinal can promote visual pigment biogenesis in the dark. Essential for the biosynthesis ... |
A8Y9I2 | MAVHQEKLYPNCDSGVWLRSCEEEVTEPLEGTITGEIPSWLQGSLLRNGPGSLKVGSMRFEHLFDSSALLHRFAINDGSVTYQCRFLQSNTFKKNRAAERIVVTEFGTRAVPDPCHTIFDRVAALFKPGESLSDNAMISLYPFGDEIYAFTEGPVIHRIDPETLDTLERRNLMDSVSLVNHTSHPHVMPNGDVYNLGMSIVQGRLKHVIVKFPYTEKGDMFAKAHIVANMSPRWPLHPAYMHTFGITENYFVIVEQPLSVSLLTMVKSQPSNEPLASSLHWYPNHETHIVLLSRRDGKEVKRYRTEPLFYLHIINAYEHD... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the oxidative cleavage at the 15,15'-double bond of carotenoids and the simultaneous all-trans to 11-cis isomerization of one cleavage product. Carotenoids like 11-cis retinal can promote visual pigment biogenesis in the dark. Essential for the biosynthesis ... |
Q9VGP2 | MGMKFQKILVLAGIVIGFLSIIVVLAGTLLKNSVPNVLAPVERHFAFDYVIVGGGTGGSTLTSLLAKNSNGSVLLIEAGGQFGLLSRIPLLTTFQQKGINDWSFLSVPQKHSSRGLIERRQCLPRGKGLGGSANLNYMLHFDGHGPDFDSWRDHHNLSDWSWAQMRSFMAAAKPKNPDMLEIPRRYSKLTEALEEAQAQFAYKDWIFRRSLYNIRNGLRHSVVQQFLNPVIHHSNLRLLPDALVKRIQLAPSPFLQATSILVGIKDEENREKEFSIELLMASGIGDVSALKKLGIPAQHSLPLVGHNLHDHFNLPLFVSM... | Function: Oxidoreductase involved in biosynthesis of 3-hydroxyretinal, a chromophore for rhodopsin Rh1. Not responsible for the initial hydroxylation of the retinal ring but rather acts in a subsequent step in chromophore production. May catalyze the conversion of (3R)-3-hydroxyretinol to the 3S enantiomer.
Sequence Ma... |
Q9I609 | MRLIGLALGLLLGALAQAGEAPGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQLDDAAADALVAYLYQAPPREPQWSAEDIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGG... | Function: Involved in heme d1 biosynthesis . Catalyzes the introduction of a double bond into the propionate side chain of pyrrole ring D of dihydro-heme d1, therefore converting dihydro-heme d1 to heme d1 .
Catalytic Activity: A + dihydro-heme d1 = AH2 + heme d1
Sequence Mass (Da): 53978
Sequence Length: 493
Domain: C... |
P24474 | MPFGKPLVGTLLASLTLLGLATAHAKDDMKAAEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPLGMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDGDSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMIDLWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAIIASHEHPEFI... | Cofactor: Binds 1 heme c group covalently per subunit.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite
Sequence Mass (Da): 62653
Sequence Length: 568
Subcellular Location: Periplasm
EC: 1.7.2.1
|
P24040 | MSNVGKPILAGLIAGLSLLGLAVAQAAAPEMTAEEKEASKQIYFERCAGCHGVLRKGATGKNLEPHWSKTEADGKKTEGGTLNLGTKRLENIIAYGTEGGMVNYDDILTKEEINMMARYIQHTPDIPPEFSLQDMKDSWNLIVPVEKRVTKQMNKINLQNVFAVTLRDAGKLALIDGDTHKIWKVLESGYAVHISRMSASGRYVYTTGRDGLTTIIDLWPEEPMTVATVRFGSDMRSVDVSKFEGYEDKYLIGGTYWPPQYSIVDGLTLEPIKVVSTRGQTVDGEYHPEPRVASIVASHIKPEWVVNVKETGQIILVDYT... | Cofactor: Binds 1 heme c group covalently per subunit.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite
Sequence Mass (Da): 61993
Sequence Length: 560
Subcellular Location: Periplasm
EC: 1.7.2.1
|
P24038 | MTDKDGNKQQKGGILALLRRPSTRYSLGGILIVGIVAGIVFWGGFNTALEATNTETFCISCHEMGDNVYPEYKETIHYANRTGVRATCPDCHVPRDWTHKMVRKVEASKELWGKIVGTIDTAEKFEAKRLTLARREWARMRASDSRECRNCHSLESMSSDMQKQRARKQHEMAREDNLTCIACHKGIAHHLPEGMTEEDED | PTM: Binds 4 heme groups per subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22825
Sequence Length: 201
Subcellular Location: Cell membrane
|
P25006 | MTEQLQMTRRTMLAGAALAGAVAPLLHTAQAHAAGAAAAAGAAPVDISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLIGGHGDYVWATGKFRNPPDLDQETWL... | Cofactor: Binds 1 Cu(+) ion.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite
Sequence Mass (Da): 40771
Sequence Length: 378
Domain: The ... |
P38501 | MAEQMQISRRTILAGAALAGALAPVLATTSAWGQGAVRKATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDDAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATGALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYEDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIP... | Cofactor: Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been... |
P81445 | GLPRVAVDLVAPPLVHPHSQVAAGAPKVVQFRMSIEEKKMVADDDGTTAQAMTFNGSVPGPTLVVHEGDYIELTLVNPATNSMPHNVDFHAATGALGGAGLTQVVPGQEAVLRFKADRSGTFVYHCAPAGMVPWHVVSGMNGALMVLPRDGLRDAAGAALAYDRVYTIGESDLYVPKAADGNYSDYPALASAYADTVAVMRTLTPSHAVFNGAVGALTGANALTAAVGESVLIIHSQANRDSRPHLIGGHGDWVWTTGKFANPPQLNMETWFIPGGSAAAALYTFKQPGTYAYLSHNLIEAMELGAAAQASVEGQWDDDL... | Cofactor: Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + ni... |
Q39161 | MTSFSLTFTSPLLPSSSTKPKRSVLVAAAQTTAPAESTASVDADRLEPRVELKDGFFILKEKFRKGINPQEKVKIEREPMKLFMENGIEELAKKSMEELDSEKSSKDDIDVRLKWLGLFHRRKHQYGKFMMRLKLPNGVTTSAQTRYLASVIRKYGEDGCADVTTRQNWQIRGVVLPDVPEILKGLASVGLTSLQSGMDNVRNPVGNPIAGIDPEEIVDTRPYTNLLSQFITANSQGNPDFTNLPRKWNVCVVGTHDLYEHPHINDLAYMPANKDGRFGFNLLVGGFFSPKRCEEAIPLDAWVPADDVLPLCKAVLEAYR... | Cofactor: Binds 1 siroheme per subunit.
Function: Catalyzes the six-electron reduction of nitrite to ammonium.
Catalytic Activity: 2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 65505
Sequence Length: 586
Pathway: Nitrogen metabolism; nitrate r... |
P38500 | MSSLSVRFLSPPLFSSTPAWPRTGLAATQAVPPVVAEVDAGRLEPRVEEREGYWVLKEKFREGINPQEKLKLEREPMKLFMEGGIEDLAKMSLEEIDKDKISKSDIDVRLKWLGLFHRRKHHYGRFMMRLKLPNGVTTSAQTRYLASVIRKYGKDGCADVTTRQNWQIRGVVLSDVPEILKGLDEVGLTSLQSGMDNVRNPVGNPLAGIDIHEIVATRPYNNLLSQFITANSRGNLAFTNLPRKWNVCVVGSHDLFEHPHINDLAYMPAIKDGRFGFNLLVGGFFSPRRCAEAVPLDAWVSADDIILVCKAILEAYRDLG... | Cofactor: Binds 1 siroheme per subunit.
Catalytic Activity: 2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 65229
Sequence Length: 583
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
Subcellular Location: Plastid
EC: 1.7.7.1
|
P43504 | MAATLPLLTQGIEPVSGESYSPPGERHVQATWGSKDGNISNTEWNDPEANRLPEKVAELEKKGELNNSHPRRRVVVVGLGMVGVAFIEKLMKYDIKRREYDIIVIGEEPHLAYNRVGLTSFFQHRQVENLYLNPQEWYSSMPEDSLHYHLNTLVTEIDSENKTVKTSSGQAVSYDILVLATGSSS | Cofactor: Binds 1 siroheme per subunit.
Catalytic Activity: 2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite
Sequence Mass (Da): 20756
Sequence Length: 185
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
EC: 1.7.1.4
|
P17847 | IPGRTGRARAAVSVPPPAGEQVPTERLEPRVEERAGGYWVLKEKYRAGLNPQEKVKLEKEPMALFMEGGIQDLARVPMEQIDAAKLTKDDVDVRLKWLGLFHRRKHQYGRFMMRLKLPNGVTTSEQTRYLASVIEAYGADGCADVTTRQNWQIRGVTLPDVPAILDGLRAVGLTSLQSGMDNVRNPVGNPLAGVDPHEIVDTRPYTNLLSSYVTNNSQGNPTITNLPRKWNVCVIGSHDLYEHPHINDLAYMPAVKDGEFGFNLLVGGFISPKRWAEALPLDAWVAGDDVVPVCKAILEAYRDLGSRGNRQKTRMMWLID... | Cofactor: Binds 1 siroheme per subunit.
Catalytic Activity: 2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 63342
Sequence Length: 569
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
Subcellular Location: Plastid
EC: 1.7.7.1
|
Q42997 | MASSASLQRFLPPYPHAAASRCRPPGVRARPVQSSTVSAPSSSTPAADEAVSAERLEPRVEQREGRYWVLKEKYRTGLNPQEKVKLGKEPMSLFMEGGIKELAKMPMEEIEADKLSKEDIDVRLKWLGLFHRRKHQYGRFMMRLKLPNGVTTSEQTRYLASVIEAYGKEGCADVTTRQNWQIRGVTLPDVPAILDGLNAVGLTSLQSGMDNVRNPVGNPLAGIDPDEIVDTRSYTNLLSSYITSNFQGNPTITNLPRKWNVCVIGSHDLYEHPHINDLAYMPAVKGGKFGFNLLVGGFISPKRWEEALPLDAWVPGDDII... | Cofactor: Binds 1 siroheme per subunit.
Function: Catalyzes the six-electron reduction of nitrite to ammonium.
Catalytic Activity: 2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 66143
Sequence Length: 596
Pathway: Nitrogen metabolism; nitrate r... |
P26715 | MDNQGVIYSDLNLPPNPKRQQRKPKGNKNSILATEQEITYAELNLQKASQDFQGNDKTYHCKDLPSAPEKLIVGILGIICLILMASVVTIVVIPSTLIQRHNNSSLNTRTQKARHCGHCPEEWITYSNSCYYIGKERRTWEESLLACTSKNSSLLSIDNEEEMKFLSIISPSSWIGVFRNSSHHPWVTMNGLAFKHEIKDSDNAELNCAVLQVNRLKSAQCGSSIIYHCKHKL | Function: Immune inhibitory receptor involved in self-nonself discrimination. In complex with KLRD1 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia molecul... |
Q9MZK6 | MNKQRGTFSEVSLAQDPKRQQRKPKDNKSSISGTKQEIFQVELNLQNPSLNHQGIDQIYDCQGLLPPPEKLTAEVLGIICIVLMATVLKTVVLIPFLEQNNSFPNTRTQKVRHCGHCPEEWITYSNSCYYIGKEKRTWAESLLACTSKNSSLLSIDNEEEMKFLTAISPSTWTGVFRDSSHHPWVTINGLTFKHEIKDSDHAEYNCAMLHLDRLKSVQCGSSKRYYCKHKL | Function: Immune activating receptor involved in self-nonself discrimination. In complex with KLRD1 on cytotoxic lymphocyte subsets, recognizes non-classical major histocompatibility MHC-E loaded with signal sequence-derived peptides from non-classical MHC-G molecules, likely playing a role in the generation and effect... |
P26718 | MGWIRGRRSRHSWEMSEFHNYNLDLKKSDFSTRWQKQRCPVVKSKCRENASPFFFCCFIAVAMGIRFIIMVTIWSAVFLNSLFNQEVQIPLTESYCGPCPKNWICYKNNCYQFFDESKNWYESQASCMSQNASLLKVYSKEDQDLLKLVKSYHWMGLVHIPTNGSWQWEDGSILSPNLLTIIEMQKGDCALYASSFKGYIENCSTPNTYICMQRTV | Function: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (N... |
O54709 | MALIRDRKSHHSEMSKCHNYDLKPAKWDTSQEQQKQRLALTTSQPGENGIIRGRYPIEKLKISPMFVVRVLAIALAIRFTLNTLMWLAIFKETFQPVLCNKEVPVSSREGYCGPCPNNWICHRNNCYQFFNEEKTWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQIPANGSWQWEDGSSLSYNQLTLVEIPKGSCAVYGSSFKAYTEDCANLNTYICMKRAV | Function: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (N... |
Q9GLF5 | MGWIRDRRSPSSMEIRELHNRDVINRGAFKSRQKRTQTLITSKCGENPSPFFLARSIAIAMGIRFIVMVMIYSGMIINLLFNQEAPSPLKESYCGPCPKNWICYRNSCYQFSNESKTWLQSQASCRSQNSSLLKIYSREDQDFFKLVKSYHWMGLVQIPTNRSWQWEDGSILSPNQITMVEMQNGSCAVYGSSFKGYTENCLTLNTYICMKRTV | Function: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (N... |
Q07444 | MSKQRGTFSEVSLAQDPKWQQRKPKGNKSSISGTEQEIFQVELNLQNASLNHQGIDKIYDCQGLLPPPEKLTAEVLGIICIVLMATVLKTIVLIPFLEQNNSSPNARTQKARHCGHCPEEWITYSNSCYYIGKERRTWEESLQACASKNSSSLLCIDNEEEMKFLASILPSSWIGVFRNSSHHPWVTINGLAFKHEIKDSDHAERNCAMLHVRGLISDQCGSSRIIRRGFIMLTRLVLNS | Function: Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 27100
Sequence Length: 240
Subcellular Location: Membrane
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Q95MI1 | MNKQRGTYSEVSLAQDPKRQQRKLKGNKSSISGTKQEIFQVELNLQNASSDHQGNDKTYHCKGLLPPPERLTAEVLGIICIVLMATVLKTIVLIPCIGVLEQNNFSLNRRMQKACDCGHCPEEWITYSNSCYYIGKERRTWEEGVCWPVLQRTLICFL | Function: May play a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 18034
Sequence Length: 158
Subcellular Location: Membrane
|
P44585 | MRCFRLSRHFIVYLFSLCAILLLAGCVQSRGGFVSKNHVVLAEQNPNTHFEQEVMIVRLSQVLLVGKMSNEERASLHFERGVLYDSLGLWGLARYDLTQALALQPKMASVYNYLGLYLLLEEDYDGALDAFNTVFELDSGYDYTHLNRGLNFYYVGRYHLAQQDFLQFYQADKKDPYRVLWLYLNEQKLKPQEAQTNLVERAKGLSEDFWGTHIVQYYLGHISVEELQQRASEFAENSQQYAEILTETYFYLAKQKLNVGLVDEAAALFKLAMANQVYNFVEYRFAAFELMKLKPVQTEDEKEEKSAVTKAIVF | Function: May be involved in cell division.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36434
Sequence Length: 314
Subcellular Location: Cell membrane
|
Q9LTR9 | MADNNSPPGSVEQKADQIVEANPLVKDDTSLETIVRRFQDSMSEAKTHKFWETQPVGQFKDIGDTSLPEGPIEPATPLSEVKQEPYNLPSVYEWTTCDMNSDDMCSEVYNLLKNNYVEDDENMFRFNYSKEFLRWALRPPGYYQSWHIGVRAKTSKKLVAFISGVPARIRVRDEVVKMAEINFLCVHKKLRSKRLAPVMIKEVTRRVHLENIWQAAYTAGVILPTPITTCQYWHRSLNPKKLIDVGFSRLGARMTMSRTIKLYKLPDAPITPGFRKMEPRDVPAVTRLLRNYLSQFGVATDFDENDVEHWLLPREDVVDS... | Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Can also use decanoyl-CoA and lauroyl-CoA as substrates.
Catalytic Activity: N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]
Sequence Mass (Da): 49799
Sequence Length: 434
Subc... |
P30419 | MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTM... | Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins . Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' . Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase ... |
O70310 | MADESETAVKLPAPSLPLMMEGNGNGHEHCSDCENEEDNSHNRSGLSPANDTGAKKKKKKQKKKKEKGSDMESTQDQPVKMTSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTM... | Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins . Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (By similarity). Lysine myristoylation is required to maintain ARF6 on membranes dur... |
P36597 | MSTNKITFLTNWEATPYHLPIFLAQTRGYYEREGIEVAILEPTNPSDVTALIGSGKVDMGLKAMIHTLAAKARGYPVTSFGSLLNEPFTGLITLKGNGINDFKDIKGKRIGYVGEFGKIQLDDLCSKFGLSPSDYTAIRCGMNIAPAIINGEIDGGIGIECMQQVELERWCVSQGRPRSDVQMLRIDRLANLGCCCFCTILYIAHDEFIAKHPDKIKAFLRAIHSATLDMLKDPVQTYKEYIHFKREMGSELHREQFERCFAYFSHDISNVPRDWNKVTNYSKRLGIIPQDFEPNCTNGYLTWELDPDEKDPMGKQEAIA... | Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. ... |
E2QUI9 | MAARAGPRAALAGAAAVALLSAALVLYELPPGAVLQRAFSLHKAHSVEDMENTLQLVRNIIPPLTTKKHKGQDGRIGVVGGCQEYTGAPYFAAISAHKVGADLSHVFCTREAAPVIKSYSPELIVHPVLDSPSAVHDVEEWLPRLHALVVGPGLGRDNILLENVKGILEASKARDIPVIIDADGLWLIAQHPALIQSYQKAVLTPNHVEFNRLSEAVLSHQVDGSDHHEAVRRLSQALGNVTVVQKGERDVISDGKQVLECTQEGSSRRCGGQGDLLSGTLGVLVHWALHAAPEKTNGSSPLLLAALGACSLTRQCSLQA... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0RU82 | MAARMIGEDDVRKFVPSRRRDSRKGENGKVLVVGGSYIYHGAPIFSSVAALRSGCDLVYTAVPKINAPATRAASPSMIVIPLADQKLTRGAARKLAGQIPTGLDSATIGMGLAIAERSALKVLVVALVDMDVRISLDAGALVREILGDISGKNCLVTPHAGEFKRLFGESPPADIEGRASMVERLAQEHGITILLKGPTDVISDGNRTLLNDRGAPAMTVGGTGDVLSGIAAGILARNRSPLESAAAAAYINGLAGEAAQEMHGLHITAMDLCELLPSVMKPFDRLE | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
F6RCC2 | MSTILFYTRALIIGATKSQGVFGKTGTLVANISSNRGIISIVPRTNPPQKLLKMQEEENSLLEEARKVVPALSFGKHKGQAGRVGVIGGSEEYTGAPYFAAISAMKAGADLAHVFCSKSASTVIKSYSPELIVHPLLDVPNAVTLLDEWLPRIHSHVIGPGLGRVDATLNTVKEILIKLKKQEIPIVIDADGLFLITRDPSIIHGYTKAILTPNVVEFQRLSKSMNLNWESKDLNGSIMETVALSKALGGVTIVRKGEVDIVAAGDEVVTMDEIGSPRRCGGQGDLLSGVMALFSYWTHNSTCTPPPTLLAGYAACFLTK... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A8N8Z0 | MPIPRTIIEQIKRIIPPLDGSLHKGQSGRVGVLGGALDYTGAPFFAAFSALRFGVDLSHVICAPTAAGAIKSYSPDLIVHPILNESSSVDKVKSELQSLLSRLHVLVVGPGLGREPYMQSYARLAISLVRERGMYLVLDADALFLVGHDLSIIKGYRRAVLTPNVVEFKRLSEQVGVDPDAPPDERAGVVSRMLGGVTVLQKGAKDIISVDTTGEEADLSASHIEGADAEKEKIKETIAVDVEGGLKRCGGQGDVLSGCVGTFMAWGKCYESGVYGDGTVPTSRVPLLAAVAGSMVTRTTSRRAYAKSGRSLITQDLLSE... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q5K8L4 | MASKQHAHILSLARSMIPPLHPKLHKGQAGRIGVLGGSGDYSGAPYFSSMGAMRFGADLAHVICEPSAGAVIKTYSPDLIVHTILDPQKSREDIRSALKGVMSRLHVLIIGPGLGRDDHMQSCAKIAFELAKDMEQMGVVVDADGLWLVQNEPKVVMDWPGVPRIILTPNVMEFKRLCDTMVGARTVLHLSPSTLINYQKINASGPHTSLCPQLATALGNATIIQKGPSDIISNGLKIPSALLSDESEEQNYLEVKVEGGLKRVGGQGDILSGSTGVLLAWGSEWVRGTYEHVGHPPPQDKAIAENIPVLAAYGASTFNR... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q54FJ9 | MTHLIDLFKPMIPSLLNNLHKGQSGRIAIMGGSKEYTGAPFFSGISSLKIGSDICHIFAPTEGGTATALKTMSPDLIVHPIEKNDPSDIIPWLLSLHVIVVGPGLGRSSGAWSCASEVIKAARNINLPIVLDGDALRLICDNLDIIKGYDKAILTPNFVEFKSLSDSVKKMIGDTSNNLLKPEHIASCLGNITIVQKGKEDIITDGNQTVVCDDEGMPRRCGGQGDILAGTVGTMYAWSQLYYKYNSNTDDKPEYPISIISAYAACSLLRHCSKKAYQISKRSTVSMDIINQISNGFEDLFPESSK | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q9VVW8 | MAAVSDIPVHLPKLLALFKTVVPKLVNNKHKGQYGRIGVIGGSLEYTGAPYFAAISSIRVGADLAHVFCHSNASAIIKSYSPDLIVHPVLDCVDAVERIAPWLERLHVVVIGPGLGREPGILKTASNVLKLCMDTKKPVVIDADGLFLLNDNLNLICGQPNVILTPNVMEFQRLFGEDDQAARQKMSLLGAGVTVLEKGANDKIYLPHCNEVHSMPSGGSGRRCGGQGDLLSGSLATFFSWSLQSGEPNPALVAACASSYFVKKLNAAAFQKFGRSLLASDMVNQIPSVFQTEFENSDPQ | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q5B0D6 | MANVHHISVPSKVLFQKARKLVPPMLEKFHKGQQGRVAVIGGSLDYTGAPYFSAMASARLGCDLSHVICESSAATVIKSYSPNLMVHPILPSSASVKDPSSIDAPSLASPIIAMLGRLHALVIGPGLGRDGVTLKVVTEVMKEARSRSIPFVLDADGLLLVTENPDLVKGYKDCILTPNVNEFSRLAKALNIEVPSLAQISSKESGDKTSKEAEACEKLSQALGGVTIIQKGPHDVISNGVTSIVSDLPGGLKRSGGQGDTLTGSLGTLLAWRAAYHDALWDSGEQEHSKEAENKEEVQGELESNKRMSPSTTLLLAAWA... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q833Y3 | MRYLSKDILEEVITQRPSDSYKSNFGRVVLIGGNRQYGGAIIMSTEACINSGAGLTTVITDVKNHGPLHARCPEAMVVGFEETVLLTNVVEQADVILIGPGLGLDATAQQILKMVLAQHQKQQWLIIDGSAITLFSQGNFSLTYPEKVVFTPHQMEWQRLSHLPIEQQTLANNQRQQAKLGSTIVLKSHRTTIFHAGEPFQNTGGNPGMATGGTGDTLAGIIAGFLAQFKPTIETIAGAVYLHSLIGDDLAKTDYVVLPTKISQALPTYMKKYAQPHTAPDSELLEQKRSR | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
C4LZV8 | MGGQLSIEARLKSIIPQLTFDSHKGACGKVAIIGGSVEYTGAPYFSGISALRVGCDLAHIFCHQDAAIAIKSYSPELIVHPFFKEDYDTNEVLKWLDTVQALVVGPGLGRDESVMEATLSILKQAITKNIIIILDADGLFLINNHLDLIRGKKNIILTPNVMEYRRLCDVLKVSHNTPCNKVALMLGGVTILQKGQVDEVSNGSYTVHVKHVGSPRRCGGQGDVLSGSLATFVAWSKLNQDFQDEDLICCSVAASALVKECSSFAFTEKHRGVIASDIIESIPSVFDQVFGQNKIQLIYE | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A6GXW4 | MRDFCQIDTQEIIKRYKPIDKYTHKGLQGHALIIGGSYGKMGSVVLASKACIRSGAGLVTAYIPKCGCDIVQISVPEVMVITDDYLEHIALINFDLNLKSIGIGVGMGQHPDTQHAFFNFLKSNKLPLVIDADALNILSQNIEWLSLLPKKAILTPHQKELERLIGKWSSEEEKLEKVKRLCLEYDLIFVLKGAPTMIVNNKSTYENTTGNQALATAGSGDVLAGIITSLLAQSYEPINAAIIGVYLHGLTADIAYPKVGYQSFIASDIIETLGEAYLHIIK | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
C7YKN8 | MSTEDLNMSAATKNVLAKVRRIIPPMLESFHKGQLGRVAVIGGSENYTGAPYFSAMASARLGCDMSHVICTPAAATVIKSYSPNLMVHPLMRQSPAPNPNQDPATRDTSKDPDSDPEHISAQIIDLLPRLHVLVVGPGLGRDPLMHATVARVIRAARNRGTPVVLDADALILVQKDPGLVRGYDGAVLTPNVVEFAKLCEALKVDVSEGASETARVEALAKTLEGVTVIQKGAKDYISNGETTLTVDLQGGRKRSGGQGDTLTGSIATFLGWRKAYLDRLWDVGQNALGEHELVGLAAFGGAAITRECSRLAFAKKGRSL... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
D3BMU4 | MFCIIHFGNPKNDKFLGSSTLYSQKLKTNNIKILCLQVFYYNIYESTNNNNNNKNKNKTLLLNNIRTYSTLSKGALSTTTTATTKKMSMDDSFELPTNLNHFLSYVPSLEYHMHKGQCGRIGVFGGSAEYTGAPFFAGITSLRLGADIVHIFAPSEGGTATAIKTLSPELIVHPLDQQMDPSTIIPWLLSIHVLIIGPGLGRSSIAWKSAKEVIKAARNINLPMVLDGDALRLICEDLELVKGYDKVILTPNFVEYRALSDAAKKLNNDNSNNILSPSDLAKALGNVVIVQKGQEDIITDGTISYSCDKAGMPRRCGGQG... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q8IW45 | MVTRAGAGTAVAGAVVVALLSAALALYGPPLDAVLERAFSLRKAHSIKDMENTLQLVRNIIPPLSSTKHKGQDGRIGVVGGCQEYTGAPYFAAISALKVGADLSHVFCASAAAPVIKAYSPELIVHPVLDSPNAVHEVEKWLPRLHALVVGPGLGRDDALLRNVQGILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVLRGPMDSDDSHGSVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSSRRCGGQGDLLSGSLGVLVHWALLAGPQKTNGSSPLLVAAFGACSLTRQCNHQA... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
B7PBI5 | MVPHVPEGCSVQQQLVCSVIPPLNSERRKGQAGRVGIVGGSAEYTGAPYFAAMAALRTGADLVHVFCHPSAATAIKAYSPELIVHPTLDAAVTCLPRLHAVVVGPGLGRDVEASWMPTLFNRIREQGLPVVVDADGLFYVTQNPDLVRGYSRAILTPNAVELDRLYRAVLGSPPRENAVPELARALGHVTVLAKGSEDIISDGHRLLRCTEQGSPRRCGGQGDLVSGSLALFAFWSHSAHDTPGEASKRQNSEYGPAMIAALGAAMLVRRCGRLAFQKMARSTLSSDMLAEVRTAFSMLFPVD | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q9CIU7 | MIELTDEILAKVIKKRKKASYKGTYGRLLVIGGNRQYGGAAILVTTSAVYSGAGLVSVALAKENHSALQARLPEAMTLDFDDLIKLREVAKAADVIVIGPGLGLERLDLLTEVLNLLTENQKLVIDGSALTLFAREHLDLPFPENTVFTPHEMELERLSGLKIGQQTKEEVQDFVNQLGAIVVAKSSETRIFAPNRESFILKIGSPAQATGGMGDTLAGMVGGFLAQFHGETEEVVAAATYLHSLIASVLARKTYVVLPSRLIEEIPLFMKKYEC | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
F9UN92 | MQPITTEIVSRTIIKRPADSHKGNYGRIMLIGGNQNFGGAIIMAATAATYSGAGLVTVATDPSNFTSLHARLPEAMVIDYHQTDTLLNLLAGMDVIVIGPGLGTDTVADQLLTAVLAATHVPQRLVIDGSALTLLAQQARPLPATDIVVTPHQMEWQRLSGIAIKDQTPTANHDAQQRLGVMAVVKAHRTTVYTDERVWFNPGGTPAMATGGMGDTLAGMIGGFVSQFHNFTDAVLSAVYLHSAIADDLAATRYVVLPHQISTRIPTYMHRFSQIERP | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q8NSS3 | MKPVFSVDQIRRAENTLFELQADPDELMISAASAVADVALAMVDGPAPAVSSEESILLLVGPGGNGGDALYAGAFLAEEGHHVDALLLGNGKVHQSALAYYESLGGQIISDFPPHYLYRLVIDGLFGIGGRGGLTPELASLVESFSASGIPILAIDVPSGVHADSGELPPGVMVTVEGFDNDAPMARQKIPAHIDADVTITFGGLRRAHAVSPACGEVLCADINIAGGGGKSLSAELSQVQAEDATPQMFASKAYQRKDSLFERANLKATAPHIHRIGQHFTVLNMEPGPDHDKYSGGIVGIVAGSGTYPGAAVLSVKAA... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q83CM5 | MTVLYQNRQIRELERLAVESGISEYELMCRAGEAAFKALLARWPEAQEITVCCGKGNNGGDGLVLARLAYENGLKVTVYLAGQRHQLKGAAAQAANACEASNLPILPFPEPLLFKGEVIVDALLGSGLSGEVKAPYDHLIAAINQAGQYVLALDVPSGINVDSGEVQGTAVKANLTVTFIAPKRGLYTDKAPAYCGELIVDRLGLSESFFRAVFTDTRLLEWKGVFPLLPKRARDAHKGSYGHVLVIGGDYGMGGAVRMAAEAAARVGAGLVTVATRPEHVPIVSGPRPELMCHQVAAADDLKPLLTAATVVVIGPGLGK... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
B8E2P6 | MKLVTSEEIKRLEERLEREYSIPPILLMENAASFLFSFLKEKFEDIENRKIAILCGPGNNGGDGVALARYLYSNGIRKITIFSYLWGKKISDLLKIQLGLLKNLVEIKDILQDYTELKEYELIVDGIFGIGLKREIDDDLKKIFRYINNLGKKIISIDIPSGINSDTGEIMGEALRADYVLTMFLPKVGLFETGAVDYVGEVIVGRLGIPIEIVNDIVESNIHLVDWELLKDIVRIPSKGVHKGKKGKVLIIGGSFRYTGAPILSALSALRTGAGMVYLAVPEKISMVYRGNYPEIIYIPLKDKDGYISYDNLGYILEII... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
P31806 | MTDHTMKKNPVSIPHTVWYADDIRRGEREAADVLGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKAVGIEVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVDLIVDALLGTGLRQAPRESISQLIDHANSHPAPIVAVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEW... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q7NIE6 | MSGLCACTLVGAAQVQQLEAALFAAGMPVEALMEKAGLRLAAAIAADYPAGGYPRVGVLVGPGHNGGDALVVARELWLVGRSVQVFCPRPPIKPLARAHLDYFQSLGGRVHTGAVPEEPGVDLWVDGLFGFGLERPVAEPYAGLMAQVNASGVPVAAVDLPSGLSSETGEALGGLAVRAARTYCLGLWKRGLWQDAALDWLGVPVRLEIGFSEAQVRSVLGEDHRSARLLLPDAARAGLPLARPATAHKYSVGTLLAVAGSRQYGGAATLVALGARSGGPGMLYLALPESLADRVAARLPEAIVHPCPQAENGALADLPG... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
P56176 | MLSVYEKVNALDKRAIEELFLSEDILMENAAMALERAVLQNASLGAKVIILCGSGDNGGDGYALARRLVGRFKTLVFEMKLAKSPMCQLQQERAKKAGVVIKAYEENALNQNLECDVLIDCVIGSHFKGKLEPFLNFESLSQKARFKIACDIPSGIDSKGRVDKGAFKADLTISMGAIKSCLLSDRAKDYVGELKVGHLGVFNQIYEIPTDTFLLEKSDLKLPLRDRKNAHKGDYGHAHVLLGKHSGAGLLSALSALSFGSGVVSVQALECEITSNNKPLELVFCENFPNLLSAFALGMGLENIPKDFNKWLELAPCVLD... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A2BLC0 | MLGRPVFGLGKAITSVDVAVIDANSEWIGVKRLQLMENAGRSVAEEAAKLAKPGSRVVVFAGPGGNGGDGLVAARHLAYMGYQVTVVMIVKPEEIRSPETRAMYEALAAMDLTVDIRIARAPADVAPVEADVVIDALLGTGLRGAPRPPYSDAIEAVNSSTGLKLAVDVPSGLNSDTGETPGAYVKADITVTFHKPKPGLLRRPDVAGRLVVVSIGAPPEAEVYVGPGDVAYRVRPRSWKAHKGSSGRVLIVGGSQDYVGAPILAALAAERSGVDLVFLAAPEHVTRAASHHPTIIPVPLRGSPNIHPDHVKKLEQLLDR... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
B1L3W1 | MKVCSVEEIRELDSLASEKYGIDQEILMENAGLAVTYLIEREFGVEGKKFSVFAGPGNNGGDAFVVARQLHSRGGIVRVLLLSDPSKYKGPALSNYKRIEGLIEIIGADDIKGAVEWADAIVDGIFGTGLSKDVEGIFKEAIESINSSGKPVFSIDIPSGINGDDAMPRGVAVRATYTVTFGLPKYGNILYPGFSYCGRLLVSPISYPPEECSKIMVELNDPIELPERVRWGHKGSFGKFLAVSGSRNYYGAPYFTALSFLKAGGGYSRLAAPKSIIPFIASKASEVVYIPLEENDQGSISLNNFDLIVRMAEEQDVVAL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q4QFL5 | MLSRLSERCTIATGLEQVLRHYVWSAAWLRDAEPAAAASENIDLSGLMERAGRAAYDVFANLYTSQKHWLILVGSGNNGGDGYVIARHAREAGKIVTVLRMPHSKPLPTEAASAQHAWKAVGGTESTMSPGAPLQLPADVDLIVDGLLGTGICGPPREQYADVIRHINGLPVPRVAIDIPSGLNAETGEAAGACVKADHTATFICLKPGLLTGQAKDYVGQLHYRSLGLEDWMTAPERMRVALCRRVALDDVYEYFGIRRSALAHKGSCGKAILVGGDHGFGGAALMSAEACVTVGAGLTRVLTRPEYAAPLLTRCPEAM... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q2FT57 | MTVIIQGRSFPDDLTQYAEFIGQGLLSPEEMRRIDQNAQALGISGLELMESAGTGLAMAARQYQPGKILILCGSGNNGGDGMVAARHLAGEADITVFWYDSGRQTDSTRTQLQRLLSCSVTSIPFRSRDDLIEHTRIFQDTDLIIDALLGTGGTGSVREPVRTCIEFANNAKAPILSADLPSPGIIPDRICAFHRAKTEGAHIYGIGIPLLAEISTGPGDLLILRNRNPDSHKGVGGNILVIGGGPYQGAPYLAGLAALRAGADIVRVVSPHYLPEPDIIHVPTAGDRITTADLATIIPLCKQADVVLCGPGLGPESHDV... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q58981 | MRRDINNFLFGERMELFEILKQKIKEKEVITPKEMAIIDDNAEFLGIQKILLMENAGKAVYEEIKDIDAEEFIIFCGTGNNGGDGFVVARHLGKGDVILIGKESEIKTYEARENFKILKNLAEFGNIRIREIKWAEEVNDIFERLKNKKAVIIDAMIGTGVKGELREPFKTIVDKINELKQINKNIFVISVDVETGHLESDLTITFHKRKTINKDNAIVKKIGIPKEAEYIVGWGDLKALRKRDSNSHKGQNGKVLIIGGSKDFYGAPILAGLAALKIVDLVGILSVGKVIDKVNHPEFIMYRVEGDYLSSQHVDYTLEI... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q8TX67 | MFITSKEMRRIELNSRWLGFEEDFMMENAGAGVARVVIGEYSPNDVLVVCGTGGNGGDGFVTARHLDSEGVDVDVLLVGRREAIKNEAAELNLRRLDRAGIPVQEVRDSEDLESVDFERDVVVDALLGFGIRGRLREPVRSAVLRINEASRAGTRVVSIDIPTGLDPDSGETPDVAVEADLVVSIHRHKRGVRKLRDVFLRRVNAGIPEIAERICGPGDLITSDIWRRDPWSHKGQHGRVLIIGGSRKYVGAPQLAARGALRAGVDLVFLLTVDAVPKNDPNVIYRAVPAERLEPEHLDEVDLEGVDTVVVGPGLGADAD... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
O27324 | MMRCGEGYPGLILAKEDFIMKPVDMAAADINAEYLGVPRLSLMENAGRAVAEEIGNAVDSGRVAIFCGPGGNGGDGFVAARHLLNMGFEVEVHLLGHPERIGSEEALVNWGVLGAMQPHPGGFSVDFVRDSSEIKPTDADVVVDAILGTGVRGSIREPSRSAIEIINRSEAFRVSVDIPSGLNPETGAVEDIAVSADLTVTFHRMKDGLKLADPAVTGEIVVRDIGIPPAAEIFMGPGDLLRIPSRRPGSHKGENGRVLIIGGSRQYSGAPAIAAKAALRAGADIVMVAAPGSAARAIRSLSPDLIVRELEGGYIGMESL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
Q2RGI2 | MYLVTAAEMGQLDRLASSEYMIPSIVLMENAGLRVVESIERHFQGQVANRRILIFCGKGNNGGDGLVVARHLLNRGAEVKVFLLARPEDIRGDARTNLEIYQKMGGKLLLLLGESHLQRADIALLYADLVVDAIFGTGFKGAAMGLPAAVINMINKAHRETVAVDLPSGLEADTGRCFGPCIQATWTVTFALPKLGLVVEPGASLTGRLEVADIGIPQKLVATQHFNRRLLTAAWCRSQLPRREASGHKGLYGRVLAVGGSPGLTGAITLAATAALKAGAGLVTAAVPRGVQGILAMKTTEIMTMSLPETPAGALSRDAL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
P37391 | MRHYYSVAAIRDAEASLLASLPDGVLMKRAAYGLASVIIRELAVRTGGVTGRRVCAVVGSGDNGGDALWAATFLRRRGAAADAVLLNPDRVHRKALVAFRKAGGRIVENVSAATDLVIDGVVGISGSGPLRPAAAAVFATVSASGVPVVAVDLPSGIDVVTGVINGPAVHAALTVTFGGLKPVHALADCGDVTLVDIGLDLPDSDILGLQAADVAAYWPVPGVHDDKYTQGVTGVLAGSSTYPGAAVLCTGAAVAATSGMVRYAGSAYTQVLAHWPEVIASATPTAAGRVQSWVVGPGLGIDATATAALWFALETDLPVL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
P9WF10 | MRHYYSVDTIRAAEAPLLASLPDGALMRRAAFGLATEIGRELTARTGGVVGRRVCAVVGSGDNGGDALWAATFLRRRGAAADAVLLNPDRTHRKALAAFTKSGGRLVESVSAATDLVIDGVVGISGSGPLRPAAAQVFAAVQAAAIPVVAVDIPSGIDVATGAITGPAVHAALTVTFGGLKPVHALADCGRVVLVDIGLDLAHTDVLGFEATDVAARWPVPGPRDDKYTQGVTGVLAGSSTYPGAAVLCTGAAVAATSGMVRYAGTAHAEVLAHWPEVIASPTPAAAGRVQAWVVGPGLGTDEAGAAALWFALDTDLPVL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A2I6PIZ6 | MDSTGRQPLSQDGQPWQALASGLGFPDEDQKYWWSVMAPLLGELMKWANYPVDKQYLVLAFCHEYILPFCGPRPTAEGGIFWPTLITKDGTPFEPSLNFYKNKATLRVGYAPACELSGSNDDPINQRAPIAALEHQKRVLPQQNLKWVDNFKKAWFIDNDDAVALKARVHNELFEQAAVQCLIGYVFSDYTQVKVAMSPLWKSVQTGQQISRVIWDTFRQLGDDASSYLDCLSVLEEYTESKQAKLAQVQPSFVNFDVNLKGDYQQSRLKVYYATPCTAFDTMVQVFTLGGRLKGPEVDHAIECLRVLWPSVLAVPENHP... | Function: Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feed... |
Q52527 | MSETFTKGMARNIYFGGSVFFFLVFLGLTYHTEQTFPERTNESEMTEAVVRGKEVWENNNCIGCHSLLGEGAYFAPELGNVFVRRGGEETFKPFLHAWMKAQPLGAPGRRAMPQFNLSEQQVDDMAEFLKWTSKIDTNDWPPNKEG | Function: Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16639
Sequence Length: 146
Subcellular Location: Cell membrane
|
Q8L4H4 | MMELQVIRIFRLVVAFVLCLCIFIRSASSATKGFESIACCADSNYTDPKTTLTYTTDHIWFSDKRSCRQIPEILFSHRSNKNVRKFEIYEGKRCYNLPTVKDQVYLIRGIFPFDSLNSSFYVSIGVTELGELRSSRLEDLEIEGVFRATKDYIDFCLLKEDVNPFISQIELRPLPEEYLHGFGTSVLKLISRNNLGDTNDDIRFPDDQNDRIWKRKETSTPTSALPLSFNVSNVDLKDSVTPPLQVLQTALTHPERLEFVHDGLETDDYEYSVFLHFLELNGTVRAGQRVFDIYLNNEIKKEKFDVLAGGSKNSYTALNI... | Function: Involved in the perception of symbiotic fungi and bacteria. Part of the perception/transduction system leading to nodulation or mycorrhizal infection . Phosphorylates PUB1 .
PTM: Autophosphorylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-ph... |
Q6FEY7 | MAKVAGFRFELKQLFHLMWPILITQFAQAGLGLIDTIMAGHLSANDLAAIAVGVGLWMPVMLLFSAIMIATTPLVAEAKGARTPEHIPVIVRQSLWVAVSLGVIAMLILQLMPFLLPILGVPESLQPKAGLFLHAIGFGMPAVTMYAALRGYSEALGYPRPVTVISLLALVVLVPLNYIFMYGIGPVPHLGSAGCGFATAILQWLMLITLASYIYRAKAYQSTQVFSHWERINLTLVKRILKLGLPIGLAVFFEVSIFSTGAIVLSPLGDTLVAAHQIAMSVTSQLFMIPMSLAIALTIRVGMYYGEKNWVSMRLVQKLG... | Function: Multidrug efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49013
Sequence Length: 449
Subcellular Location: Cell inner membrane
|
Q8UDF5 | MSSSVVAETVPSGSGSWFSHFKATLVLGIPLIGAQLAQLGIHTTDMVIVGQLGAEKLAAMVLAGQFFFVVFIFGSGFSVAVVPMVAQAYGQGDATSARRSLRMGMWVAIAYWLLALPIFFNAERILVYLGQNPNVAALTGHYLAIAKFGLLPALLFYVLRGLVSAIGRAGIILYVTIIMLVMNGLMAYVLVFGHFGLPAMGMNGAAVVAVIVNAFSFIFIVAYVQTREETKKYELFVRFWRPDWHALFEVLRLGLPISITILAEVTLFAAASILMGQIGTVQLAAHGIALQLASIAFMIPLGLSQAATVRVGVARGQGDF... | Function: Multidrug efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49726
Sequence Length: 465
Subcellular Location: Cell inner membrane
|
Q5NYX9 | MSAPILFPLSAPESSFTIAGRLFHHAWPVLVAQLLSMSMLIADTVITGRYGTLDLAAVAVGSGVYISIVMLLVGVLQAVAPTVAHHFGARRVDAIGPALQQGFWLALMLALPGIALLAFPGFLLELSSVPADVAGKTRDYLLATAFGLPAVLLYRTFYAFNNALGRPRALMMISFIVTSTHIPLAWALVHGAFGLPPLGAIGCGISTAIVNWIAFACGAGYLAHNRDYRPYRLFANWQPPRRRDLLALLKLGIPMGLSTFIEVSSFTLIALFAARLGAEAVAGHRVVANLAALIYMLPLAISIAILVLVGQAAGAREPAR... | Function: Multidrug efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49428
Sequence Length: 463
Subcellular Location: Cell inner membrane
|
A0KEJ2 | MSTTTQSDAGISREIVVIGSGFAAQQLVKSLRKLDAEQPIRLITADSGDEYNKPDLSHVVSRGCAAAAMTRQSGSDFAEQQRIALLPHCPVLGIDPVRRLVLTEQGEFPYGQLVLATGASAVRPELPGSEHLVTLNSQQEYAAVEGAIQQARRILVLGAGLIGCELAMDMASDGREVTLLDLADSPLSALLPATLTQPLQQALRSQGVSLQFGTGLARIDGQPGDGWRVTLTDGRTSEQDLVIAAIGLRPNLALARGAGLAVERGILVGDRLQTSDPHIFALGDCVQWQGQLLPFLQPIVLGANALARTLLGTPTPLALP... | Function: One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [nitric oxide reductase rubredoxin domain] = NADH + 2 oxidized [nitric oxide reductase rubredoxin domain]
Sequence Mass (Da): 41275
Seq... |
Q5E3X0 | MSLPIVIIGSGFASYQLIKTIRRTNNDCPIHVFTNDSGDDYNKPDLSHVFSKQQSPEEVVTLSGGDFAEQYNVILHRHTWVESIDTEIQAITANGEQYAYGKLVLATGSQTFIPPFHGDGCGDILTLNSLKEFAGIQQKVLESKKVLVVGGGLIGTELAMDLANAGKMVTLVEPNTHLLANMVPDFISLPLEKACKEKGITVNLSDCVQAVNKQEQGYRVTTSNGHSYYVDCVISAAGLKPNTKLATEANLMVNRGIVVDLNLQTSANNIYALGDCAEIEGKVMAYLQPILLSANALAKTLLGTDTALSMPNMMVKVKTP... | Function: One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [nitric oxide reductase rubredoxin domain] = NADH + 2 oxidized [nitric oxide reductase rubredoxin domain]
Sequence Mass (Da): 41392
Seq... |
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