ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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A7HZF9 | MRISIKKILDNESTAGIFLLAAAVFALIFSNVGFLHDIYRHFLELPIVIGVSDYKLDKPLEFWVNDALMAIFFFSIGLELKRERIEGQLRHFSQVFLPSFAAIGGVIFPAVIFAVINFSDSHALRGWAIPTATDIAFAVGVMALLGRRIPTSLKIFVLTLAIMDDLCAIVIIALFYSTALNFTYLGLAFVCFLVLLVMCKLKIPQKIPFVIMSILLWIFVLHSGIHATIAGVAAGFCIPINTSRGNSMLKEMESSLGYFVNYVVLPLFAFANAGVDMRGMQISYLFGPVPLGVMLGLFLGKQLGIFTFSWFLIKMNIVGMPDRANFKQLYAVAIICGIGFTMALFVDNLSYGGSDLYHHTDKLAILLGSIISGVVGYFVAKAVGNKPKKGIKNEYN | 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 | MISPNPALPTPPHAPTAPGRGARLSRFLSRDTTGGILLLIATVLALVIANSPAADLYERVRGFTFGPEALHLDLSVSAWAADGLLAIFFFVVGLELKQEFVAGSLRDPRVAALPIAAAAGRVIVPAGIFTLINLGAGPEALRGWAIPAATDIAFAVAVVAVVGRRLPPVLRTFLLTLAVVDDLLAITIIAVFYTAGIAFVPLLLASVPLAVFGILVQRGVRAWYVLIPLGVAAWALVHASGIHATIAGVALGLLVPAIATARAGVTHRGTAGREERHALTHFFAERWSPISSGIAVPVFAFFSAGVTVGGLEGLTSSLTDSVAVGIIVALVIGKAAGITGASLLVARLPGIRLDPTLRWPDVLGLSFVAGIGFTVSLLVGELAYGTGSAQDDAVKVGVLIGLLTSAVIGGTLLALRGRWHAAASLHEPVPAAVR | 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 | MTIRRPGGACLFGLLLAVSPTPFPRRTTLTPIRTLLTPFGEFFKGQASSGLVLILAAVLAFAWANSPWRESYFTLRELPLTLSLGSWTLSHGLYWWVNDLLMALFFLLVGLEIKRELRVGELRHPRQASLALFAALGGMLLPAGLYTLVNAGGPGAAGWGVPMATDIAFALGVLALLGDRVSPGLKVLLAALAILDDLGAVLVIALFYTSGLNLLALGLMGAVWALGLGLNAAGVRHLGPYAVLGAALWLTTLASGLHPTVAGVLLALTIPLGRRAEQEDAEPSPLHRLEHGLHPWSAFLILPLFALFNAGVSVAGGSLDRVTLGVVLGLIIGKPLGVVAFAWLAVQLRAASLPEDVTWPGMLGLGLLAGIGFTMALFIGGLAFPEGALLNAAKLGILTASVLAALAAITVLTRAFPRQPR | 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 | MVDPIRSPLSRAFAPVRALFVSDASAGILLILVAAAAMIVANSPLAGAYEEMFYGDLAWTPIAKLDDLHLWINDGLMAIFFFVVGLEVKRELICGQLSSPEQRTLPVLAAIAGMAVPAIVYVGVVGTDSALVRGWAIPAATDIAFAMGVLGLLGSRVPASLRLFLLTVAIVDDIGAVLVIAAFYTANLKVMWLVIALGIFGVMVGMNKFGVDRIWPYILVALVLWVAVLFSGVHATIAGVMAALTIPMRRKDGHSLLEKLEHGLAPWSAYLVVPIFGFANAGVNLSGMGLDAVLAPLPLAIAAGLVVGKQLGIFGIIVAAVKLGIAKAPANANWIEIWGVSILTGIGFTMSLFISGLAFTDSRLLIDEAKIGILGGSLISAILGYTILRLTTTHPEERPPQTVTP | 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 | MKLTKTFKAFFENEKSGGLLLLFVTVISLWAANSSYSAGYIAFWEKDLAGHSITHWINDGLMTIFFLLIGLELEREIYHGELSNIKNASLPIMAAFGGMLIPAATFLALNFGTSTQNGAGIPMATDIAFAIGILSLLGDKVPASLKVFLTALAVIDDLGAIIVIAVFYTTSIGFVNLAIALGIWVFLFVLNRMKVYNLIPYLIGGVIMWYFMLNSGIHATITGVILAFVIPFGDGGEKSTSYKLQHFLHQPVAFFILPLFAIANTCIAIESNWHIGLNHPNAFGIILGLVIGKPLGILLFSSIGVSAGLCALPKNLKWAHILGAGMLGGIGFTMSIFITLLAFKDPEIIVFSKIAIIIASIISGITGFVYLRYILTTNKNT | 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 | MSEAKITPSRHSYVKDRLQDSLNRFIKHESFGGVLLAFCVGAAMLVANSSYADMYFTFFHSEFGAFFSDSHFKVSLQDFINDVLMSFFFLLVGLEMKREMLYGELAGFKKVSFSFLAAFGGIICPVMIYSYFNSGTAYESGFGVAMSTDTAFALGLIMLLGDRVPKILKIFLVTLAVADDLGAISVIAIFYSDNINMQWIYASLILVAVLIYLNYRDTKYLSLYFLAGILLWFCVHHSGIHVTIAAVILAMAIPGRTRVNKKYFINMLKEFERMKVATNDWNDVVYARESEKVGFWRGSFKNIRSFIFGNQDVEKKIDMAKTSQLVHMLDTIGTYSRYAQNPLIRLEIALQPICAYFFVPLFAFANAGVTLEGNIDISLNSVMLGTILGLVVGKPVGVLLFCFLGEKLNLATRPKDLNYLHILSVGMISGIGFTMSMFVANLAYKDDIMSIDMSKISILVASSIAAVLGLLVVYLSTIKQDNQLENINEEDEIQKLKETQSII | 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 | MSALSSNRLPNRASLVTNRAFSALEGFLHVEAFSGIVLLLAAAAALIFANSQYASVYESLWHTPLGFNFGHFTLSWDLHFWVNDALMTVFFLVAGMEIRREIHEGALADFKQAILPIVSAIGGVCFPALIYLSFNFNSEHTHGWAVPTATDIAFALGILALLGKKIPANLHVILLSLAIIDDIIAVLIIAFFYSTNIDPSGLAIAIAGIALVLFFQWIGLASAWLYILPGAIIWWGLMITGVHPSLTGVILGMMTPVFPTRTLVAPLTILSNAMQILQEKNIKTDLHHISTALKKMRKGQRDMIAPVIRVQKTLHPWVAYGVMPIFAFANAGVSFANFDLSSHESFLVVLSVVIGLFIGKPLGIITASYLAVKSGLCRLPPHMTWTGILLIGFLAGIGFTMSIFVSMLAFKDIVLLDSAKIGVLCGSGLSALAGLGYGLIYIKRNKNKKVLHNLNGIK | 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 | MATTAGAKKGLWSTIRRIAASDRISGLIMLGFALTGLVLANLPATAHAFETVAETHLFIPYTNLDLPIGHWAQDGLLTIFFLTVGLELKQELTTGSLANPKAAAVPMLCAVGGMIAPPILFLAVTALFSQIGPGEPGTLILTTTGSSIPFSEMSHGWAVPTATDIAFSLAVLALFAKALPGSIRAFLMTLATVDDLLAIILIAVFFSSINAWYWFIGIAVCAAIWAYLVRLKKVPWIAVGIVGILAWIMMFEAGVHPTLAGVLVGLLTPSREMHGELSPRAERYANKLQPFSALLALPIFALFATGVHFESMSPLLLASPLVIALIVALVVGKPLGIITTAWLSTHVGGLKMAKGLRVRDMIPAAVACGIGFTVSFLIASLAYKNAELSAEARFGVLVASLIAAAISGVLLSRQSKRFEKTAAAAAADEEDDESIDGDGIGQPSHTTEPTTPTEHPGTLADGTASVEIDFRH | 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 | MNHSPQSARPVSIMRRFLDSEAAGGITLMAAAALALIVANSPFAQTYFDALHLYIGPLSLAHWINDALMAIFFLLVGLEIKREMLDGQLASWPNRMLPGIAAAGGVILPAIIFAVLNHDNPAKLRGWAVPSATDIAFALGVLSLLGSRAPSSLKVFLATLAILDDLAAVVIIAIFYTAEISMPYLGAAFITAAVLFVMNRMDVVKLLPYLISAVILWFFVFNSGVHATVAGVVAALMIPLKPAPGRPDDMTSPLHKLEHALAKPVAFIVVPIFGFANAGISFKGLEASVLGDTLTLGILLGLFLGKQFGVFGAAWLAIKTGLAEKPMGASWVQLYGVAILCGIGFTMSIFIGLLSFPSDLMQTETKIGVLSGSALSAICGYLLLRAARPDQSAANPLWKADESPEAKNFGRFLCVFHFASYIASTYCTERLQAASSLLRRSSLEFALPGLLKRLIPRRFRAVETEIPVVRLHGAIMTGGTSLRPTLSLASTAGILEKAFADKHAPAVAISINSPGGAPVQSRLIYRRIRDLAAEHQKKVFVFVEDVAASGGYMIALAGDEIIADPSSIVGSIGVVSASFGFPELLKKIGVERRVYTAGSNKVTLDPFQPEKAEDIERLKALQLEIHATFIDMVKERRAGKLGDNPDLFSGLFWTGTTAASLGLIDGLGDMLSFLRKTYGDKVKLKLIQPQRGLLGRKLPGIGMDSGSVEPAQIAAHLGDGLLCVAEEKAIWARYGL | 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 | MLQRVRKLSLLRELLESGAAGGLLLMACAVLALFVANSPLAEGYFHALHVPFAGLDLLHWINDGLMAIFFLFVGLEIKREFLDGQLSTWANRALPCIAAAGGVVVPGLIYASLNAGSPETLRGWAIPTATDIAFALGVLSLLGSRVPTSLKIFLATLAIVDDLVAVLIIAVFYTAELNTAALMGAALVTLVLLGFNRLKVKRLAPYLVMGVALWWLVLLSGVHATIAGVVLAMTIPLHASKAAPDDATSPLHRLEHALSPWVAFLVVPIFGFANAGLSFAGMTPSVLAEPVTLGVALGLFFGKQIGVFGAAWLAIRLGVARLPVAASWAQLYGVSLLCGIGFTMSLFIGLLAFRDAALQNEVKVGVLVGSLSSALIGATLLSLTKRRLPAVDPSRDHQADATALDDLGREDAR | 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 | MGQSVRNQSTIGYIRETATKFLDRETAGGIFLIIATIVALLLANSQWAGAYHHFLGDELLFEFSEHLSFGLTIEEWINDGLMAIFFLVAGLELKREVMVGELSSIKKASAPLLAALGGMAVPALIFISLNLGTENIKGWGIPMATDIAYSLGIIGLLGKNVPRQLKTFLIALAIADDIGAILVIALFYSNELSWIYLGSGMGAFGLLLLMNWTGVKNLIWYIIIGIILWYCFLNSGIHPTIAGVLFAITIPIVPKLDSKILKERTATNVTNLEKTELEKLNPLQDKKQQIILKAIKTDTENSRPPLLKLENSLVDFNAFFIIPIFAVANAGVKLDVNLIEVVSGSLGLGILLGLAIGKVTGIGIFTLIGQKLGVSELHITLNWKHIIGIGMIAGIGFTMSLFITNLAFNDQELIKISKISILIASLLAAIGGAVILLLTSNKGRKNIVK | 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 | MTNIQAFMKNFLGASPEWYKLAIVVFLIINPIVFFFISPFIAGWLLVAEFIFTLAMALKCYPLQPGGLLAIEAIIIGMTNAKHVKAEIMANFEVILLLIFMVAGIFFMKQLLLYVFTKLLVKIRSKIALSIAFCFSAAFLSAFLDALTVVAVIISVAMGFYGVYHKVASGNNLIDAVDISDDRKIIEQQHEILEKFRAFLRSLMMHAGVGTALGGVMTVVGEPQNLIIAEQAKWNFMEFFLRMAPVTIPVFICGLLTCFLVEKFKLFGYGEKLPDEVWKILSDLDRTNSEKMSKQDKIKLGMQALIAIWLIVGLAFHLAAVGLIGLSIIIFATSFTGVTDEHTIGKAFQESLPFTALLVVFFSVVAVIIDQKLFSPIIHFVLSAEENTQLALFYLFNGLLSSISDNVFVATVYINEAKAALTNGVIAPHQFELLSVAINTGTNLPSVATPNGQAAFLFLLTSSISPLIRLSYGRMVYMALPYTIVLSIIGLLAIEFILPAATIWLASLGLILPI | 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 | MTSTTITPHHIGGAWTRTERRRLASVVGAIVILHVLGVALYLGYSGNPAAAGGLAGSGVLAYVLGVRHAFDADHIAAIDDTTRLMLLRGRRPVGVGFFFAMGHSTVVVVLALVVALGASALTTTELEGVQEIGGLVATVVAVTFLSIVAGLNSVVLRNLLCLSRQVRAGSDITGDLESRLSERGLFTRLLGNRWRGLVRSSWHMYPVGLLMGLGLETASEVTLLTLTASAATGGTLSIAAVLSLPLLFAAGMSTFDTADSLFMTRAYSWSYQDPQRRLNFNIATTGATVVIGLFVAGIYVCALLAHLPMFAALSPIGDISENFEFLGYAVAAAFILTWTGALLFNHLKPQRN | 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-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O-acetyltransferase activity (Probable).
PTM: Acetylated on Lys-214 and Lys-281. Deacetylated by CobB.
Catalytic Activity: acetyl-CoA + an arylamine = an N-acetylarylamine + CoA
Sequence Mass (Da): 32275
Sequence Length: 281
Subcellular Location: Cytoplasm
EC: 2.3.1.5
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P11067 | MELSVLGQNNGGQHSAGGCSSSSCGSTHDQLSHLPENIRAKVQNHPCYSEEAHHYFARMHVAVAPACNIQCHYCNRKYDCANESRPGVVSEVLTPEQAVKKVKAVAAAIPQMSVLGIAGPGDPLANPKRTLDTFRMLSEQAPDMKLCVSTNGLALPECVEELAKHNIDHVTITINCVDPEIGAKIYPDLLEQQAHPRRQGRKILIEQQQKGLEMLVARGILVKVNSVMIPGVNDEHLKEVSKIVKAKGAFLHNVMPLIAEPEHGTFYGVMGQRSPEPEELQDLQDACAGDMNMMRHCRQCRADAVGMLGEDRGDEFTLDKIESMEIDYEAAMVKRAAIHAAIKEELDEKAAKKERLAGLSVASVQNGTSGRYRPVLMAVATSGGGLINQHFGHATEFLVYEASPSGVRFIGHRRVDQYCVGNDTCGEKESALAGSIRALKGCEAVLCSKIGFEPWSDLETAGIQPNGEHAMEPIEEAVMAVYREMIESGRLENDGALLQAKA | 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 nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
Sequence Mass (Da): 54579
Sequence Length: 502
Pathway: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
EC: 4.-.-.-
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Q8KC85 | MTLNIKNHPCFNDSSRHTYGRIHLPVAPKCNIQCNYCNRKFDCMNENRPGITSKVLSPRQALYYLDNALKLSPNISVVGIAGPGDPFANPEETMETLRLVREKYPEMLLCVATNGLDMLPYIEELAELQVSHVTLTINAIDPEIGQEIYAWVRYQKKMYRDRQAAELLLENQLAALQKLKRYGVTAKVNSIIIPGVNDQHVIEVARQVASMGADILNALPYYNTTETVFENIPEPDPMMVRKIQEEAGKLLPQMKHCARCRADAVGIIGEINSDEMMAKLAEAALMPKNPDEHRPYIAVASLEGVLINQHLGEADRFLVYALDEEKKSCTLVDSRQAPPPGGGKLRWEALAAKLSDCRAVLVNSAGDSPQSVLKASGIDVMSIEGVIEEAVYGVFTGQNLKHLMKSSQIHACKTSCGGDGNGCD | 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 nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
Sequence Mass (Da): 46794
Sequence Length: 424
Pathway: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
EC: 4.-.-.-
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P27714 | MQPTQYVGIQDIKSLGTLLDKVAEHKGCGTSSEGGKASCGSSDGPADMAPEVWEKVKNHPCYSEEAHHHYARMHVAVAPACNIQCNYCNRKYDCANESRPGVVSEKLTPEQAAKKVFAVASTIPQMTVLGIAGPGDPLANPAKTFKTFELISQTAPDIKLCLSTNGLALPDHIDTIAAFNVDHVTITTNMVDPEIGQHIYPWIYYQNKRWTGIDAARILHERQMLGLEMLTARGILCKVNSVMIPGINDQHLVEVNRAVKSRGAFLHNIMPLISAPEHGTVFGLNGQRGPSAQELKALQDACEGEMNMMRHCRQCRADAVGLLGEDRSAEFTTEKIEAMEVAYDGATRKAYQELVEQERQAKSAAKAAEQQELAQMADQSGLSLLVAVATKGQGRVNEHFGHVSEFQIYEVSSAGSKFVGHRRVDQYCQGGYGEEDALETVIRAINDCHAVLVAKIGGCPKDDLQKVGIEPVDRYAHEFIEQSVIAYFMDYLERVRSGQIEHRPRGDADIRQGAYTSVQSTSAAA | 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 nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
Sequence Mass (Da): 57440
Sequence Length: 525
Pathway: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
EC: 4.-.-.-
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P10390 | MTSCSSFSGGKACRPADDSALTPLVADKAAAHPCYSRHGHHRFARMHLPVAPACNLQCNYCNRKFDCSNESRPGVSSTLLTPEQAVVKVRQVAQAIPQLSVVGIAGPGDPLANIARTFRTLELIREQLPDLKLCLSTNGLVLPDAVDRLLDVGVDHVTVTINTLDAEIAAQIYAWLWLDGERYSGREAGEILIARQLEGVRRLTAKGVLVKINSVLIPGINDSGMAGVSRALRASGAFIHNIMPLIARPEHGTVFGLNGQPEPDAETLAATRSRCGEVMPQMTHCHQCRADAIGMLGEDRSQQFTQLPAPESLPAWLPILHQRAQLHASIATRGESEADDACLVAVASSRGDVIDCHFGHADRFYIYSLSAAGMVLVNERFTPKYCQGRDDCEPQDNAARFAAILELLADVKAVFCVRIGHTPWQQLEQEGIEPCVDGAWRPVSEVLPAWWQQRRGSWPAALPHKGVA | 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 nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
Sequence Mass (Da): 50856
Sequence Length: 468
Pathway: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
EC: 4.-.-.-
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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 nitrogenase activity.
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate
Sequence Mass (Da): 29208
Sequence Length: 265
EC: 1.18.6.1
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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 nitrogenase activity.
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate
Sequence Mass (Da): 31205
Sequence Length: 292
EC: 1.18.6.1
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Q44290 | MNKVLINDTTLRDGEQAAGVVFTLEEKVAIAKFLDTIGVPELEVGIPAMGEEEMRAICAISNLGLKANLLAWNRAVISDIKASVACGMERVHIAIPVSGIQIAAKFHGQWRVSLQRLKDCISFAVDQGLWVAVGGEDSSRADENFLLDVALYAQEWGASRFRFCDTVGVLDPFTTYGKVKLLVSALTIPVEVHTHNDFGMATANALAGIKAGASSVNTTVIGLGERAGNAALEEVVMAIKRIYGVDMGIDTPRLLELSQLVAAASGANVPPWKAIVGENTFAHESGIHAHGVLQNPDTYEPFAPEEVGWERRLVVGKHSGRHSVSNLLEQHGIFLNPEETQSVLDAVRQQSIKKKRSLTTEELLNLVKEQRYSHAAR | 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 | MAVVMDGVKKNIIDRTIPNLVKKFQNFNNDDIAYFLKLLHETGIDLFEINRDSMDKIKKFPLNLDYIYRIENIEDYNYLNNYNFKYIILNYKTIYRFLLEDEKIQKNLKEHNIILEIDIEDLDELYLSEDNKIFCIFNIVCLRINNLSKLDFIDEDFRIKDLKSKFNVLVDFCASNKYNMATAIIINAFLNGSDIITTEFNSNDYAAMEEVIIALKSIRNIEIRGDLKLISKLTRIYEKITSERVYSMKPILGEDIFKYESGIHADGIAKNPKNYEPFNPELIGTNRKLYIGKHSGKAALVVKFKELNLNCNNIDMNLFLQDIREKSIQEKRNVLDNEIIEMYKEYNKSYQR | 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 | MAGSTIINDTHARDGEQTAGVAFTLDEKIAIAQALDEAGVAELEIGIPAMGREERERIRAVASLGLKARLMVWCRMHDTDLKARSTAVAPSLSVPVSDIHITKKLNGSRAWALREIERKVKTARDHGLEVSLGGEDSSRADMDFLIAAATVAQRPRFRFADTLGVLDPFQHARLHLTAAATDPEIGYHAHTPRLANATAWVTLAAVLGGATHVNTTVNGLGERAGNAPLEEVVVSLKVLYGQDCGVDTRALGAISDLVERASNRPVAVNKSIVRDAVFTHEAGIHVDGLLTDRAPTRISTPPRWGASTASCWASIPARGGEDGLRQLGIACDDATAQACCRGSGRATRAKPPDGGGAARPFHDDACWQAFPAAGGV | 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 | MASVIIDDTTLRDGEQSAGVAFNADEKIAIARALAELGVPELEIGIPSMGEEEREVMHAIAGLGLSSRLLAWCRLCDVDLAAARSTGVTMVDLSLPVSDLMLHHKLNRDRDWALREVARLVGEARMAGLEVCLGCEDASRADLEFVVQVGEVAQAAGARRLRFADTVGVMEPFGMLDRFRFLSRRLDMELEVHAHDDFGLATANTLAAVMGGATHINTTVNGLGERAGNAALEECVLALKNLHGIDTGIDTRGIPAISALVERASGRQVAWQKSVVGAGVFTHEAGIHVDGLLKHRRNYEGLNPDELGRSHSLVLGKHSGAHMVRNTYRDLGIELADWQSQALLGRIRAFSTRTKRRSPQPAELQDFYRQLCEQGNPELAAGGMA | 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 | MSRQQPRASFLPESPLAPVALCDTTLRDGEQTAGVAFTRAEKRAIAEALQAAGVAEVEVGVPAMGEEERADIRAVAAVLKTAAPVVWCRLRAEDLAAAQRTGVVRLHIGVPVSERQISAKLGKDAAWVRDKVEKLVRAASWAGHKVSVGAEDASRADPFFLAEIAHVAAEAGAIRFRISDTLGVLDPFAAHELVGRVVTRCPLPVEFHGHNDLGMATANSLAAARAGASHLSVTVNGLGERAGNAALEEVAAALEAAGRATGVALGQLCALSELVARASGRPLSPQKPIVGEGVFTHECGIHVDGLMKDRATYESADLRPERFGRSHRIAIGKHSSAAGLARALAEAGLPADAATLAALMPALRDWAAITKRAAAPEDLAALLAAQTETAR | 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 | MTVRETRFPSSSATATQPDAVVRFCDTTLRDGEQAPGVAFTAAEKLAIAGALDAIGVHQIEAGIPGMGVTERDVLREILATDPKAEIVGWCRADHRDVEAAASCGLVTAHLTIPVSDLHLKSKLERDRAWARRRVRDCVVDGTDRGMRVSVGFEDASRADDAFVTDLAGELRDVGVTRLRWADTVGLLDPVSAYDRLGRLVRAVPGPWEIHAHDDFGLATANTIAAVQAGFTWVSTTVLGLGERAGNAPIEEVAMALRHLLKLPIDLDTTSFRTLAQLVVGWPLPAGKKAVVGESVFAHESGIHVHGILRHPATYEPFDPEVGGRRRLTVGKHSGRASLRHALEQCGITAEESELEPLVEQVRLAATRHKRGLDSRDLPGTSRAGRDAGPRAGTPTREEPV | 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 | MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQNAPAARLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAAAWKPSALGLERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSGRQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIYDELCGESALRARG | 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 | MHIPDGYLSPVTCAVTFAATVPFWYVSMRKLDRDLNGQHLPLVALVAAFSFVIMMFNLPIPGGTTAHAAGIGIAAVLLGPWAAVPAISVALLIQAIFFGDGGITAFGANCLNMAVVGPMVAAAVYALGTRGAAIGSRRRVIMAGLASYAGLNAAALLAAVEFGVQPLFFHDAAGAPLYAPYPLSVAVPAMALTHLTIAGAAEFIVTAGLVAWLQRSNPELLAPRRAPAAPERHLRLWAGIGALVVLCPLGLIAAGTAWGEWGAEDFTSEAGRAAMAGASGGVAPPAGLPGGFARLAELWSAPLPDYAPAFVQNAPLGYVLSALLGVALIVAGIGLSAGLRALTRRAG | 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
Subcellular Location: Cell inner membrane
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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 membrane protein
Sequence Mass (Da): 27039
Sequence Length: 254
Subcellular Location: Cell inner membrane
EC: 3.6.3.-
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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
Subcellular Location: Cell inner membrane
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Q9VFS2 | MAAGVFKSFMRDFFAVKYDEQRNDPQAERLDGNGRLYPNCSSDVWLRSCEREIVDPIEGHHSGHIPKWICGSLLRNGPGSWKVGDMTFGHLFDCSALLHRFAIRNGRVTYQNRFVDTETLRKNRSAQRIVVTEFGTAAVPDPCHSIFDRFAAIFRPDSGTDNSMISIYPFGDQYYTFTETPFMHRINPCTLATEARICTTDFVGVVNHTSHPHVLPSGTVYNLGTTMTRSGPAYTILSFPHGEQMFEDAHVVATLPCRWKLHPGYMHTFGLTDHYFVIVEQPLSVSLTEYIKAQLGGQNLSACLKWFEDRPTLFHLIDRVSGKLVQTYESEAFFYLHIINCFERDGHVVVDICSYRNPEMINCMYLEAIANMQTNPNYATLFRGRPLRFVLPLGTIPPASIAKRGLVKSFSLAGLSAPQVSRTMKHSVSQYADITYMPTNGKQATAGEESPKRDAKRGRYEEENLVNLVTMEGSQAEAFQGTNGIQLRPEMLCDWGCETPRIYYERYMGKNYRYFYAISSDVDAVNPGTLIKVDVWNKSCLTWCEENVYPSEPIFVPSPDPKSEDDGVILASMVLGGLNDRYVGLIVLCAKTMTELGRCDFHTNGPVPKCLHGWFAPNAI | 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 of the 3-hydroxyretinal chromophore of rhodopsin from zeaxanthin and for proper photoreceptor development. Also essential for larval light perception.
Catalytic Activity: all-trans-zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
Sequence Mass (Da): 69932
Sequence Length: 620
Pathway: Cofactor metabolism; retinol metabolism.
EC: 1.13.11.65
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A8Y9I2 | MAVHQEKLYPNCDSGVWLRSCEEEVTEPLEGTITGEIPSWLQGSLLRNGPGSLKVGSMRFEHLFDSSALLHRFAINDGSVTYQCRFLQSNTFKKNRAAERIVVTEFGTRAVPDPCHTIFDRVAALFKPGESLSDNAMISLYPFGDEIYAFTEGPVIHRIDPETLDTLERRNLMDSVSLVNHTSHPHVMPNGDVYNLGMSIVQGRLKHVIVKFPYTEKGDMFAKAHIVANMSPRWPLHPAYMHTFGITENYFVIVEQPLSVSLLTMVKSQPSNEPLASSLHWYPNHETHIVLLSRRDGKEVKRYRTEPLFYLHIINAYEHDGVLVVDLCAYKDAKAIDAMYINAIETMQSNADYAEWFRGRPKRLELPLNATNCSRIEPRLLAQLGCETPRIHYDLYNGRPYRYFYAISSDVDAANPGTIIKVDTKTGETKTWCDTNCYPSEPIFVPAPGATEEDDGVILSALVWGGAGAHCRRVALLVLEARGLRELARATFCAPSPVPKCLHGWFLPRRTQL | 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 of the 3-hydroxyretinal chromophore of rhodopsin from zeaxanthin and for proper photoreceptor development.
Catalytic Activity: all-trans-zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
Sequence Mass (Da): 57839
Sequence Length: 513
Pathway: Cofactor metabolism; retinol metabolism.
EC: 1.13.11.65
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Q9VGP2 | MGMKFQKILVLAGIVIGFLSIIVVLAGTLLKNSVPNVLAPVERHFAFDYVIVGGGTGGSTLTSLLAKNSNGSVLLIEAGGQFGLLSRIPLLTTFQQKGINDWSFLSVPQKHSSRGLIERRQCLPRGKGLGGSANLNYMLHFDGHGPDFDSWRDHHNLSDWSWAQMRSFMAAAKPKNPDMLEIPRRYSKLTEALEEAQAQFAYKDWIFRRSLYNIRNGLRHSVVQQFLNPVIHHSNLRLLPDALVKRIQLAPSPFLQATSILVGIKDEENREKEFSIELLMASGIGDVSALKKLGIPAQHSLPLVGHNLHDHFNLPLFVSMGVTGPTLNQNTLLNPMTLINYLSSGSGPLGNFGVLGNVVSYGGLGAPPYGITFFGAGAIDESALMSISNFKGPAFRALFPRYYNSSQEGFVVISSCLQPKSRGSVGLLNRHMRRNPLIDPNYLSSEEDVACTISAIRSAVELVNSTAFAALHPRIHWPRVQECSNFGPFERDFFDNRPSDQYLECLMRHVGLGSHHPGGTCALGSVVDSQLRLKGVSNVRVVDASVLPRPISGNPNSVVVAIALRAASWILKSELQAGDSK | 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 Mass (Da): 63475
Sequence Length: 581
Subcellular Location: Secreted
EC: 1.-.-.-
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Q9I609 | MRLIGLALGLLLGALAQAGEAPGEALYRQHCQACHGAGRLGGSGPTLLPESLSRLKPAQAREVILHGRPATQMAGFAGQLDDAAADALVAYLYQAPPREPQWSAEDIRASQVQPHPLATLPSRPRFEADPLNLFVVVESGDHHVTILDGDRFEPIARFPSRYALHGGPKFSPDGRLVYFASRDGWVTLYDLYNLKVVAEVRAGLNTRNLAVSDDGRWVLVGNYLPGNLVLLDARDLSLVQVIPAADAQGQASRVSAVYTAPPRHSFVVALKDVHELWELPYANGKPVAPKRLAVADYLDDFSFSPDYRYLLGSSRQARGGEVIELDSGARVASIPLSGMPHLGSGIYWKRDGRWVFATPNISRGVISVIDLQNWKPLKEIVTDGPGFFMRSHADSPYAWTDTFLGKKHDEILLIDKQTLEIAHRLRPSPGKVAGHVEFTRDGRYALLSVWDRDGALVVYDAHSLEEVKRLPMNKPSGKYNVGNKIGYAEGTSH | 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: Consists of an N-terminal domain that binds the heme c cofactor, followed by a long linker segment, and a C-terminal region that exhibits an eight-bladed heme d1-binding beta-propeller domain.
Pathway: Porphyrin-containing compound metabolism.
Subcellular Location: Periplasm
EC: 1.3.-.-
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P24474 | MPFGKPLVGTLLASLTLLGLATAHAKDDMKAAEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPLGMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDGDSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMIDLWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAIIASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSIGAAPFLHDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGKTPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHPQYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDARISQSVAVFDLKNLDAKYQVLPIAEWADLGEGAKRVVQPEYNKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAVVKDPRLITPTGKFNVYNTQHDVY | 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
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P24040 | MSNVGKPILAGLIAGLSLLGLAVAQAAAPEMTAEEKEASKQIYFERCAGCHGVLRKGATGKNLEPHWSKTEADGKKTEGGTLNLGTKRLENIIAYGTEGGMVNYDDILTKEEINMMARYIQHTPDIPPEFSLQDMKDSWNLIVPVEKRVTKQMNKINLQNVFAVTLRDAGKLALIDGDTHKIWKVLESGYAVHISRMSASGRYVYTTGRDGLTTIIDLWPEEPMTVATVRFGSDMRSVDVSKFEGYEDKYLIGGTYWPPQYSIVDGLTLEPIKVVSTRGQTVDGEYHPEPRVASIVASHIKPEWVVNVKETGQIILVDYTDLKNLKTTTIESAKFLHDGGWDYSKRYFMVAANASNKVAAVDTKTGKLAALIDTAKIPHPGRGANFVHPQFGPVWSTGHLGDDVVSLISTPSEESKYAKYKEHNWKVVQELKMPGAGNLFVKTHPKSKHFWADAPMNPEREVAESVYVFDMNDLSKAPIQLNVAKDSGLPESKAIRRAVQPEYNKAGDEVWISLWGGKTDQSAIVIYDDKTLKLKRVITDPAVVTPTGKFNVFNTMNDVY | 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
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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
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P25006 | MTEQLQMTRRTMLAGAALAGAVAPLLHTAQAHAAGAAAAAGAAPVDISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKVTGEWNDDLMTSVVKPASM | 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 type I copper site in NIR plays a crucial role for electron transfer from pseudoazurin to the type II copper site of NIR, which comprises the catalytic center of NIR for the reduction of nitrite.
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.
Subcellular Location: Periplasm
EC: 1.7.2.1
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P38501 | MAEQMQISRRTILAGAALAGALAPVLATTSAWGQGAVRKATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDDAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATGALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYEDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSGT | 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 experimentally proven.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite
Sequence Mass (Da): 40332
Sequence Length: 376
Domain: The type I copper site in NIR plays a crucial role for electron transfer from pseudoazurin to the type II copper site of NIR, which comprises the catalytic center of NIR for the reduction of nitrite.
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.
Subcellular Location: Periplasm
EC: 1.7.2.1
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P81445 | GLPRVAVDLVAPPLVHPHSQVAAGAPKVVQFRMSIEEKKMVADDDGTTAQAMTFNGSVPGPTLVVHEGDYIELTLVNPATNSMPHNVDFHAATGALGGAGLTQVVPGQEAVLRFKADRSGTFVYHCAPAGMVPWHVVSGMNGALMVLPRDGLRDAAGAALAYDRVYTIGESDLYVPKAADGNYSDYPALASAYADTVAVMRTLTPSHAVFNGAVGALTGANALTAAVGESVLIIHSQANRDSRPHLIGGHGDWVWTTGKFANPPQLNMETWFIPGGSAAAALYTFKQPGTYAYLSHNLIEAMELGAAAQASVEGQWDDDLMTSVAAPGPA | 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(+) + nitrite
Sequence Mass (Da): 34413
Sequence Length: 330
Domain: The type I copper site in NIR plays a crucial role for electron transfer from pseudoazurin to the type II copper site of NIR, which comprises the catalytic center of NIR for the reduction of nitrite.
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.
Subcellular Location: Periplasm
EC: 1.7.2.1
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Q39161 | MTSFSLTFTSPLLPSSSTKPKRSVLVAAAQTTAPAESTASVDADRLEPRVELKDGFFILKEKFRKGINPQEKVKIEREPMKLFMENGIEELAKKSMEELDSEKSSKDDIDVRLKWLGLFHRRKHQYGKFMMRLKLPNGVTTSAQTRYLASVIRKYGEDGCADVTTRQNWQIRGVVLPDVPEILKGLASVGLTSLQSGMDNVRNPVGNPIAGIDPEEIVDTRPYTNLLSQFITANSQGNPDFTNLPRKWNVCVVGTHDLYEHPHINDLAYMPANKDGRFGFNLLVGGFFSPKRCEEAIPLDAWVPADDVLPLCKAVLEAYRDLGTRGNRQKTRMMWLIDELGVEGFRTEVEKRMPNGKLERGSSEDLVNKQWERRDYFGVNPQKQEGLSFVGLHVPVGRLQADDMDELARLADTYGSGELRLTVEQNIIIPNVETSKTEALLQEPFLKNRFSPEPSILMKGLVACTGSQFCGQAIIETKLRALKVTEEVERLVSVPRPIRMHWTGCPNTCGQVQVADIGFMGCLTRGEEGKPVEGADVYVGGRIGSDSHIGEIYKKGVRVTELVPLVAEILIKEFGAVPREREENED | 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 reduction (assimilation).
Subcellular Location: Plastid
EC: 1.7.7.1
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P38500 | MSSLSVRFLSPPLFSSTPAWPRTGLAATQAVPPVVAEVDAGRLEPRVEEREGYWVLKEKFREGINPQEKLKLEREPMKLFMEGGIEDLAKMSLEEIDKDKISKSDIDVRLKWLGLFHRRKHHYGRFMMRLKLPNGVTTSAQTRYLASVIRKYGKDGCADVTTRQNWQIRGVVLSDVPEILKGLDEVGLTSLQSGMDNVRNPVGNPLAGIDIHEIVATRPYNNLLSQFITANSRGNLAFTNLPRKWNVCVVGSHDLFEHPHINDLAYMPAIKDGRFGFNLLVGGFFSPRRCAEAVPLDAWVSADDIILVCKAILEAYRDLGTRGNRQKTRMMWLIDELGIEGFRSEVVKRMPNQELERAAPEDLIEKQWERRELIGVHPQKQEGLSYVGLHIPVGRVQADDMDELARLADTYGCGELRLTVEQNIIIPNIENSKLEALLGEPLLKDRFSPEPPILMKGLVACTGNQFCGQAIIETKARALKVTEEVQRQVAVTRPVRMHWTGCPNSCGQVQVADIGFMGCMARDENGKPCEGAAVFLGGRIGSDSHLGNLYKKGVPCKNLVPLVVDILVKHFGAVPREREESED | 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
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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
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P17847 | IPGRTGRARAAVSVPPPAGEQVPTERLEPRVEERAGGYWVLKEKYRAGLNPQEKVKLEKEPMALFMEGGIQDLARVPMEQIDAAKLTKDDVDVRLKWLGLFHRRKHQYGRFMMRLKLPNGVTTSEQTRYLASVIEAYGADGCADVTTRQNWQIRGVTLPDVPAILDGLRAVGLTSLQSGMDNVRNPVGNPLAGVDPHEIVDTRPYTNLLSSYVTNNSQGNPTITNLPRKWNVCVIGSHDLYEHPHINDLAYMPAVKDGEFGFNLLVGGFISPKRWAEALPLDAWVAGDDVVPVCKAILEAYRDLGSRGNRQKTRMMWLIDELGMEVFRSEVEKRMPNGVLERAAPEDLVDKRWERRDYLGVHPQKQEGLSYVGLHVPVGRLQAADMFELARLADEYGTGELRLTVEQNIVLPNVSNERLDALLAEPLLQEQRLSPRPSMLLRGLVACTGNQFCGQAIIETKARALQVAREVEKRVAVPRPVRMHWTGCPNSCGQVQVADIGFMGCLTKDSDGKIVEAADIFVGGRVGSDSHLADVYRKSVPCKDLVPIVADLLVERFGAVPREREEDEE | 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
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Q42997 | MASSASLQRFLPPYPHAAASRCRPPGVRARPVQSSTVSAPSSSTPAADEAVSAERLEPRVEQREGRYWVLKEKYRTGLNPQEKVKLGKEPMSLFMEGGIKELAKMPMEEIEADKLSKEDIDVRLKWLGLFHRRKHQYGRFMMRLKLPNGVTTSEQTRYLASVIEAYGKEGCADVTTRQNWQIRGVTLPDVPAILDGLNAVGLTSLQSGMDNVRNPVGNPLAGIDPDEIVDTRSYTNLLSSYITSNFQGNPTITNLPRKWNVCVIGSHDLYEHPHINDLAYMPAVKGGKFGFNLLVGGFISPKRWEEALPLDAWVPGDDIIPVCKAVLEAYRDLGTRGNRQKTRMMWLIDELGMEAFRSEVEKRMPNGVLERAAPEDLIDKKWQRRDYLGVHPQKQEGMSYVGLHVPVGRVQAADMFELARLADEYGSGELRLTVEQNIVIPNVKNEKVEALLSEPLLQKFSPQPSLLLKGLVACTGNQFCGQAIIETKQRALLVTSQVEKLVSVPRAVRMHWTGCPNSCGQVQVADIGFMGCLTKDSAGKIVEAADIFVGGRVGSDSHLAGAYKKSVPCDELAPIVADILVERFGAVRREREEDEE | 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 reduction (assimilation).
Subcellular Location: Plastid
EC: 1.7.7.1
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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 molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self . Upon HLA-E-peptide binding, transmits intracellular signals through two immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHP-1 and INPPL1/SHP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules . Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions . Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity . On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens . In HLA-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion .
PTM: Phosphorylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26314
Sequence Length: 233
Domain: The cytosolic N-terminus contains two immunoreceptor tyrosine-based inhibitory motifs (ITIMs), which are essential for the association with INPP5D/SHIP-1 and INPPL1/SHIP-2 phosphatases and functional inhibition.
Subcellular Location: Cell membrane
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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 effector functions of adaptive natural killer (NK) cells and in maternal-fetal tolerance during pregnancy. Regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, and in particular may play a role in adaptive NK cell response to viral infection. Upon MHC-E-peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26389
Sequence Length: 231
Subcellular Location: Cell membrane
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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 (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, RAET1L/ULBP6, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 25304
Sequence Length: 216
Subcellular Location: Cell membrane
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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 (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26710
Sequence Length: 232
Subcellular Location: Cell membrane
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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 (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24773
Sequence Length: 214
Subcellular Location: Cell membrane
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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
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P44585 | MRCFRLSRHFIVYLFSLCAILLLAGCVQSRGGFVSKNHVVLAEQNPNTHFEQEVMIVRLSQVLLVGKMSNEERASLHFERGVLYDSLGLWGLARYDLTQALALQPKMASVYNYLGLYLLLEEDYDGALDAFNTVFELDSGYDYTHLNRGLNFYYVGRYHLAQQDFLQFYQADKKDPYRVLWLYLNEQKLKPQEAQTNLVERAKGLSEDFWGTHIVQYYLGHISVEELQQRASEFAENSQQYAEILTETYFYLAKQKLNVGLVDEAAALFKLAMANQVYNFVEYRFAAFELMKLKPVQTEDEKEEKSAVTKAIVF | Function: May be involved in cell division.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36434
Sequence Length: 314
Subcellular Location: Cell membrane
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Q9LTR9 | MADNNSPPGSVEQKADQIVEANPLVKDDTSLETIVRRFQDSMSEAKTHKFWETQPVGQFKDIGDTSLPEGPIEPATPLSEVKQEPYNLPSVYEWTTCDMNSDDMCSEVYNLLKNNYVEDDENMFRFNYSKEFLRWALRPPGYYQSWHIGVRAKTSKKLVAFISGVPARIRVRDEVVKMAEINFLCVHKKLRSKRLAPVMIKEVTRRVHLENIWQAAYTAGVILPTPITTCQYWHRSLNPKKLIDVGFSRLGARMTMSRTIKLYKLPDAPITPGFRKMEPRDVPAVTRLLRNYLSQFGVATDFDENDVEHWLLPREDVVDSYLVESPETHDVTDFCSFYTLPSTILGNPNYTTLKAAYSYYNVATQTSFLQLMNDALIVSKQKGFDVFNALDVMHNESFLKELKFGPGDGQLHYYLYNYRLKSALKPAELGLVLL | 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
Subcellular Location: Cytoplasm
EC: 2.3.1.97
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P30419 | MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ | 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 cycle .
Catalytic Activity: N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56806
Sequence Length: 496
Subcellular Location: Cytoplasm
EC: 2.3.1.97
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O70310 | MADESETAVKLPAPSLPLMMEGNGNGHEHCSDCENEEDNSHNRSGLSPANDTGAKKKKKKQKKKKEKGSDMESTQDQPVKMTSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMEKKDIPVVHQLLSRYLKQFHLTPVMNQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ | 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 during the GTPase cycle (By similarity). Required for normal embryogenesis .
Catalytic Activity: N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56888
Sequence Length: 496
Subcellular Location: Cytoplasm
EC: 2.3.1.97
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P36597 | MSTNKITFLTNWEATPYHLPIFLAQTRGYYEREGIEVAILEPTNPSDVTALIGSGKVDMGLKAMIHTLAAKARGYPVTSFGSLLNEPFTGLITLKGNGINDFKDIKGKRIGYVGEFGKIQLDDLCSKFGLSPSDYTAIRCGMNIAPAIINGEIDGGIGIECMQQVELERWCVSQGRPRSDVQMLRIDRLANLGCCCFCTILYIAHDEFIAKHPDKIKAFLRAIHSATLDMLKDPVQTYKEYIHFKREMGSELHREQFERCFAYFSHDISNVPRDWNKVTNYSKRLGIIPQDFEPNCTNGYLTWELDPDEKDPMGKQEAIAEIQDEIKQKGGVFSGNSLRYVEPANL | 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. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Catalytic Activity: 2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
Sequence Mass (Da): 38966
Sequence Length: 346
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.-.-.-
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E2QUI9 | MAARAGPRAALAGAAAVALLSAALVLYELPPGAVLQRAFSLHKAHSVEDMENTLQLVRNIIPPLTTKKHKGQDGRIGVVGGCQEYTGAPYFAAISAHKVGADLSHVFCTREAAPVIKSYSPELIVHPVLDSPSAVHDVEEWLPRLHALVVGPGLGRDNILLENVKGILEASKARDIPVIIDADGLWLIAQHPALIQSYQKAVLTPNHVEFNRLSEAVLSHQVDGSDHHEAVRRLSQALGNVTVVQKGERDVISDGKQVLECTQEGSSRRCGGQGDLLSGTLGVLVHWALHAAPEKTNGSSPLLLAALGACSLTRQCSLQAFQKHGRSTTTTDMIAEIGPAFSKLFET | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 36941
Sequence Length: 347
Subcellular Location: Mitochondrion
EC: 4.2.1.93
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 30027
Sequence Length: 287
EC: 4.2.1.136
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F6RCC2 | MSTILFYTRALIIGATKSQGVFGKTGTLVANISSNRGIISIVPRTNPPQKLLKMQEEENSLLEEARKVVPALSFGKHKGQAGRVGVIGGSEEYTGAPYFAAISAMKAGADLAHVFCSKSASTVIKSYSPELIVHPLLDVPNAVTLLDEWLPRIHSHVIGPGLGRVDATLNTVKEILIKLKKQEIPIVIDADGLFLITRDPSIIHGYTKAILTPNVVEFQRLSKSMNLNWESKDLNGSIMETVALSKALGGVTIVRKGEVDIVAAGDEVVTMDEIGSPRRCGGQGDLLSGVMALFSYWTHNSTCTPPPTLLAGYAACFLTKRCANQAFQKHGRSTATTDLISEINSVFVNNFENPTDPKS | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 38630
Sequence Length: 359
EC: 4.2.1.93
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A8N8Z0 | MPIPRTIIEQIKRIIPPLDGSLHKGQSGRVGVLGGALDYTGAPFFAAFSALRFGVDLSHVICAPTAAGAIKSYSPDLIVHPILNESSSVDKVKSELQSLLSRLHVLVVGPGLGREPYMQSYARLAISLVRERGMYLVLDADALFLVGHDLSIIKGYRRAVLTPNVVEFKRLSEQVGVDPDAPPDERAGVVSRMLGGVTVLQKGAKDIISVDTTGEEADLSASHIEGADAEKEKIKETIAVDVEGGLKRCGGQGDVLSGCVGTFMAWGKCYESGVYGDGTVPTSRVPLLAAVAGSMVTRTTSRRAYAKSGRSLITQDLLSEAGPAFEECFGGDKGRL | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 35595
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 4.2.1.93
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Q5K8L4 | MASKQHAHILSLARSMIPPLHPKLHKGQAGRIGVLGGSGDYSGAPYFSSMGAMRFGADLAHVICEPSAGAVIKTYSPDLIVHTILDPQKSREDIRSALKGVMSRLHVLIIGPGLGRDDHMQSCAKIAFELAKDMEQMGVVVDADGLWLVQNEPKVVMDWPGVPRIILTPNVMEFKRLCDTMVGARTVLHLSPSTLINYQKINASGPHTSLCPQLATALGNATIIQKGPSDIISNGLKIPSALLSDESEEQNYLEVKVEGGLKRVGGQGDILSGSTGVLLAWGSEWVRGTYEHVGHPPPQDKAIAENIPVLAAYGASTFNRTVSKRGFQKKGRSMVTGDLVDMVGEVYEEVFGKPGEMEGRGKL | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 38975
Sequence Length: 363
Subcellular Location: Cytoplasm
EC: 4.2.1.93
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 33168
Sequence Length: 306
EC: 4.2.1.93
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 32153
Sequence Length: 300
EC: 4.2.1.93
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Q5B0D6 | MANVHHISVPSKVLFQKARKLVPPMLEKFHKGQQGRVAVIGGSLDYTGAPYFSAMASARLGCDLSHVICESSAATVIKSYSPNLMVHPILPSSASVKDPSSIDAPSLASPIIAMLGRLHALVIGPGLGRDGVTLKVVTEVMKEARSRSIPFVLDADGLLLVTENPDLVKGYKDCILTPNVNEFSRLAKALNIEVPSLAQISSKESGDKTSKEAEACEKLSQALGGVTIIQKGPHDVISNGVTSIVSDLPGGLKRSGGQGDTLTGSLGTLLAWRAAYHDALWDSGEQEHSKEAENKEEVQGELESNKRMSPSTTLLLAAWAGAAITRECSRRAFKAKGRSMQASDLTDEVHESFLTLIGEPEGSKVPERL | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 39268
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 4.2.1.93
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 31723
Sequence Length: 291
EC: 4.2.1.136
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 32623
Sequence Length: 300
EC: 4.2.1.93
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 30918
Sequence Length: 282
EC: 4.2.1.136
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C7YKN8 | MSTEDLNMSAATKNVLAKVRRIIPPMLESFHKGQLGRVAVIGGSENYTGAPYFSAMASARLGCDMSHVICTPAAATVIKSYSPNLMVHPLMRQSPAPNPNQDPATRDTSKDPDSDPEHISAQIIDLLPRLHVLVVGPGLGRDPLMHATVARVIRAARNRGTPVVLDADALILVQKDPGLVRGYDGAVLTPNVVEFAKLCEALKVDVSEGASETARVEALAKTLEGVTVIQKGAKDYISNGETTLTVDLQGGRKRSGGQGDTLTGSIATFLGWRKAYLDRLWDVGQNALGEHELVGLAAFGGAAITRECSRLAFAKKGRSLQASDLTEEVHVAFLNIFGEEDEETDSSRL | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 37277
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 4.2.1.93
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D3BMU4 | MFCIIHFGNPKNDKFLGSSTLYSQKLKTNNIKILCLQVFYYNIYESTNNNNNNKNKNKTLLLNNIRTYSTLSKGALSTTTTATTKKMSMDDSFELPTNLNHFLSYVPSLEYHMHKGQCGRIGVFGGSAEYTGAPFFAGITSLRLGADIVHIFAPSEGGTATAIKTLSPELIVHPLDQQMDPSTIIPWLLSIHVLIIGPGLGRSSIAWKSAKEVIKAARNINLPMVLDGDALRLICEDLELVKGYDKVILTPNFVEYRALSDAAKKLNNDNSNNILSPSDLAKALGNVVIVQKGQEDIITDGTISYSCDKAGMPRRCGGQGDVLAGVIGTFYAWTQNALKGKTSEELEHLKESIGENQSAAASAAYAGCVLVRYAAKLAFKNNRRSTITDDIIKSVPNALVWGFLTDDRGRPTI | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 45077
Sequence Length: 413
EC: 4.2.1.93
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Q8IW45 | MVTRAGAGTAVAGAVVVALLSAALALYGPPLDAVLERAFSLRKAHSIKDMENTLQLVRNIIPPLSSTKHKGQDGRIGVVGGCQEYTGAPYFAAISALKVGADLSHVFCASAAAPVIKAYSPELIVHPVLDSPNAVHEVEKWLPRLHALVVGPGLGRDDALLRNVQGILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVLRGPMDSDDSHGSVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSSRRCGGQGDLLSGSLGVLVHWALLAGPQKTNGSSPLLVAAFGACSLTRQCNHQAFQKHGRSTTTSDMIAEVGAAFSKLFET | 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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 36576
Sequence Length: 347
Subcellular Location: Mitochondrion
EC: 4.2.1.93
|
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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Mass (Da): 32363
Sequence Length: 303
EC: 4.2.1.93
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 29853
Sequence Length: 275
EC: 4.2.1.136
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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 heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 29787
Sequence Length: 278
EC: 4.2.1.136
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Q8NSS3 | MKPVFSVDQIRRAENTLFELQADPDELMISAASAVADVALAMVDGPAPAVSSEESILLLVGPGGNGGDALYAGAFLAEEGHHVDALLLGNGKVHQSALAYYESLGGQIISDFPPHYLYRLVIDGLFGIGGRGGLTPELASLVESFSASGIPILAIDVPSGVHADSGELPPGVMVTVEGFDNDAPMARQKIPAHIDADVTITFGGLRRAHAVSPACGEVLCADINIAGGGGKSLSAELSQVQAEDATPQMFASKAYQRKDSLFERANLKATAPHIHRIGQHFTVLNMEPGPDHDKYSGGIVGIVAGSGTYPGAAVLSVKAAVRATSAMVRYVGPALNFVIQSLPEVVATQSLATAGRVQAWVHGPGRGLEAEQSAELAELLSRPEPVLIDADSLSLLQLSAELRQALRERKAPTVLTPHKGEFERIAAELRSEGVEIPQADKDPIGAAQALAKEFDCCVLLKGKYTVIAAHDFVHAINAGHSWLATPGSGDVLSGLVGAHLAQSYAELNRLPEFFPDVTLSDSAIYTQIAPAATIHAVAAGLAARTEFGFAPTSASLIADAIPAATAKVDLKRIV | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 59796
Sequence Length: 574
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Q83CM5 | MTVLYQNRQIRELERLAVESGISEYELMCRAGEAAFKALLARWPEAQEITVCCGKGNNGGDGLVLARLAYENGLKVTVYLAGQRHQLKGAAAQAANACEASNLPILPFPEPLLFKGEVIVDALLGSGLSGEVKAPYDHLIAAINQAGQYVLALDVPSGINVDSGEVQGTAVKANLTVTFIAPKRGLYTDKAPAYCGELIVDRLGLSESFFRAVFTDTRLLEWKGVFPLLPKRARDAHKGSYGHVLVIGGDYGMGGAVRMAAEAAARVGAGLVTVATRPEHVPIVSGPRPELMCHQVAAADDLKPLLTAATVVVIGPGLGKSDWAKSLLNKVLETDLPKVLDADSLNLLAESPSQREDWILTPHPGEASRLLGISCNEVQRDRFQAINDLQEKYQGVLVLKGVGTLIKDESQAYYVCPAGNPGMATGGMGDILSGIIGGLVAQRLSLASAAQAGVFIHSMAADRAAEEGGERGLLATDLFPHLRVLVNP | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 51699
Sequence Length: 488
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B8E2P6 | MKLVTSEEIKRLEERLEREYSIPPILLMENAASFLFSFLKEKFEDIENRKIAILCGPGNNGGDGVALARYLYSNGIRKITIFSYLWGKKISDLLKIQLGLLKNLVEIKDILQDYTELKEYELIVDGIFGIGLKREIDDDLKKIFRYINNLGKKIISIDIPSGINSDTGEIMGEALRADYVLTMFLPKVGLFETGAVDYVGEVIVGRLGIPIEIVNDIVESNIHLVDWELLKDIVRIPSKGVHKGKKGKVLIIGGSFRYTGAPILSALSALRTGAGMVYLAVPEKISMVYRGNYPEIIYIPLKDKDGYISYDNLGYILEIIETYGIEAVAIGPGIGINEDVRRLVQDFLRKVDKKVVVDADALSFVKDILGDISGKDVVFTPHYGEMSRIVEESVETISKKRVEIGRNFVERYKLNLIIKGPNSLFFDPKNHVYVNPFADFLLATAGSGDVLTGIIAGFSAQGYSLKEACILGNFVHGYSSVIWKKYKGSVGLTASDIIKILPLAIDEVIRRRNV | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 57287
Sequence Length: 514
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P31806 | MTDHTMKKNPVSIPHTVWYADDIRRGEREAADVLGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKAVGIEVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVDLIVDALLGTGLRQAPRESISQLIDHANSHPAPIVAVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCAKRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFSTLQRIVNPEVTDKNHDESSNSAP | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 54650
Sequence Length: 515
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Q7NIE6 | MSGLCACTLVGAAQVQQLEAALFAAGMPVEALMEKAGLRLAAAIAADYPAGGYPRVGVLVGPGHNGGDALVVARELWLVGRSVQVFCPRPPIKPLARAHLDYFQSLGGRVHTGAVPEEPGVDLWVDGLFGFGLERPVAEPYAGLMAQVNASGVPVAAVDLPSGLSSETGEALGGLAVRAARTYCLGLWKRGLWQDAALDWLGVPVRLEIGFSEAQVRSVLGEDHRSARLLLPDAARAGLPLARPATAHKYSVGTLLAVAGSRQYGGAATLVALGARSGGPGMLYLALPESLADRVAARLPEAIVHPCPQAENGALADLPGVDLEKFDAVVCGPGLGKAEQALVLRLAREAAGALVLDADGLNLIAGQLEVLAQRAAPTVLTPHPGEFKRLFPDIALADRQGAARTAALRSHAWIVLKGARTVVASPSGQVWVNPGGSPALARGGSGDVLAGLLGALLAQCENPEPAVLGAVWWHAAAGEWLAARHTVLGVDAETLALGLLPFLAADGP | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 52119
Sequence Length: 508
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P56176 | MLSVYEKVNALDKRAIEELFLSEDILMENAAMALERAVLQNASLGAKVIILCGSGDNGGDGYALARRLVGRFKTLVFEMKLAKSPMCQLQQERAKKAGVVIKAYEENALNQNLECDVLIDCVIGSHFKGKLEPFLNFESLSQKARFKIACDIPSGIDSKGRVDKGAFKADLTISMGAIKSCLLSDRAKDYVGELKVGHLGVFNQIYEIPTDTFLLEKSDLKLPLRDRKNAHKGDYGHAHVLLGKHSGAGLLSALSALSFGSGVVSVQALECEITSNNKPLELVFCENFPNLLSAFALGMGLENIPKDFNKWLELAPCVLDAGVFYHKEVLQALEKEVILTPHPKEFLSLLKLVGINISMLELLDNKLEIARDFSQKYPKVVLLLKGANTLIAHQGQVFINILGSVALAKAGSGDVLAGLILSLLSQNYTPLDAAINASSAHALASLEFKNNYALTPLDLIEKIKQL | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 50737
Sequence Length: 466
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A2BLC0 | MLGRPVFGLGKAITSVDVAVIDANSEWIGVKRLQLMENAGRSVAEEAAKLAKPGSRVVVFAGPGGNGGDGLVAARHLAYMGYQVTVVMIVKPEEIRSPETRAMYEALAAMDLTVDIRIARAPADVAPVEADVVIDALLGTGLRGAPRPPYSDAIEAVNSSTGLKLAVDVPSGLNSDTGETPGAYVKADITVTFHKPKPGLLRRPDVAGRLVVVSIGAPPEAEVYVGPGDVAYRVRPRSWKAHKGSSGRVLIVGGSQDYVGAPILAALAAERSGVDLVFLAAPEHVTRAASHHPTIIPVPLRGSPNIHPDHVKKLEQLLDRVDAIAIGMGVGLSDETKEAIPQIIVKALEKEKPVVVDADGIKILGERGIPNSNRKLVVTPHQREFQILFGDALSGVDEDIKARALKAAEKAQRHGLVILLKGPIDIVTDGERIRLNRTGVPAMSVGGTGDTLAGITAALLARKLEPFHAASIAAFVNGLAGALAYAEKKDSMTAMDLIEKIPEALNNPIEAANRVPAYQRLVRGRIEWQPPVGRSES | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 56671
Sequence Length: 537
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B1L3W1 | MKVCSVEEIRELDSLASEKYGIDQEILMENAGLAVTYLIEREFGVEGKKFSVFAGPGNNGGDAFVVARQLHSRGGIVRVLLLSDPSKYKGPALSNYKRIEGLIEIIGADDIKGAVEWADAIVDGIFGTGLSKDVEGIFKEAIESINSSGKPVFSIDIPSGINGDDAMPRGVAVRATYTVTFGLPKYGNILYPGFSYCGRLLVSPISYPPEECSKIMVELNDPIELPERVRWGHKGSFGKFLAVSGSRNYYGAPYFTALSFLKAGGGYSRLAAPKSIIPFIASKASEVVYIPLEENDQGSISLNNFDLIVRMAEEQDVVALGPGVSTNEETQELILKLIEAIDKPIIIDGDGLTALSRNIEVMRGRKETILTPHLGEMSRLTRIPVAEIERRKIEMARSFASQNNCYLVLKGAHSIIAFPDGRCFINMTGNPGMATAGSGDVLTGTIAAMKGIGLSIEDSVRMGVFVHGLAGDLAAEEKGEDGITATDILEKLPLAMKLLRSDIDLLRRRYSLEVI | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 55708
Sequence Length: 515
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Q4QFL5 | MLSRLSERCTIATGLEQVLRHYVWSAAWLRDAEPAAAASENIDLSGLMERAGRAAYDVFANLYTSQKHWLILVGSGNNGGDGYVIARHAREAGKIVTVLRMPHSKPLPTEAASAQHAWKAVGGTESTMSPGAPLQLPADVDLIVDGLLGTGICGPPREQYADVIRHINGLPVPRVAIDIPSGLNAETGEAAGACVKADHTATFICLKPGLLTGQAKDYVGQLHYRSLGLEDWMTAPERMRVALCRRVALDDVYEYFGIRRSALAHKGSCGKAILVGGDHGFGGAALMSAEACVTVGAGLTRVLTRPEYAAPLLTRCPEAMVTAVETDTGEQLKQQMLEAFEWASTLAVGPGLGTGAYGQAALTAALRHAELHQDKTLVLDADALNLLAGCLHGREGGAAAGARKHLPVLPNSIITPHPGEAARLLDCRVADVEKDRLAAARRLAAILGGTCLLKGPGTIVHCHSSAKTAIVDAGNAGMASGGMGDVLTGLLAGLAAQRMHDTFDTTCAGALVHGVAADMVAAEDGRGTRGIRATELIHRVPLIVNASGPSPASRQRPSGQ | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 58434
Sequence Length: 560
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Q2FT57 | MTVIIQGRSFPDDLTQYAEFIGQGLLSPEEMRRIDQNAQALGISGLELMESAGTGLAMAARQYQPGKILILCGSGNNGGDGMVAARHLAGEADITVFWYDSGRQTDSTRTQLQRLLSCSVTSIPFRSRDDLIEHTRIFQDTDLIIDALLGTGGTGSVREPVRTCIEFANNAKAPILSADLPSPGIIPDRICAFHRAKTEGAHIYGIGIPLLAEISTGPGDLLILRNRNPDSHKGVGGNILVIGGGPYQGAPYLAGLAALRAGADIVRVVSPHYLPEPDIIHVPTAGDRITTADLATIIPLCKQADVVLCGPGLGPESHDVITSLAPYIRKGVFDADALRDPLPVAGESLYTPHAGEFARMSGLSPGKTPRERAHAIMKAQILGTVLLKGAVDVICDGSRVRFNQTGTPAMTTGGTGDVLAGVCAALMAVVPAFEAACIGAYVTGRAGELITQTCGYGMTARDLLTAVPQVLFRSTSERE | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 50414
Sequence Length: 479
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Q58981 | MRRDINNFLFGERMELFEILKQKIKEKEVITPKEMAIIDDNAEFLGIQKILLMENAGKAVYEEIKDIDAEEFIIFCGTGNNGGDGFVVARHLGKGDVILIGKESEIKTYEARENFKILKNLAEFGNIRIREIKWAEEVNDIFERLKNKKAVIIDAMIGTGVKGELREPFKTIVDKINELKQINKNIFVISVDVETGHLESDLTITFHKRKTINKDNAIVKKIGIPKEAEYIVGWGDLKALRKRDSNSHKGQNGKVLIIGGSKDFYGAPILAGLAALKIVDLVGILSVGKVIDKVNHPEFIMYRVEGDYLSSQHVDYTLEIAKKYDVVVLGNGLGANNRTKAFLNEFLAKYDGKVVIDADAIKVIDYNNFEFSENYIFTPHKREFEYMGIDLDNIENIKSTIVLKGKYDIIFNANNLKINKTGNAGLTKGGTGDVLAGLIGALFAVNEAFLSACCGAFINGYAGDLLLKEKGYYYTPLDLIEKIPNVLKIFQ | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 54979
Sequence Length: 491
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Q8TX67 | MFITSKEMRRIELNSRWLGFEEDFMMENAGAGVARVVIGEYSPNDVLVVCGTGGNGGDGFVTARHLDSEGVDVDVLLVGRREAIKNEAAELNLRRLDRAGIPVQEVRDSEDLESVDFERDVVVDALLGFGIRGRLREPVRSAVLRINEASRAGTRVVSIDIPTGLDPDSGETPDVAVEADLVVSIHRHKRGVRKLRDVFLRRVNAGIPEIAERICGPGDLITSDIWRRDPWSHKGQHGRVLIIGGSRKYVGAPQLAARGALRAGVDLVFLLTVDAVPKNDPNVIYRAVPAERLEPEHLDEVDLEGVDTVVVGPGLGADADSVGILRELAESFDGMIIVDADGLRGISGVNVDDRFVLTPHAGEFRREFGEELGRSLEDRSEAVRRVSEELGCTILLKGRVDVIGSPDGEIRWNVTGTPAMTVGGTGDVLAGVVAGVAARCREGFEAACIGAFVVGSAGCLAERRLSQGLTAEDVAEYVPKVLRNPWAAEPEAVTEVRRD | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 53849
Sequence Length: 499
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O27324 | MMRCGEGYPGLILAKEDFIMKPVDMAAADINAEYLGVPRLSLMENAGRAVAEEIGNAVDSGRVAIFCGPGGNGGDGFVAARHLLNMGFEVEVHLLGHPERIGSEEALVNWGVLGAMQPHPGGFSVDFVRDSSEIKPTDADVVVDAILGTGVRGSIREPSRSAIEIINRSEAFRVSVDIPSGLNPETGAVEDIAVSADLTVTFHRMKDGLKLADPAVTGEIVVRDIGIPPAAEIFMGPGDLLRIPSRRPGSHKGENGRVLIIGGSRQYSGAPAIAAKAALRAGADIVMVAAPGSAARAIRSLSPDLIVRELEGGYIGMESLDEILELAEKADSVLMGCGAGRETSTARTFMRAIEDLHEMEKPIVLDADALRLMDYSDVSEYRELTVTPHMAEFSSFFKLKSMIFNDFRESVSAFQSISSRIRGTVLLKGRIDMIFQGDRLRLNKTGCPGMTVGGTGDALAGLTAGLRALGLSSFDSASLAAFINGMAGELAMERHGNGFTASDMVDMIPSVMDPGFYGF | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 55021
Sequence Length: 519
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Q2RGI2 | MYLVTAAEMGQLDRLASSEYMIPSIVLMENAGLRVVESIERHFQGQVANRRILIFCGKGNNGGDGLVVARHLLNRGAEVKVFLLARPEDIRGDARTNLEIYQKMGGKLLLLLGESHLQRADIALLYADLVVDAIFGTGFKGAAMGLPAAVINMINKAHRETVAVDLPSGLEADTGRCFGPCIQATWTVTFALPKLGLVVEPGASLTGRLEVADIGIPQKLVATQHFNRRLLTAAWCRSQLPRREASGHKGLYGRVLAVGGSPGLTGAITLAATAALKAGAGLVTAAVPRGVQGILAMKTTEIMTMSLPETPAGALSRDALDPLLERLAEVDVLAIGPGLSRDPATVDLVKELLPRVQVPAVVDADALNALATDTRVLTGDHGPLVLTPHPGEMARLLGTTAAKIQEDRLEIAAKYAREWQAVLLLKGARTVIAWPDGQVYINPTGNPGMATAGSGDVLTGIIAGLAGQGLKPGVAAALGAYLHGAAGDEAARQRGQRAMMAGDLLDFLPYVLRNLEEEVETIVAAGLGRD | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 55712
Sequence Length: 530
|
P37391 | MRHYYSVAAIRDAEASLLASLPDGVLMKRAAYGLASVIIRELAVRTGGVTGRRVCAVVGSGDNGGDALWAATFLRRRGAAADAVLLNPDRVHRKALVAFRKAGGRIVENVSAATDLVIDGVVGISGSGPLRPAAAAVFATVSASGVPVVAVDLPSGIDVVTGVINGPAVHAALTVTFGGLKPVHALADCGDVTLVDIGLDLPDSDILGLQAADVAAYWPVPGVHDDKYTQGVTGVLAGSSTYPGAAVLCTGAAVAATSGMVRYAGSAYTQVLAHWPEVIASATPTAAGRVQSWVVGPGLGIDATATAALWFALETDLPVLVDADGLTMLAAHPDLVINRNAPTVLTPHASEFARLAGTPPGDDRVGACRKLADSFGATVLLKGNVTVIADPGGPVYLNPAGQSWAATAGSGDVLSGMIGALLAAGLPAAEAAAAAAFVHARAAALSAADPGPGDVPTSASRMVSHIRTALAAL | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 47227
Sequence Length: 473
|
P9WF10 | MRHYYSVDTIRAAEAPLLASLPDGALMRRAAFGLATEIGRELTARTGGVVGRRVCAVVGSGDNGGDALWAATFLRRRGAAADAVLLNPDRTHRKALAAFTKSGGRLVESVSAATDLVIDGVVGISGSGPLRPAAAQVFAAVQAAAIPVVAVDIPSGIDVATGAITGPAVHAALTVTFGGLKPVHALADCGRVVLVDIGLDLAHTDVLGFEATDVAARWPVPGPRDDKYTQGVTGVLAGSSTYPGAAVLCTGAAVAATSGMVRYAGTAHAEVLAHWPEVIASPTPAAAGRVQAWVVGPGLGTDEAGAAALWFALDTDLPVLVDADGLTMLADHPDLVAGRNAPTVLTPHAGEFARLAGAPPGDDRVGACRQLADALGATVLLKGNVTVIADPGGPVYLNPAGQSWAATAGSGDVLSGMIGALLASGLPSGEAAAAAAFVHARASAAAAADPGPGDAPTSASRISGHIRAALAAL | 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 is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Mass (Da): 46857
Sequence Length: 473
|
A0A2I6PIZ6 | MDSTGRQPLSQDGQPWQALASGLGFPDEDQKYWWSVMAPLLGELMKWANYPVDKQYLVLAFCHEYILPFCGPRPTAEGGIFWPTLITKDGTPFEPSLNFYKNKATLRVGYAPACELSGSNDDPINQRAPIAALEHQKRVLPQQNLKWVDNFKKAWFIDNDDAVALKARVHNELFEQAAVQCLIGYVFSDYTQVKVAMSPLWKSVQTGQQISRVIWDTFRQLGDDASSYLDCLSVLEEYTESKQAKLAQVQPSFVNFDVNLKGDYQQSRLKVYYATPCTAFDTMVQVFTLGGRLKGPEVDHAIECLRVLWPSVLAVPENHPDDQDLPRRYHSVAVTQFNFELWPGAKLPVPQIYLPTNFYGRDELEIAEGLEGFFKTLGWSEPFHAYKQNYIATCATPEGKWKAIQHDVSFSFKDSSPYVSVYYKPELSVLSSPS | 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-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed . The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB . The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA . NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD-dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable).
Sequence Mass (Da): 49261
Sequence Length: 434
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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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
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Q8L4H4 | MMELQVIRIFRLVVAFVLCLCIFIRSASSATKGFESIACCADSNYTDPKTTLTYTTDHIWFSDKRSCRQIPEILFSHRSNKNVRKFEIYEGKRCYNLPTVKDQVYLIRGIFPFDSLNSSFYVSIGVTELGELRSSRLEDLEIEGVFRATKDYIDFCLLKEDVNPFISQIELRPLPEEYLHGFGTSVLKLISRNNLGDTNDDIRFPDDQNDRIWKRKETSTPTSALPLSFNVSNVDLKDSVTPPLQVLQTALTHPERLEFVHDGLETDDYEYSVFLHFLELNGTVRAGQRVFDIYLNNEIKKEKFDVLAGGSKNSYTALNISANGSLNITLVKASGSEFGPLLNAYEILQARSWIEETNQKDLEVIQKMREELLLHNQENEALESWSGDPCMIFPWKGITCDDSTGSSIITKLDLSSNNLKGAIPSIVTKMTNLQILNLSHNQFDMLFPSFPPSSLLISLDLSYNDLSGWLPESIISLPHLKSLYFGCNPSMSDEDTTKLNSSLINTDYGRCKAKKPKFGQVFVIGAITSGSLLITLAVGILFFCRYRHKSITLEGFGKTYPMATNIIFSLPSKDDFFIKSVSVKPFTLEYIEQATEQYKTLIGEGGFGSVYRGTLDDGQEVAVKVRSSTSTQGTREFDNELNLLSAIQHENLVPLLGYCNEYDQQILVYPFMSNGSLLDRLYGEASKRKILDWPTRLSIALGAARGLAYLHTFPGRSVIHRDVKSSNILLDQSMCAKVADFGFSKYAPQEGDSYVSLEVRGTAGYLDPEYYKTQQLSEKSDVFSFGVVLLEIVSGREPLNIKRPRIEWSLVEWAKPYIRASKVDEIVDPGIKGGYHAEALWRVVEVALQCLEPYSTYRPCMVDIVRELEDALIIENNASEYMKSIDSLGGSNRYSIVMDKRALPSTTSTAESTITTQTLSHPQPR | 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-phospho-L-seryl-[protein]
Sequence Mass (Da): 104181
Sequence Length: 925
Subcellular Location: Membrane
EC: 2.7.11.1
|
Q6FEY7 | MAKVAGFRFELKQLFHLMWPILITQFAQAGLGLIDTIMAGHLSANDLAAIAVGVGLWMPVMLLFSAIMIATTPLVAEAKGARTPEHIPVIVRQSLWVAVSLGVIAMLILQLMPFLLPILGVPESLQPKAGLFLHAIGFGMPAVTMYAALRGYSEALGYPRPVTVISLLALVVLVPLNYIFMYGIGPVPHLGSAGCGFATAILQWLMLITLASYIYRAKAYQSTQVFSHWERINLTLVKRILKLGLPIGLAVFFEVSIFSTGAIVLSPLGDTLVAAHQIAMSVTSQLFMIPMSLAIALTIRVGMYYGEKNWVSMRLVQKLGLATATFFAMCTMSLIWFARPQIVAIYTQDPAVFDIALYLLLFAMAYQLMDAWQVGAAGCLRGMQDTKGPMWITLIAYWVVAFPVGTYLARVAKMGPAGVWLGLITGLSIACVLLLMRLYRNNHKLAQQS | Function: Multidrug efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49013
Sequence Length: 449
Subcellular Location: Cell inner membrane
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Q8UDF5 | MSSSVVAETVPSGSGSWFSHFKATLVLGIPLIGAQLAQLGIHTTDMVIVGQLGAEKLAAMVLAGQFFFVVFIFGSGFSVAVVPMVAQAYGQGDATSARRSLRMGMWVAIAYWLLALPIFFNAERILVYLGQNPNVAALTGHYLAIAKFGLLPALLFYVLRGLVSAIGRAGIILYVTIIMLVMNGLMAYVLVFGHFGLPAMGMNGAAVVAVIVNAFSFIFIVAYVQTREETKKYELFVRFWRPDWHALFEVLRLGLPISITILAEVTLFAAASILMGQIGTVQLAAHGIALQLASIAFMIPLGLSQAATVRVGVARGQGDFKNLIRASIMIYAIACGIALCGGILFAAVPEFLAKWFLDPKLPEAAEVLAYASSLVVIAGIFQLVDGIQAVTAGLLRGLKDARIPAMLALISYWPIGLALAWTMAFPLGFGGRGVWFGFVIGLSTAAVLLTVRFVLLVKREMKTAR | Function: Multidrug efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49726
Sequence Length: 465
Subcellular Location: Cell inner membrane
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Q5NYX9 | MSAPILFPLSAPESSFTIAGRLFHHAWPVLVAQLLSMSMLIADTVITGRYGTLDLAAVAVGSGVYISIVMLLVGVLQAVAPTVAHHFGARRVDAIGPALQQGFWLALMLALPGIALLAFPGFLLELSSVPADVAGKTRDYLLATAFGLPAVLLYRTFYAFNNALGRPRALMMISFIVTSTHIPLAWALVHGAFGLPPLGAIGCGISTAIVNWIAFACGAGYLAHNRDYRPYRLFANWQPPRRRDLLALLKLGIPMGLSTFIEVSSFTLIALFAARLGAEAVAGHRVVANLAALIYMLPLAISIAILVLVGQAAGAREPARARATVRVGMGLTVGLVALIGVLLWVGREPVVALFSADPAVRAVALGLVFYICIYQIFDAVQTVAAHALRGYKVTFMPMLLHALCFWGIALAGGYWLAFHAPGREQSPTVAGFWEASVVATILASVLFGWLLRVVMRRPQNVQT | Function: Multidrug efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49428
Sequence Length: 463
Subcellular Location: Cell inner membrane
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A0KEJ2 | MSTTTQSDAGISREIVVIGSGFAAQQLVKSLRKLDAEQPIRLITADSGDEYNKPDLSHVVSRGCAAAAMTRQSGSDFAEQQRIALLPHCPVLGIDPVRRLVLTEQGEFPYGQLVLATGASAVRPELPGSEHLVTLNSQQEYAAVEGAIQQARRILVLGAGLIGCELAMDMASDGREVTLLDLADSPLSALLPATLTQPLQQALRSQGVSLQFGTGLARIDGQPGDGWRVTLTDGRTSEQDLVIAAIGLRPNLALARGAGLAVERGILVGDRLQTSDPHIFALGDCVQWQGQLLPFLQPIVLGANALARTLLGTPTPLALPPMLVKVKTPRYPLQLAGRTQGEDLAWQCRWNSHGMVAEARDQAGELCGFVVGGDQMSAAFPLLRQLPR | 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
Sequence Length: 388
Pathway: Nitrogen metabolism; nitric oxide reduction.
Subcellular Location: Cytoplasm
EC: 1.18.1.-
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Q5E3X0 | MSLPIVIIGSGFASYQLIKTIRRTNNDCPIHVFTNDSGDDYNKPDLSHVFSKQQSPEEVVTLSGGDFAEQYNVILHRHTWVESIDTEIQAITANGEQYAYGKLVLATGSQTFIPPFHGDGCGDILTLNSLKEFAGIQQKVLESKKVLVVGGGLIGTELAMDLANAGKMVTLVEPNTHLLANMVPDFISLPLEKACKEKGITVNLSDCVQAVNKQEQGYRVTTSNGHSYYVDCVISAAGLKPNTKLATEANLMVNRGIVVDLNLQTSANNIYALGDCAEIEGKVMAYLQPILLSANALAKTLLGTDTALSMPNMMVKVKTPNYPIQLAGNTSTDIERWSVDIDTQGLCAKAYNINNQLTGFVVTNERVKNAFPLFRELNTTN | 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
Sequence Length: 381
Pathway: Nitrogen metabolism; nitric oxide reduction.
Subcellular Location: Cytoplasm
EC: 1.18.1.-
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