ids
stringlengths 6
10
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stringlengths 11
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stringlengths 108
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B0S919 | MFVLKSASPRRKQILFDLGFDLKIDPEHIDESQKELESPLEYLERMVHSKLGTLFEPNNVYLAADTIVVYQNQILHKPIDTNDAFRILKILSGKNHSVFSGAALRHPNGTEYFYEETMIGFQNWNDFEINEYIKRSKPFDKAGSYGIQDKEGPVLQWIGSYTNVMGFPLRSFLSRHELWIGSWEERIMRRD | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22348
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q72WC1 | MIVLRSKSPRRKQILESLDLDFRIESEDIDESSLKDEHPLEYLKRISLSKLGTRSKDELLISCDTIVVQENSILQKPENFSQAIEMLERLSGKTHIVYSGLGIYYNRLEQFAFDSSKVHFHTWNKEQIKKYIERYSPFDKAGSYGVQDIEGPVQSFEGSYTNILGFPIRMFFQYHELWKKYLKGNQA | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21940
Sequence Length: 187
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q9JXS2 | MGLELPLILGTSSVFRREQMERLGIAFQAASPDFDETPMLGESAPQTALRLAEGKARSLTGRFPEALIVGADQVAWCDGRQWGKPMNLANAQKMLMHLSGREIEFYSAIVLLNTVTGRMRRHIDKTVVVMRQLDELHILRYLEREPDAVYCSCALKSEDLGALLIERIESTDPNALIGLPVFRLVDFLKNEGVEVL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 21911
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q13VL1 | MSDSLNRPPRLILASSSPYRRELLQRLRVPFDVAVPAIDETPLAGETPEVTALRLAQAKARAVAGGLGAGVAALVIGSDQVATYDGLQIGKPGTHANALAQLQAMRGREVQFHSALCLFDSRSGTVQAVDVVTRVQFRDLPDAALEAYLLAETPYDVAGSAKSEGLGIALLEAIHSDDPTALVGLPLIALSRMLLAVGYPLLGAQ | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 21489
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q126I4 | MNSALNPVAASTAATALTPTSRPLVLGSTSPYRRELLQRLHLPFEVATPDVDETPLPGETPRLLAERLALAKARAVARNFPHAVVIGSDQVADLNGLPLGKPGTHERAVAQLRQMRGQTVVFQTAVAVVCLDSGFEQSSLAAVRVTFRNLTDGEIENYLRAEQPYDCAGSAKSEGLGIALLESIDNDDPTALVGLPLIRTCKMIQAAGVALFADRGEHP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 23286
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q9HZN2 | MPDLILASSSPYRRELLTRLRLPFESASPDIDESHRAGESAEELVRRLSASKAEALAGRYPQHLVIGSDQVAVLDGNILGKPHTPERAIQQLRDASGKSVTFLTGLALLNSASRRIQVACVPFTVHFRHLDESRIRRYVEAERPLDCAGSFKAEGLGVSLFRSTEGEDATSLVGLPLIRLVDMLLEEGVEIP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 21054
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q88LM1 | MLPLLLASSSAYRRELLARLHLPFTWASPDIDEQRLDGEPPVELVRRLARQKAEALAGSHPRHLIIGSDQVAVLGEQVLGKPHTFERACEQLLECSGQQVSFLTGLALLNSATGQCQVDCVPFTVTLRELSREQVERYVAAEQPLDCAGSFKAEGLGVSLFQSTHGCDATSLIGLPLIRLVDMLTKEGVMVP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 20929
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q3IHD5 | MKYPLILASSSLFRQSLLQKFNLPFDTFSPNVDESALNNETPAQLVKRLSELKARAASKHFSKGLVIGSDQVAVFNEQILGKPHNKHNAVKQLSLFSGHSVTFLTGLCVYDLTSGESKTCIEPFNVTFKTLTDAQISAYCDAEQPYNCAGSFKSEGLGICLFEKLTGDDPNSLIGLPLIKLSQLLAEFGLDVLSAQSNTPLS | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 21963
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
O27140 | MKILITGRPGSGKSTMVGRLRDYLEGMGFSVGGIITPEVRVGGSRWGFEVVDIASGRRGLLASVETEGPRIGRYGVNVGVMDELAVPAIRRAMLEDDCIIIDEIGPMELKSREFRRTVDEVLSSDVLLIAAVHRKTLQSIKKREDIRVFVVDPEKRDRVYLRIIDLLGDYHGMR | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19426
Sequence Length: 174
EC: 3.6.1.15
|
B2A6V4 | MTESNILLTGKPGIGKTTVIKRTVELLSCSSTGFYTREIKRGDPRVGFEIISLQTGERLPLAHTDFTTAEDRVGKYGVKAENLLGFLKEINEAMTSNKPQCLVIDEIGKMEFFTPGFHETVDKAFQSSYPLLATIMKKSHKFCDYLKNRGDTDVIEVTENNRDDLPEKLAKRIEEQL | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19950
Sequence Length: 177
EC: 3.6.1.15
|
Q8ZTE6 | MTWRERAELRIGISGMPGVGKTTLVLKIAELARSRVKVCGFVTVEVREGGTRIGFDVVDLANGRRMALARVGRGEPSVGKYVVNLEACNVISEALRRECDLKIIDEIGAMEFKCKNFGEDLQTALHTSPRVIATVHRNYIDIAKKLGLEIIWLTRENWGLVFRQLLIQLGLTQ | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19335
Sequence Length: 173
EC: 3.6.1.15
|
Q97WP0 | MLEESKNALRVFITGNPGVGKTTILLFLINKLSENNYKVAGFYCPEVRENGRRIGFRIVDITTNEGDWLAKENAPGRVKIGKYTVLEDSAKRITEITLSNINKADVLAIDEIGPMELKIPTIKKLIETILNNQKPLIAVLHRTQKPMGGRIYVITVENRDSIKYEILNYILSSLD | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19730
Sequence Length: 175
EC: 3.6.1.15
|
A3DNY5 | MKNYIITGRPGIGKSTLFNNIINTLRKSGIIVGGIKSPEVRDSKGFRIGFKIIDLMSNEEGWLAKRNYYSTIKVGKYGIVLDESSRIIREALRKALEKADVIGIDEIGPMELKIHVFRTMLEQVLNSDKPKILVIHYRLRDPSILDKIYRVENEKYVLTEHNRDLLNKVLPQKIVMEIKQIIKK | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 21219
Sequence Length: 184
EC: 3.6.1.15
|
Q4JCN8 | MDKPFRIYITGKPGIGKTTLLFNIYRILKEKNWRITGFYCPEVRVNNTRMGFKIKSVLSGKEAWLARVDARSGIRIGKYYVVLEDNFVRQLEEEIFSFPDIILIDEIGPMELSSVSLKNLINKILTSNYPVIAVVHRSIKFDDGVIYEVTIQNRDILLEEILGRVTSNKNNI | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19842
Sequence Length: 172
EC: 3.6.1.15
|
Q96YL7 | MQTRLRVYITGEPGVGKTTIFLKVIDKLKSQGYSISGFYCPEVREKGQRIGFKIKSLDNEVEDWLASIYAKSSIKIGKYYITINEDIINKIKEKISKSEIIGIDEIGPMELSVPKLKEIIDYVLNEKPIVVAVVHRKISFKDGKTFVVTYENRNRLDNEIFNYIISSIQ | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19398
Sequence Length: 169
EC: 3.6.1.15
|
Q9HJH0 | MIPLAIKIGITGPVGSIKSEALQKIIDMLKNDNLNVQGVLVSKVTNNGKLTGYTIEDIESKRKAQFCFDNFVSRVKIDKLGVDTKILEEILIPSLQKARETADVIVIDEIGKLENTTKKVHAEIEETLKCGKPLIVTLHKRSRNPVLQEIKSLEGVRVFDITPINKNILPFKVMHVLKGEE | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20194
Sequence Length: 181
EC: 3.6.1.15
|
Q5JF42 | MALRIFVTGPAGVGKTTLVERVAREVDRWGYIVGGVITREVRRGGRRIGFKITALDTGEEGTLASLRGTSHLPGVPFGKYVVHVDEIERVAVPAIRRAIVEADLIVIDEIGPMEYTSNEFIRAVGEVLKSEKPLLAVVHRKFIDRFRPLGEVHTLSFENRNAEFGIILDRVMKELKGIRG | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20001
Sequence Length: 180
EC: 3.6.1.15
|
Q9WXP3 | MKILITGRPGVGKTTLIKKLSRLLQNAGGFYTEEMREGEKRIGFKIITLDGEEGILARTDLPSPYRVGKYYVNLKDLEEIGVRSLERAFQEKDLIIVDEIGKMELLSRKFREVVEKIFDSEKDVIATIKKSSDPFVEKIKNRNDVVIFELNEKNRNSLLNEILSVLKFNRGEKQ | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20034
Sequence Length: 174
EC: 3.6.1.15
|
A1RYX5 | MAAKNFLLTGRPGIGKTTCVVKTAELLVSRGVKVGGMVTHEVREGGSRVGFKVRDLLTGREGFLAKVGAGAGPRVGKYVVHVEELEAVGVGAILRAVSEAQVVVIDEIGPMELYSPSFLPAVLKALDSDKPVLATIHERESSSGRLRGILERGDVKLYTVTLQNRDLLPPQLAREIASLVAR | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19393
Sequence Length: 182
EC: 3.6.1.15
|
Q37165 | MIIYATAVQTINSFVKLESLKEVYGLIWIFVPIFSLVLGIITGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKENLRPSRGNTPLFSIGPSIAVISILLSYSVIPFSNHLVLADLNIGIFLWIAISSIAPIGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWRQPIGFIIFLISSLAECERLPFDLPEAEEELIAGYQTEYSGIKFGLFYVASYLNLLISSLFVTVLYLGGWNISIPYISILELFQRDQIFGTTIGIFITLAKTYLFLFVSIATRWTLPRLRMDQLLNLGWKFLLPISLGNLLLTTSFQLFSL | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40021
Sequence Length: 360
Subcellular Location: Plastid
EC: 7.1.1.-
|
P51931 | MEFILSLIGSLLLIICVLVSVAFLTLLERKVLGYIQIRKGPNKVGLMGIPQPFCDAIKLFTKEQTYPLLSNYLSYYISPIFSLFLSLFVWMCMPFFVKLNSFNLGGLFFLCCTSLGVYTVMVAGWSSNSNYALLGGLRAVAQTISYEVSLALIGFKILLFSLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18169
Sequence Length: 163
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P18929 | MEFILSLIGSLLLIICVLVSVAFLTLLERKVLGYIQIRKGPNKVGLMGIPQPFCDAIKLFTKEQTYPLLSNYLSYYISPIFSLFLSLFVWMCMPFFVKLYSFNLGGLFFLCCTSLGVYTVMVAGWSSNSNYALLGGLRAVAQTISYEVSLALILLSFIFLIGSYNMIYFFFYQVYMWFLIILFPMALVWMSISLAETNRTPFDFAEGESELVSGFNVEYSSGGFALIFMAEYASILFMSMLFCVIFLGCDVFNLLFYMKLTFISFVFIWVRGTLPRFRYDKLMYLAWKCFLSFSLNYLLFFIGFKILLFSLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35957
Sequence Length: 312
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q2I3H4 | MFLINVLTVTLPILPAVAFLTLVERKALGYMQLRKGPNVVGPYGLLQPIADAIKLFTKEPIYPQTSSKFLFTVAPILALTLALTVWAPLPMPYPLINLNLSLLFILAMSSLMVYSILWSGWASNSKYALMGALRAVAQTISYEVSMTTITLSMVLMNGSFTLTAFATTQEHLWLIFPMWPLMMMWFTSTLAETNRAPFDLTEGESELVSGFNVEYSAGPFALFFMAEYANIIMMNALTVILFMGTSCDPQMPEISTINFVMKTIILTICFLWVRASYPRFRYDQLMYLLWKNFLPLTLALCMWHISILISLACIPPQA | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35789
Sequence Length: 318
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
Q9B6E8 | MIINIVEILIFLVCVLFSVAYLTVAERKTLAYMQRRLGPNFVGYYGLLQAFADAVKLLLKEIVLPKESNYIILVISPLITLITALIGWVVIPLGPGITLGELNLGILFSLAIGSLGVFGSLLSGWSSNSKYSLLGSIRSTAQLISYELILTSIFIIIIMFVSSLNITTIIETQRVVWYCIPLLPLLLIFFIASVAETARPPFDLTESESELVAGYFTEYSGSPFVFFFLAEYSNIILISAFNGYLLLGGYLSFNYSYLFNILFNDYSYVSFLFEGLINSSAYAIKLVFLMFSFIWVRAAFPRFTYDNLINFCWIILLPLLFGIFLIIPSTLYIFDSFPTLI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38348
Sequence Length: 341
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q35140 | MIIMTILSLLLSNAVTLRRDISILFNRIVIIALIYCILHDTMSLSIISKGVGLHGGLLHITNITQVFQIFIFLISILILQLTSFDPIKKFYIMRHPRFINKWPRAIGYSIPLSSIQAVLKDYLFKIQGFNKEHLKIIEYPLILLFVICGAVFLMSTNDLVSIFLSIELQSYGLYILSTIYRNSELSTTGGLIYFLLGGFSSCFILLGASLLYANSGTTSLDGLYIINSISDVNDNMTSWYKSYYLNFSLLIFSVGFLFKVSAAPFHFWSPDVYDAIPTIVTTFVAIIAKISIFILLLELVYHTNNYLSEFSWIYGLLVSSFLSLIIGTVVGLTQFRIKRLLAYSTISHLGFILLALSVSTQSVESTQAFIFYLIQYSFSNLNVFIILITIGFSLYGYVWNNKEYKNLLDINNSPVQLISQLKGYFYLNPLLSLSLAITIFSFAGIPPLVGFFAKQMVLSAALDNGYIFLSLIAILTSVVGAVYYLNIIKEIFFYSPGHKLKTVDVENTWPFPVKRDLKLNDSNAFSISYDRYTVSSPLSSGYTISSPFSITISIITIVILLFIFMNKEWLSMGTIMVQVLFST | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65743
Sequence Length: 583
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q36451 | MTPMTTLIMLFSLLLGTTLTLTSSHWLLMWMGLEVSTLAIIPLLTYTNHPRSIESAIKYFLTQATASMLLMFAASLNTWMTGHWTLMQIDNTISSGIMTFALAMKLGLAPFHYWVPEVLQGSSLMSGMILLTWQKLAPISIIYQISPTLNMDILLTLAISSTLLGGWNGLNQTQLRKVMAYSSIAHMGWMVLIIIYFPTLTTLNLTLYIMSTVALFTVFHTTNITKTKPLSLMWNKAPIMTLAIILLLLSLGGLPPLTGFAPKWLVIQELIKHDNMIMATVLAITALLNLFFYMRIIYSSTLTTFPTTNNNKFHWYSKSTKNPLSLPTLVILSTTLLPLTPMFITLS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38823
Sequence Length: 347
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P12771 | MHQMISIFLFLTVVSGTIIVVSAENWFVIWLGLELSTLALIPILWFCFTPRNIEATIKYFLVQAFSAALLLNSALIQAWFSGSWSALIPMESFPSLCLSVALAFNLGLAACHFWLPDVLQGLPFIQGLIIATWQKIAPLFLLFYFNQLNFSYFIILAALISILVGGWGGLNQTQTRKILAFSSIGNMGWIVVTSAFSLGTAAMMLFIYLVINTSIFLILDFLSIFTLGHLNNTSQLSPISITLVILTILSLGGLPPLTGFILKFSSLYSLINNGFIFFSSVMIIGSLLSLFFYLRIAFNTTLILFPQHLISLTAWRNSTEAEPLMAKTWLVSSFSVLSILAIPLTIPLYINV | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39010
Sequence Length: 352
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P15577 | MRAHLLHCELAFSFGKYFYSTSFLNLLMINLMFSKLGAIFFLNLALYLLALALFFFFLFNVKVALLKSVSQIYYFNNIFFFKFFVLIFFLNLAGIPPLLGFFLKFLIFFFLFFKTNLAFILIFLGFNMATLFFYLSTVKSFVNRKQASVLNSFNFFIRAELSFLYFFNFFYFFLFFAFFFLDSTFLIFLNLFF | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23181
Sequence Length: 193
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q33819 | MHRNILMVLIANVVLGTLIVLSSHHWFTLWVGLEMNTLSILPILSYQFTPRNVESSVKYFLVQSVSAGIVLNVVIIQAWLYSSWSLMEPLNQATSFLMTLALGLKLGLFPCHYWFPDVIQGVGFIQGLVLSTWQKIAPFAVLVYVVESLNISLLASLGVLSVLVGGWGGLNQTQMRKIFAFSSIAHIGWICSTVGYSVSVACVMLVAYIIINSSVFFMANSFDLKSLSHVGRLSLYNFVGGAGLVLSILSLGGLPPLFGFLIKFISLKCLVENGCFILAGVLVMGSLLSLFFYLRIAFNSSLTLFPQHSLVVFSWRSNRNQTGGFTSEGVLLSVSFGISSLGLVCLPVFISLLN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38654
Sequence Length: 354
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
P03897 | MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor . Essential for the catalytic activity of complex I .
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13186
Sequence Length: 115
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q34950 | MILTALSSAIALLVPIIILGAAWVLASRSTEDREKSSPFECGFDPKSTARIPFSTRFFLLAIIFIVFDIEIVLLMPLPTILHTSDVFTTVTTSVLFLMILLIGLIHEWKEGSLDWSS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12982
Sequence Length: 117
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P16265 | MLEFAPICIYLVISLLVSLILLGVPFLFASNSSTYPEKLSAYECGFDPFGDARSRFDIRFYLVSILFIIFDLEVTFFFPWAVSLNKIDLFGFWSMMAFLLILFIGSLYEWKRGALDWE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13711
Sequence Length: 118
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P26847 | MEFAPIFVYLVISLLLSLILIGVSFLFASSSSLAYPEKLSAYECGFDPFDDARSRFDIRFYLVSILFIIFDLEVTFLFPWAVSLNKIGLFGFWSMMVFLFILTIGFVYEWKKGALDWE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13688
Sequence Length: 118
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q35100 | MYTEFYGILVLLIFSVVLSAIISGASYILGDKQPDREKVSAYECGFDPFGTPGRPFSIRFFLIGILFLIFDLEISFLFPWCVVCNQVFPFGYWTMIVFLAVLTLGLVYEWLKGGLEWE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13517
Sequence Length: 118
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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B1X495 | MTIMLEAYLTLAAVLFCIGVWGLINSRNAVRVLMSIELMLNAVNINLMAFSNYLDGELIRGQVFAIFVITVAAAEAAVGLAILLSLYRNRQTVDMERFNLLRW | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11540
Sequence Length: 103
Subcellular Location: Plastid
EC: 7.1.1.-
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Q36423 | MSMFGLFTCLSIYFSGVYVFCSKRKHLLVVLLSLEYIVLSLFMLIVLFLVEFDYDYFFPVIFLVFSVCEGALGLSILVSMIRSHGNDFFNSFFLSLC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11188
Sequence Length: 97
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q34948 | MYSSIMSLVFLLPIVAVVNLISNQSHFLMTLLSLEGITLSLVLFVPISLSIMSASNVSISVILLTFGACEASLGLSLMVLMSRSYGTDMLNSLTANKC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10463
Sequence Length: 98
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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O79554 | MELMKMTLYTTFMITIIALSLQQKHLMLALMCVETMMLIVFTMLVMFNSNSLTVSQTPMPIILLTISVCGAAVGLSLVVAITRTHGNDFLKNLNLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10653
Sequence Length: 96
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q9XL45 | MIPTYMNIMLAFTISLLGMLTYRSHLVASLLCLEGMMMSLFIMTTLIASNTHSPLINIMPIILLVFAACEAAVGLALLISISNTYGLDYIHNLNLLQC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10767
Sequence Length: 98
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q36903 | MRLTILLIIIGLIGYIINSGPLGRTNIIKLFISIEIMLLGVTLLIILSGYNNDDILGLIIGIIVLIITGIESAIGLTILVNYYKIKGSLPTNI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10048
Sequence Length: 93
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P03904 | MTLIHFSFCSAFILGLTGLALNRSPILSILLCLEGMLLMSMDGIVLTPLHLTIYLSSMMLYIMLPFAAPEAATGLSLNSDHYTTHGTDKLFSLNLLEC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10710
Sequence Length: 98
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q9B6D4 | MFIGTIILVLSFLGFVFNRRNIILAFICLETMLLGINLILLRNSVLFDDISGSLFAIVIIILAGVESAIGLSLLVSYYRLRGVINSYGI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9811
Sequence Length: 89
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q37375 | MAFLLYYTLFISFMLWLAALLIISFSVYGSPEKVKLIKKTSLFFSFFQFILIIFFWILSDNISVLAEFDIYNFQFYKQWLFLYNFHYVIGMDNISLLFLLLTFFLTPICILISWNSIKYRYNSFIICLIFITFILFNIFCVLDLVFFYIFFESILIPMFILIGVWGSRQRKIHAVYQLFFYTLLGSLLMLLGILVIYSHIQTTDIRVLYNTNFSFYRQLILWASFFFAFCVKVPLFPFHIWLPEAHVEAPTVGSVILAGVLLKLGTYGLLRFVIPIFCDATYFFLPLVYTLCLLGIIYTCCSTIRQVDLKKVIAYASVSHMSFVILGLFTSNIQGIGGSVFLMLSHGIVSSGLFFCIGCVYDRYKTRILRYYSGLVSTMPIFSLCLFILILSNISFPGTSSFIGEFLILLGLFENNHFAALIATFSIILTAVYSIWLYNRIIFNRLVVNYYLRFSDFSKKEFVVGFIFCFITILFGLKGSYIISLIEAPLYVYLSFK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57768
Sequence Length: 497
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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B1VKJ3 | MEFIYKYAWIVPFLPLSASVPIGLGSLFFPGATKSVRRTWALISIFLLSVAMFLSFNLFLQQITGGPIYRYFWSWVINNKFSLELGYLIDPLTSIMLVLVTTVGTMVMIYSDNYMSHDKTYVRFFAYLNFFNASMLGLVISPNLLQIYIFWELVGMCSYLLIGFWFTRPSAANACQKAFITNRAGDFGLLLGILGFYWVTGSFEFQYLSEKLNELTAIDGVGSFFVTSCAFLLFLGPVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLFPLFKALPLIMYLISWIGGITALLGATMALAQKDLKRGLAYSTMSQLGYMMLALGIDSYRIALFHLITHAYSKALLFLGSGSVIHSMEPIVGYCPRKSQNMALMGGLRKYMPITGITFLLGTLSLSGIPPFACFWSKDQILSDSKLYSPIFGGITWFTAGLTAFYMFRMYLLTFEGDFRVNLVNSYNNHITLYSTSMWGEEESRILNRTRADSMSNQIIGRNNSFSKEAFQISNKMEGLYKKNRGLVVTYPFFYKGSFAYPKESGKAMLFPLVVLGIFTLFVGLIGVPFFRSGMRYDILSQWFASSTAPFDKKHPENWSEFFIDAIPSVGIAFLGILIACILYRPIYFLSQDVYHKTNPHMKIIMDQSINIIYNWSFYQAYIDIYYDIILIKGIRGLAETSHSFDQWAIDGIPNGVGFLGLFVGEGMRCLGGGRISSYIFFSLFCVLISILIYYYSFSFYP | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83621
Sequence Length: 741
Subcellular Location: Plastid
EC: 7.1.1.-
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Q2QD43 | MEYTYQYSWIIPFISLPIPILIGVGLLLFPTATKNLRRLWSFPSILLLSIVMIFAVYLSIDQINTSYIYQYVWSWTINNDFSLELGYFIDPLTCIMAILITTVGIMVLIYSDNYMSHDQGYLRFFAYMSLFNTSMLGLVTSSNLIQIYIFWELVGMCSYLLIGFWFTRPTAANACQKAFVTNRVGDFGLLLGILGLYWTTGSFEFRDLFQIFNNLIDNNEVNFLFLTLCAVLLFAGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFIAIPYIMNLIALIGIITVLFGATLALAQKDIKRSLAYSTMSQLGYMMLALGMGSYQAALFHLITHAYSKALLFLGSGSIIHSMESVVGYSPDKSQNMVLMGGLTKHVPITKNAFLLGTLSLCGVPPLACFWSKDEILNDSWLYSPIFAIIACSTAGLTAFYMFRIYLLTFDGHLNLYCKNYSGKTNNSLYSISLWGKEGSKIIKKNFPFFSLLTMNNKERSSFWMKKTTYPFNSNVTKKMRPFVSSPHFSTKNTFYYPYESENTMLFPMFVLSLFTLFVGVIGSPFTQFNQEAIDLNILDKWLTPSINLLHESSKDSENWYEFVKNATFSVTIAFFGIFIASFFYKPTYSSLQNLNFRNSFVKSFTKNFFFEKIINIIYNWSYNRGYIDTFYRISLIGGIRILAELTYFFDRRIIDGITNAVGILNFFVAESIKYVGGGRISSYILLYLVYLVIFILVIYFVFF | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85207
Sequence Length: 748
Subcellular Location: Plastid
EC: 7.1.1.-
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A6MMR6 | MEHTYQYAYIILFLPLPVTMSIGFGLLFVPTATKNIRRMWAFVSVLLLSMVMGFSVNLAIQQINGSFIYQYLCSWTINNDFSLEFGYLIDPLTSIMSLLISTVGIMVLMYSDNYMSHDQGYLRFFAYMSFFNTSMLGLVTSSNLIQIHIFWELVGMCSYLLIGFWFTRPIAASACQKAFVINRVGDFGLLLGILGFYWITGSLEFRDLFEIVNNLIHNNGVNFRFAILCACLLFLGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLRPLFIVIPYIMNLISLIGIITLLLGATLALAQGDIKRSLAYSTVSQLGYIMLALGIGSYRAALFHLITHAYSKALLFLGSGSIIHSMEPVVGYSPDKSQNMVLMGGLKKYVPVTRTTFLLGTLSLCGIPPLACFWSKDEILTDSWLYSPIFAIIAYFTAGLTAFYMFRVYLLTFDGCLRVHFQNYSSTKRSLFCSMSVSVWGREPLKIDNQNLPFLILKRNINNNKVFFFSFFSKGTYKNKIYNNVINRMQYFRTYFQNKYTYMYPHESENTVLFPLLVLVLFTLVVGLIGIPFDQGVIDFDILSKWLTNPFQKNLNHSVDWYEFLTNAIFSVSVSLFGLFIASIFYGSVYSSFQNLDLINFFVKRGPRRILLDQIKNVIYNWSYNRGYIDIFYTKGLTMSIRRLSKLIQFFDRYIIDGITNGIGVASFFIGEGIRYIGGGRISSYLFLYLSYVSIFLIFYQYFDF | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85075
Sequence Length: 746
Subcellular Location: Plastid
EC: 7.1.1.-
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Q9ZZM3 | MHPTTLILSSTLLMIFALLLYPLITTLNPTPQQENWALTHVKTAIKMAFLVSLLPLFIFLDQGTETIVTNWQWMNTTTFDINLSFKFDHYSIIFTPIALYVTWSILEFASWYMHADPNMNRFFKYLLLFLIAMIILVTANNMFQLFIGWEGVGIMSFLLIGWWYGRADANTAAMQAVIYNRVGDIGLILSMAWFATNLNSWEIQQMFASSKELDLTLPLMGLILAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRLHPLMENNQTALTTCLCLGALTTLFTATCALTQNDIKKIVAFSTSSQLGLMMVTIGLNQPQLAFLHICTHAFFKAMLFLCSGSIIHSLNDEQDIRKMGGMHNLTPFTSSCLTIGSLALTGTPFLAGFFSKDAIIEALNTSHLNAWALTLTLLATSFTAVYSLRVVFFVSMGHPRFTATAPINENNPSVINPIKRLAWGSIIAGLLITSNFLPSKTPIMTMPLPLKLAALLVTISGLLIALELASLTNKQFKTTPNLITHNFSNMLGFFPAIIHRLAPKLNLTLGQTIASQMVDQTWFEKIGPKGVVSTHLPMVTTTSNIQQGMIKTYLTLFFLSTALAVLLTLT | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67610
Sequence Length: 612
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P50368 | MNLIILFLPFVGAFISGFLGRFVGTTGAQILTCACILTSALLSLYYWLSINELIIGLFSFEGDQVYFTDWNFLSNNTFINLGTWVDSEYIKISWEFTFNEITLPFLFTVLFISFLIHLFSVNYMANDPHIQRFFSYLSLFTFFMAILVTGANYFVLFVGWEGIGVVSYLLINFWFTRIQANKAAILAFNTNRIGDMALSIAYFVMLPAFGSADFSTVFSLPAYINQTTITIIGFLLLVGAMAKSSQIPLHNWLPGSMEGPTPVSALIHAATLVTAGSYLLIRSSPILEYAPTVLLVITIIGASTAFFAATCGLVQNDIKRIIAFSTISQLGYMVMAIGLSQYNVALAHTLFHAYFKALLFLGAGSVIHAFGDIQDVRKMGGLINFLPFTYAVMLVGTLSLLATPFLTGFYSKDLIIELAYGQYSFSGTYAYILGSVTAGLTAFYSFRLISLVFLTKPNGNKQNYLNSHEASITVIIPLAVLAIFSIFFGYVTSDLFVGIGSDFFANTIFIHPNNISLVEAEFSMSLIFKLLPTIFSLAGTLFALYLYNYNPHFIDSLVENNLGKKVYGFLNGKYYFDVIYNNYIISKGLQFGYNISKEIDRGVIELIGPYGMSNVLYSTSANIAKLDTGIITTYALYITLGLLSLLFIVFAPMLVNTTINDEFRLIILFIFTLIVNSAYLNKKLSK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76186
Sequence Length: 686
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q9ZZ44 | MNMIIFNSAFLLIFIILLYPLISSLSPKELYPNWSSSHVKTAVKTSFFISLIPLFIYLDQGLESITTNWNWINIGPFDINMSFKFDMYSIIFTPVALYVTWSILEFALWYMHSDPNMNRFFKYLLLFLISMIILVTANNMFQLFIGWEGVGIMSFLLIGWWYSRADANTAALQAVIYNRVGDIGLILSMAWLAMNLNSWEIQQLFILSKDKDLTLPLLGLVLAAAGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRLHPLMQDNQLILTTCLCLGALTTLFTAACALTQNDIKKIVAFSTSSQLGLMMVTIGLNQPQLAFLHICTHAFFKAMLFLCSGSIIHSLNDEQDIRKMGGLHKLLPFTSSSLTVGSLALTGMPFLSGFFSKDAIIESMNTSHLNAWALILTLIATSFTAIYSLRLIFFALMEYPRFPPLSPVNENNILVINPIKRLAYGSILAGLIITSNLPPMKTQIMTMTPLLKLSALLVTIIGLLLALELASLTNTQLKTTPTLSTHHFSNMLGYFPMVIHRLVPKTNLKWAQHISTHLIDLTWSEKIGPKSTLIQQTPLIKLSTQPQQGMIKTYLTLLFLTLTLAVLIIAI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68082
Sequence Length: 610
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P15552 | MVISPSLIISSLNLGILTILLGSIFFFSKSYFSKGNVNFPLIKTTSACLSVNNDKEETIEYNSGPFAMAILKVLAFLSVLSLLVTCNNSIQSINITLSLWLSNTPLNISLNFIYDQYFLVFLSVALIVTWSIMEFSFYYMTEDPNSSAFFRLLTIFLLNMLILTCSNSLFLIFLGWEGGGFLSFLLISWWTTRNDASSSALEAVITNRIGNIGLITFMALSALNFNSSNLTNILSSNENLTPLLPFLLFGLILAAAGKSAQFGLHPWLPALLEGPTPVSALLHSSTMVVAGVFLLVRTSELFSSPLITHSLVLILGGTTALFAASTAIAQHDIKKIIAYSTTSQLGLMVTAIGIGQPALAFFHICTHAFFKAMLFLCSGSVIHSLSDEQDLRKMGGLSKLLPVTSSCLILGSLALMAPLLAGFYSKDLILEATSASVLNLLGIVLSIVATMLTAVYSFRIIFFCFSLSPSCSSPFSHSEENFNLNNALLRLATGTIASGWFFSNLLFAPPSFNVTSLAKGTPLIVPIIGVAALFMSLISSTSNSIGSNAHSATTSQWFFVDAVHLSIITMSLALSFFSSRTLDRGWQENIGPQGIAPTSTALSKISQAGQIGLIKRYILSSMASVLVILALSLLILS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68558
Sequence Length: 637
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P04540 | MFLIFFLFFIMFGFISGSFMFGRNFLSFWLSLVMIIFIVLCMIFSFLMVSVCLYGYYYYDFCLILMLDFCFIWLTYVCSGFYMFIMLLINMVFCFIVFYAFYYMYFDMLLGRFLIIFWIFVVCMNLFILSYDFLTAYCGWELLGLFSFFLISYFWYRFFALKFGFKAFFIGKIGDVLLIFAFSIIFLSNGFCMTTFYFLNFFCMDYYYIEFSICLLVGCAFTKSTQFGLHIWLPDAMEGPIPVSALIHAATLVVCGIILLSFVYWCFDFWFSYFYNLIGWSTLILILMTLCVFYNFDVKRYVAFSTICQISFSMFCCLCIDIYIGSLFFCYHMFYKATLFIVLGIWIHIFFGLQDLRCYFFMYFCGCVLARLLLIFAILNSCSIWFLCGFYCKDMLLALLMLLSFYNIIEFLFISIIFIFFTMIYNYFLLFFLMFVFKCFCLVDCLFLLFDYECCLVYCLISLYMCILSIFFIIDFVCIFVFSSYCVFWSFFLNFYNFFDIAIFVVFLILSVGFLYYGCLFFYFFNIDCIMLFWRIFFVIIILVVFMIFCCWYFVCMIIFMLLFVWNFVIYFRYNLKYCLFFCILWILYV | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71495
Sequence Length: 590
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q0H8X0 | MYLSLLLLPMFGSAVTGLLGRKIGVTGAHIITCSCLITSAILAIVAFYEVGLCNSSVSINLISWIDSELMDVSWGFMFDSLTVSMLLPVLVVSSLVHIFSVDYMSADPHNQRFFAYLSMFTFFMLVLVTGDNYLIMFVGWEGIGISSYLLINFWFTRIQANKSAIKALVVNRVGDMFLSIGFFAIFFVFGNLDYSTVFSIAPFINETIITIIGLLLLLAAMGKSAQLGLHTWLPDPSMEGPTPVSALIHAATLVTAGVYLLLRSSPVIEYGPTTLIVITWVGALTAFFAASTGLLQNDLKRVIAYSTCSQMGYLFMACGLSQYNVALFHLVNHAFFKALLFLAAGAVLHATYDQQDQRRLGGLIGFLPFTYTAILIGSLSLIALPWLTGFYSKDLILEVAYGQYEFSGQVAYWLGTLSACLTAFYSLRLISLTFLTYPNASKSVYLHTHDAPTIVMIPLIILSLLAIFFGYVARDLFVGMGSDFLSPSLFTHPSHITLIEAEFGLPQIIKLLPAIGTLLGAGLALYLYHMLPVFTIDLTNSTLGQKLYRFFNGKYYVDVIYNHYIIYGGLQLGYVISKVLDRGIIELVGPYGLATGLTSGSKDIAKLDTGNLTSYALYLAIALVTLIMILLSPVLLNAALINAPLILVLLVAMVCIPYINSSSNDTVTTVQVKL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73658
Sequence Length: 674
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q37024 | MILFITLPLLNVIISGLLSRYIGVNNIKRLNIINLFIILILLIYYYINIIKTDNEYTLKIIEWINIEYLNINYSFNLDLLSITMLIPIILISLIVNIFAWEYMKDDSHNPRFYTYLALFTLFMIILVLGDNYLILFLGWEYIGIASFLLIGFWYNNIDNIKSSLNALFINKIGDIFFIIALIYLIYIYKSLNYSLIFSLVSYINIDINNIIILCLVIAASAKSAQFGLHNWLIWAMAGPTPVSVLLHAATLVIAGIYLLMRSSPILENCPNILLFNLWLGAITSLISGLIAINSNDIKRIIALSTMSQLGIMFISIGLSSYNLTLYHVLCHSLYKALLFICAGTIIHSLNNELQDIRFMGGLLIYMPITYICMLIGSLSLMGLPSLTGYYSKDIIIESSIGIFTISGLIIYWLVVLSSLLTNIYILKLIYYSFINIPQLNKYIYNSLSLNNTYSLPFNFKFNFDKSWMAIICMIILSIGSLFIGYLLQDIYLGQGNSINGLFIYPNNLNLIETHFAINIYYKWIPIFNIFISILLIIYLYEFNYKLLYIYNNPLFYNFYILFNTRFLFDQILNNYIIRYTLYLSKSLNSLLDKGFLYTLGPNGLNYLLNLLSFNIIKFNTHLFNHYLIYISFSLLLFIYLQFDL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74560
Sequence Length: 644
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P03922 | MNFPLIFNSSMLITISILILPILMSTFNMNIMNLHHLIKTSVKTAFLISIIPLIIFLDQGLESITTNFHWMNINTFDINMSFKFDIYSSIFIPIALFVTWSILEFATWYMASDPMISRFFKYLLTFLVAMVILVTANNFFQFFIGWEGVGIMSFLLIGWWYARAEPNTAALQAVIYNRVGDIGLILSMAWVAMNLNSWEMQQVFMLNSDNLTLPLLGLILAATGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVVAGIFLLIRISPMMNNNQTALTICLCLGAMTTLFTAACALTQNDIKKIVAFSTSSQLGLMMVTIGLIFQLAFFHICNNAFFKVYYFFCSGQYSSCLNDEQDIRKMGGLQNSLPITTSCLTIGSLALTGTPFLAGFFSKDAIIEALNTSQTNTWALTLTLIATSFTAIYSFRVIFFASMGHPRSNPLSPINENNKTVINPIKRLAWGSIVAGLLIASNMLPINSPIMTMPTLAKQAAIIVSVTGLIIAMDLSKLTTYINQESKTNIHSFSNLLGFFPTIIHRMMPKTNLNLAQNIATHLIDLSWYEKSGPQGMVNQQLPMIKTTTNIQQGLIKTYLTLFLMTSAIIITLF | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67156
Sequence Length: 604
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q9B6D3 | MYNAISLIIILPCISWLFPLFFGRQLGYVFVTRMTSTLIIITTLITYYYFYQLLGNNNPINLELFNYLNIDYLDINYNFEIDALTITMLLAITTISSMVHIYSIGYMETDPHQVRFFSLLSMFTFWMIILVTGSNYFVLFVGWEFIGVTSYLLISFWVTRLQAMKSALSAVLMNRFGDAFFVLGLCVIAYVFGTLNYSTIFATAYLINTDLLVLIMLALFIAAMAKSAQFGLHNWLTLAMEGPTPVSSLLHAATLVTAGIYLLLRSANILEYTPTVLFIILWIGALTTLSAGLIAICSNDLKRIIALSTMSQLGMMTIAIGLSAYNLALFHLLGHAFFKALLFMSAGSIIHSILNESQDIRTYGGLLSYLPYTYICITIASLSLMAMPGLTGYYTKDIIIESTYGSYSISNYVVYWIAYLSAVLTCVYSMKILYLTFYSNPNNNTITYYNAHESNIYITLPMFILAIFAMFAGWILKDIYLGVGTDFVGTHILPNNFSYFDTEFSITQFYKLLPLISAILVSILIVVLNEFFAIVFNLNNKYINTVYSIFNQKLVSDQILNHFIIFKGLVTSGNIAHHVDKGSLYRLGPVGINRLLNKASYNVINLSSNTRSSLSMNSMLILITIVSLLLLVLVMNVNFIIVIPVLISILYILFS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73705
Sequence Length: 655
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q85FH2 | MNISELIHDFVLALVELGILLGSLGAVLLVNTVNSAFSLGLVFTCISLLYFVLNADFVAAAQLLVYVGAINVLTVFAVMITDEPAGSETTARGIGYIITAGTCTILFSILSFVIHNTKWSDLSLIPQSGISTSGTLGSNVQQLGYKLLGEFVIPFELLSILLLAALVGAINLARNEDAFIVNKKSAASAPYKNSTFF | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20866
Sequence Length: 197
Subcellular Location: Plastid
EC: 7.1.1.-
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Q37626 | MDFLFYIFSSLTLISGSLVIQARNPVHSVLFLVLVFFNAAGLLVLLGLDFFALIFLVVYVGAIAVLFLFVVMMLNIRITEISEKRLRYLPVGGVLGVLFLFEICILIDNDCIPLLSYDIENTALLANYNQLSFIDWRMYLSTSHTIDALGSLLYTYYFYFFLVASLILLVAMIGAIVLTMQKGIRIKRQQVFLQNTRDFAKTIRKVA | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23536
Sequence Length: 207
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P03926 | MTNYMFILSLLFLTGCLGLALKPSPIYGGLGLIVSGCIGCLMVLGFGGSFLGLMVFLIYLGGMLVVFGYTTAMATEEYPETWGSNWFIFSFFVLGLFMELVVFYLFSLNNKVELVDFDSLGDWLMYEIDDVGVMLEGGIGVAAIYSCATWMMVVAGWSLFAGIFIIIEITRD | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18923
Sequence Length: 172
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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O99827 | MLFSEIKFLIFMSVICLSSSHPILMLSSLILLTLFLSLIFYFIYQFSIMSMMMILIILGGMLIIFMYMISLCPNKKMSFYKKLSVTFTMMLILIPYDSFMTKLEMININKIYSVNFVNMIILMMIFLIVMLTIISKNLSWINAPIQKFN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17489
Sequence Length: 149
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q9ZZM2 | MTYIVSLFLLGLVLGLVAVASNPAPYFAALGLVVAAGVGCGVLVGYGGSFLSLVLFLIYLGGMLVVFAYSAALAAEPFPESWGDRSVLGYVVVYTVGVMLVAGWFWSGWYETSWVVVDEFKEFSVLRGDTSGVALMYSYGGGMLIVCAWVLLLTLFVVLELTRGLSRGALRAV | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18388
Sequence Length: 173
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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O63849 | MNSLFMIFSLGIVGASLMVISTPNPVYSVFWLVIAFVNAAVMFISLGLDYIGLIFIIVYVGAIAILFLFVIMLIQQPNKIDSQDHSHFLPIGLSVIFLFYSLLTNSPKYISNPVIGSRTNIGAIGSHLYTTYYELVLIASLVLLVAMIGAILLAKQPNSPFLYNSHGESLRSRQDLFLQISREHL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20516
Sequence Length: 185
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P15553 | MVVYVTLIVMLFGSTLVFYSLSPYYSALGLVVFSVPGSFVLSFLGSSFVPIVLFLVYIGGMLVVFPYSSAISPERFPSVNNLGEVVGLVFLFSSWVFMSFDNFQDLKNIFHCFVSGESLVGSNTFYNSGGVLVILGVFVLLVALVGALIISRGIESTIIRAIWLW | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18040
Sequence Length: 165
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q9YDF6 | MSQEASVDGRFGVASSPTIEEAAGLLEKLLDGSSMVVVAGVCSSEYEGRGASVSTEGDKLLIVKPGGAVILHGPRGFRPLNWQPSTSHTEVATADGLLTLKFYRRTPREVLKIACGSIWYIAWVRFPEEGAFWMYMTEDDLRKAVALHPRELLGEDIRFFAEEKRTPSGKADLYGVDERGNIVIVEVKRVRADESAVRQLEGYVRDYPTQAKVRGILVAPDISDAARRLLESRGLEFRRVDLKKAYSLLKPGRGRSVLDFL | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 28928
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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A1A3C3 | MRIIVADCSAEYSERLNASLPLAKRVLLIKADNSLLIFSELGSYKPLNWMSAPCSIRDITPDHADDDVDTEVPQKVIRASADKSNDVLEVTLQRIYSDESYDLGEDPGLIKDGVEDHLQKYLAEQIERIGKGAKLVRREYPTAIGPVDIMAIDGNGEHVAIEIKRNGGIDGVEQLTRYCDLLNRDPLLAPVHGIFAAQTITPQARVLAQDRGFKCLLLDYEEMKGTEDDSLRLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 26055
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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B3DTU8 | MRVIVADCSAEYSGRLNASLPLAKRVLLIKADSSLLIFSELGSYKPLNWMTAPCTIREIDPAAKSAQHSRESVAGGAVDGDSATHSPESVAAGEPEKVLRVSADKGSDILEVTLQHIYSDQTYDLGEDPGLIKDGVEDHLQRYLAEQIERIGKGAKLVRREYPTAIGPVDIMAVNAEGEHVAVEIKRHGGIDGVEQLTRYCELLNRDPLLAPVHGIFAAQTITPQAQVLAKDRGFTCLILDYDDMKGTEDDSLRLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 27867
Sequence Length: 256
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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C4LJL1 | MRLVIATCSVDYVGRLTAHLPKATRLLMVKADGSVSVHADDRAYKPLNWMTPPCTLTVHPIAIDDPDTDFTDGSSVGNSEEQGTDGSAHTAHEEELWVVENKKGEQLRITVHDKISDTTYDLGEDPGLTKDGVEAHLQELLAQHPEALGEGFTLVRREYPTPIGPVDILTRDASGKTVAVEVKRRGGIDGVEQLTRYVELLNRDEILAPVQGLFAAQEIKPQARTLAEDRGFTCVTVDYDELRGTPSQELRLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 27841
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q2J6P5 | MRLVIARCSVDYVGRLTAHLPSAVRLVLVKADGSVSIHADGRAYKPLNWMSPPCVIAEADGVWRVTNRAAEQLVITLEQVLHDSTHDLGVDPGLRKDGVEAHLQVLLADRPDAIAPGLTLVRREYETGIGPVDLLCRDADGSTVAVEIKRRGEIDGVEQLTRYLVRLEADPALPHPVRGILAAQSITPQARLLAADRGLGCAVVDYDELRGLEPSIPTLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 23841
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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P00644 | MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSSANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
Catalytic Activity: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
Sequence Mass (Da): 25471
Sequence Length: 231
Subcellular Location: Secreted
EC: 3.1.31.1
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P43270 | MKKITTGLIIVVAAIIVLSIQFMTESGPFKSAGLSNANEQTYKVIRVIDGDTIIVDKDGKQQNLRMIGVDTPETVKPNTPVQPYGKEASDFTKRHLTNQKVRLEYDKQEKDRYGRTLAYVWLGKEMFNEKLAKEGLARAKFYRPNYKYQERIEQAQKQAQKLKKNIWSN | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5'-position of the phosphodiester bond.
Catalytic Activity: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
Sequence Mass (Da): 19472
Sequence Length: 169
Subcellular Location: Secreted
EC: 3.1.31.1
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Q6NPD7 | MSDQEAPLRNGVEHKIFEVLPFVDDDYGGVIVEMKTPMDTKNFVAALRDSFEQWRLQGKKGVWLNLPLSHVNLVEPAVKEGFRYHHAEPTYLMLVYWIPEAESTIPLNASHRVRVGAVVLNHNKEEKYGSLCGSGIWKIPTGVVDEGEEIFAAAIREVKEETGIDTEFLEILAFCQTHESFFAKSDLFFVCLLRPTSFDIQKQDLEIEAAQWMRFEDSASQPITHKNDLFKDIHHICSMKMEKSYSGFSKKPITTFFDDKLGYLYLNKQEDMEQPIS | Function: May mediate the hydrolysis of some nucleoside diphosphate derivatives. In vitro, uses both ADP-ribose and NADH as substrates; however the relevance of such substrates in vivo is unclear.
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Mass (Da): 31816
Sequence Length: 277
EC: 3.6.1.-
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Q8NFP7 | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDPKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 18500
Sequence Length: 164
Subcellular Location: Cytoplasm
EC: 3.6.1.52
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Q8LET2 | MSSTTTDSTELQNLIKLFQNCQTHPRQHFPAKSSAVLVCLYQEQREDKNELRVILTKRSTTLSSHPGEVALPGGKRDQEDKDDIATALREAREEIGLDPSLVTIISVLEPFVNKKGMSVAPVIGFLHDKKAFKQLPNPAEVEEIFDVPLEMFLKDRNRRAEEREHEGERYLLQYFDYYSEDKERSFIIWALTAGILIRVASIVYQRLPEFQERKPSFWNQPN | Function: Coenzyme A diphosphatase which mediates the cleavage of CoA into 3',5'-ADP from CoA and 4'-phosphopantetheine. Can use malonyl-CoA, hexanoyl-CoA, lauroyl-CoA, myristoyl-CoA and palmitoyl-CoA as substrates, but not isobutyryl-CoA or propionyl-CoA.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25679
Sequence Length: 222
Subcellular Location: Peroxisome membrane
EC: 3.6.1.-
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Q96G61 | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 18559
Sequence Length: 164
Subcellular Location: Cytoplasm
EC: 3.6.1.52
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Q93ZY7 | MSVLSSRTGRDRQRYDNNFRLVSGCIPYRLMKADETEEDSGVDFVNKLEVLMVSSPNRHDLVFPKGGWEDDETVLEAASREAIEEAGVKGILRELPLGVWEFRSKSSTVEDECLGGCKGYMFALKVTEELEDWPERKNRERRWLTVKEALELCRYEWMQRALEEFLRVMEDERRLRTEEETVHDSSKLEEESQIDPWYCFVVN | Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
Sequence Mass (Da): 23869
Sequence Length: 203
Subcellular Location: Mitochondrion
EC: 3.6.1.-
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Q9BQG2 | MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPEIVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKRLCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDARWFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA . The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay . Preferentially acts on NAD-capped transcripts in response to nutrient stress . Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP . May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle . Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity).
Catalytic Activity: a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-nicotinamide D-ribonucleotide + 2 H(+)
Sequence Mass (Da): 52076
Sequence Length: 462
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q52K88 | MSNLSARTGRDHQRYDNNFRLVSGCIPYRLVKDEEEDSTSVDFENKLQVLMISSPNRHDLVFPKGGWEDDETVLEAASREAMEEAGVKGILREDPLGVWEFRSKSSSVEADCCLGGGCKGYMFALEVKEELAIWPEQDDRERRWLNVKEALELCRYEWMQSALEEFLRVMAEEGSTKEDSLAISSISNRGERQIDPRYCFVV | Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use diadenosine 5',5'''-P(1)P(6) hexaphosphate (Ap(6)A), diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A) and adenosine tetraphosphate (p(4)A) as substrates, but not diadenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A), diadenosine 5',5'''-P(1)P(3) triphosphate (Ap(3)A), deoxyribonucleoside triphosphates, ribonucleoside triphosphates, diphosphoinositol pentakisphosphate (PP-InsP(5)) and 5-phospho-alpha-D-ribosyl diphosphate (PRPP).
Sequence Mass (Da): 23187
Sequence Length: 202
Subcellular Location: Mitochondrion
EC: 3.6.1.-
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Q86X67 | MSLYCGIACRRKFFWCYRLLSTYVTKTRYLFELKEDDDACKKAQQTGAFYLFHSLAPLLQTSAHQYLAPRHSLLELERLLGKFGQDAQRIEDSVLIGCSEQQEAWFALDLGLDSSFSISASLHKPEMETELKGSFIELRKALFQLNARDASLLSTAQALLRWHDAHQFCSRSGQPTKKNVAGSKRVCPSNNIIYYPQMAPVAITLVSDGTRCLLARQSSFPKGMYSALAGFCDIGESVEETIRREVAEEVGLEVESLQYYASQHWPFPSGSLMIACHATVKPGQTEIQVNLRELETAAWFSHDEVATALKRKGPYTQQQNGTFPFWLPPKLAISHQLIKEWVEKQTCSSLPA | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP. Has a marked preference for the reduced pyridine nucleotides. Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'-end of some RNAs.
Catalytic Activity: H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-ribonucleotide
Sequence Mass (Da): 39688
Sequence Length: 352
Subcellular Location: Mitochondrion
EC: 3.6.1.22
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Q8JZU0 | MSLYCRTFFRRKSFGCYRLLSTYVTKARYLFELKEDEEACRKAQKTGVFYLFHDLDPLLQASGHRYLVPRLSRAELEGLLGKFGQDSQRIEDSVLVGCSEQQEAWFALDLGLKSASSSRASLPKSEMEAELGGSFIKLRQALFQLNSVDSSLLFTAQALLRWHDGHQFCSKSGQPTQKNVAGSKRVCPSSKIIYYPQMAPVVITLVSDGARCLLARQSSFPKGLYSALAGFCDIGESVEETVHREVAEEVGLEVENIQYSASQHWPFPNSSLMIACHATVKPGHTEIQVNLKELEAAAWFSLDEVTTALRRKGSLALQPSEASPLLLPPKLAIAHHLIKKWVETRSCSSLAA | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP . Has a marked preference for the reduced pyridine nucleotides . Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'-end of some RNAs .
Catalytic Activity: H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-ribonucleotide
Sequence Mass (Da): 39137
Sequence Length: 352
Subcellular Location: Mitochondrion
EC: 3.6.1.22
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Q9CA40 | MSTGEAIPRVAVVVFILNGNSILLGRRRSSIGNSTFALPGGHLEFGESFEECAAREVMEETGLKIEKMKLLTVTNNVFKEAPTPSHYVSVSIRAVLVDPSQEPKNMEPEKCEGWDWYDWENLPKPLFWPLEKLFGSGFNPFTHGGGD | Cofactor: Magnesium may be the real cofactor in vivo.
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Its substrate specificity is unclear. In vitro, it can use NTP, dNTP, 8-oxo-GTP, 8-oxo-dGTP, dGTP, dATP, dTTP or dihydroneopterin triphosphate (DHNTP) as substrate. Has some NADH pyrophosphatase activity in vitro; however, such activity may not be relevant in vivo due to the high concentration of manganese used during the experiments. Plays an important role in protection against oxidative DNA and RNA damage by removing oxidatively damaged form of guanine.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 16357
Sequence Length: 147
Subcellular Location: Cytoplasm
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M4I1C6 | MGNETVVVAETAGSIKVAVVVCLLRGQNVLLGRRRSSLGDSTFSLPSGHLEFGESFEECAARELKEETDLDIGKIELLTVTNNLFLDEAKPSQYVAVFMRAVLADPRQEPQNIEPEFCDGWGWYEWDNLPKPLFWPLDNVVQDGFNPFPT | Function: Involved in a cytosolic pathway for the biosynthesis of free monoterpene alcohols that contribute to fragrance. Lacks terpene synthase activity, but has a diphosphohydrolase activity with geranyl diphosphate and farnesyl diphosphate as substrates. No activity with 8-oxo-dGTP and dGTP and unable to dephosphorylate geranyl phosphate to geraniol.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (2E)-geranyl phosphate + H(+) + phosphate
Sequence Mass (Da): 16790
Sequence Length: 150
Subcellular Location: Cytoplasm
EC: 3.6.1.68
|
Q94B74 | MSASSSSTNPMSREDATTLLPSVQDKYGGVMTEMTHPMDPSLFSTLLRSSLSTWTLQGKKGVWIKLPKQLIGLAETAVKEGFWFHHAEKDYLMLVYWIPKEDDTLPANASHRVGIGAFVINHNKEVLVVQEKTGRFQGQGIWKFPTGVVNEGEDIHDGSVREVKEETGVDTEFDQILAFRQTHKAFFGKSDLFFVCMLKPLSLEINAQESEIEAAQWMPWEEYINQPFVQNYELLRYMTDICSAKTNGDYEGFTPLRVSAPDQQGNLYYNTRDLHSRN | Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear. Confers tolerance to oxidative stress .
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Mass (Da): 31611
Sequence Length: 278
EC: 3.6.1.-
|
A2VE79 | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPGTAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVSIGRKREWFKIEDAINVLQCHKPVQASYFETLRQGYSANNGTPLVAPTYSVSAQSSMPGIR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). InsP6 (inositol hexakisphosphate) is not a substrate (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (By similarity). The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A (By similarity). Also able to hydrolyze 5- phosphoribose 1-diphosphate (By similarity). Acts as a decapping enzyme that can hydrolyze both monomethylated and unmethylated capped RNAs (By similarity). Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA (By similarity). Modulates the stability of a subset of mRNAs implicated in cell motility (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity (By similarity). Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions, diadenosine hexaphosphate hydrolase activity in the presence of manganese ions and endopolyphosphatase activity in the presence of zinc ions (By similarity). Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity (By similarity).
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 19362
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 3.6.1.52
|
O95989 | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEDAIKVLQYHKPVQASYFETLRQGYSANNGTPVVATTYSVSAQSSMSGIR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction . InsP6 (inositol hexakisphosphate) is not a substrate . Acts as a negative regulator of the ERK1/2 pathway (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates . The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A . Also able to hydrolyze 5-phosphoribose 1-diphosphate . Acts as a decapping enzyme that modulates the stability of a subset of mRNAs implicated in cell motility . Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA . Can hydrolyze unmethylated capped RNAs (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity . Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions, diadenosine hexaphosphate hydrolase activity in the presence of manganese ions and endopolyphosphatase activity in the presence of zinc ions . Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity .
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 19471
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 3.6.1.52
|
Q566C7 | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEEAVKVLQYHKPVQASYFEALRQGYSANNGTPVLPTTYSSSMSGIR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction . InsP6 (inositol hexakisphosphate) is not a substrate (By similarity). Acts as a negative regulator of the ERK1/2 pathway (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (By similarity). The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A (By similarity). Also able to hydrolyze 5- phosphoribose 1-diphosphate (By similarity). Acts as a decapping enzyme that can hydrolyze both monomethylated and unmethylated capped RNAs (By similarity). Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA (By similarity). Modulates the stability of a subset of mRNAs implicated in cell motility (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity (By similarity). Exhibits endopolyphosphatase activity in the presence of zinc ions . Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions and diadenosine hexaphosphate hydrolase activity in the presence of manganese ions (By similarity). Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity (By similarity).
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 19096
Sequence Length: 168
Subcellular Location: Cytoplasm
EC: 3.6.1.52
|
Q9LE73 | MTGFSVSLFVSNLSNVASYLSPIFENIPSTKVVPAQIEKVVSLVSRTGRDLQRYDHAGYRQVVGCVPYRYKKQEVNGVETQVIQVLLVSAQKGKGMLFPKGGWETDESMEEAALRETIEEAGVTGELEEKLGKWQYKSKRHSIIHDGYMFALLVSQEFERWPEAEMRQRRWVSLDEAREVCQNWWMREALEAFINLKCLADDDESGN | Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear.
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Mass (Da): 23701
Sequence Length: 207
EC: 3.6.1.-
|
Q9NZJ9 | MMKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFENQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPANGNSTVPSLPDNNALFVTAAQTSGLPSSVR | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction . Can also catalyze the hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) but not diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the major reaction products are ADP and p4a from Ap6A . Also able to hydrolyze 5-phosphoribose 1-diphosphate . Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity).
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 20306
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 3.6.1.52
|
Q8R2U6 | MKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFENQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPTNGNSSVPSLPDNNALFVTAAPPSGVPSSIR | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). Can also catalyze the hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) but not diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the major reaction products are ADP and p4a from Ap6A (By similarity). Also able to hydrolyze 5-phosphoribose 1-diphosphate (By similarity). Does not play a role in U8 snoRNA decapping activity . Binds U8 snoRNA .
Catalytic Activity: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Sequence Mass (Da): 20156
Sequence Length: 179
Subcellular Location: Cytoplasm
EC: 3.6.1.52
|
Q6N1Y8 | MGDLTLPINSGAALAIHVALSAGIVAAIIVVAAWLREKRSGARPDVPYEGGVLPAQPQQGPLNAPYFLIAALFVIFDMEAAILFAWAVAARDAGWLGLIEAAVFIGVLLLALVYLWLDGALDWVKGKRR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13690
Sequence Length: 129
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
Q92ID5 | MLQNSELLQEYLPIAIFFGIAVLVSGLIMILPNLLSTKKYNKDKLEPYECGFEPFSDARSKFDICFYLVAILFIIFDLEIAFLVPWAISLNTIGKIGFFSMMFFLFVLIIGFIYEWKKGALDW | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14242
Sequence Length: 123
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
A7NL04 | MLADYAFIGVFFIGAVIFPLVPLVAAYFLGPKRPTPIKLDTYECGLEAVGDIRVQFKIQYYLYALAFVIFDIEVVFLYPWAVAYGQIGLFALIAMAIFLVILVGGLVYEWKKGALEWV | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13267
Sequence Length: 118
Subcellular Location: Cell membrane
EC: 7.1.1.-
|
O67334 | MVAINSNGFVTTTVEELLRWGRRNSLWPVTIGLACCAIEMMHTAASRFDLDRLGVIFRASPRQADVLIVAGTVVNKVAPMLKLIWDQMPDPKWCISMGGCASAGGPFPTYSTLQGVDRIIPVDVYIPGCPPTPQGLIYGILQLQRKIKEQGITKYDKLFADFNREIEKEGIFVPRELKV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19880
Sequence Length: 179
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
A7GV50 | MAINFEELHPQEQAELERNIFFTTLEQIKGWARSNSLWPMTFGLACCAIEMMGVGSSHYDLDRFGSFFRTSPRQSDVMIVSGTVTKKMAPIVRRLYDQMPEPKWVIAMGSCATAGGPYVNSYAVVKGVDQIVPVDVYIPGCPPNPAALIYGINKLKEKIRYEAKTGKQVTNK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19198
Sequence Length: 172
Subcellular Location: Cell membrane
EC: 7.1.1.-
|
A0QU35 | MGLEERLPGGILLSTVETVAGYVRKGSLWPATFGLACCAIEMMSTAGPRFDIARFGMERFSATPRQADLMIVAGRVSQKMAPVLRQIYDQMVEPKWVLAMGVCASSGGMFNNYAVVQGVDHVVPVDIYLPGCPPRPEMLLHAILKLHDKIQQMPLGVNREEAIREAEQAALAVPPTIELKGLLR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20103
Sequence Length: 184
Subcellular Location: Cell membrane
EC: 7.1.1.-
|
Q1D8S3 | MADADLANIVTTRRDESMGWLQSIVSKGLGWARKYSLFTYPYATACCGMEYMSVAASRHDISRFGAEFPRFSPRQADLLMVVGTINLKQAPILKRVYEQMAEPKWVVAFGVCASSGGFYDNYAVLQGIDRIIPVDVYIPGCPPRPEQVLDGLMLLQDKIGNQVHRIAEREEANPTAARHNLLLSMNK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20871
Sequence Length: 187
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
Q9PGJ4 | MGVIQAIDRLMTNPIPDGQVDDILRPQGESPLLQKGYVTTSVDALLNWARTGSMWPMTFGLACCAVEMMHAGAARLDLDRYGIVFRPSPRQSDVMIVAGTLVNKMAPALRKVYDQMPDPKWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGILQLQKKIWRTQTNAG | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20196
Sequence Length: 184
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
O68854 | MSEALNELASYLREARGALIADAEVKYGELTVTAKAENLIALLTFLRDDVQCGFVSFIDVCGVDYPQRPDRFDVVYHLLSPRQNQRVRVKVATGENDPVPSATSVFPGADWFEREAYDMYGILFTGHPDLRRILTDYGFEGYPLRKDFPLTGFVEVRYDNEAKRVVYEPVELKQEFRNFDFLSPWEGTEYVLPGDEKARPR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23074
Sequence Length: 201
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
P56896 | MTGERPVHLTAIIGSFGGAVENLGAAHGIYAFAVPPEQIVEFCRFLKEHPALEFDFLSDICGVDHYPETPRFETVYHLYSLKNKWRVRIKCRLGEPPHVPTVTGVWRTANWHEREAWDMYGIRFEGHPDLRRIYMWEGFEGFPQRKDFPLRGYKDKLNPFGAEGPPPTQPDLATNDIPQGGR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20893
Sequence Length: 182
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
Q5ZRU0 | MTKNEYLIEKLQADLANHITELTSAYGEVTIECEVQNLLPVMIELRDREEFSFDQLIDLCGVDYLHYGDYDWETESATEHGFSRGVERQEAKAYAVNKPRFAVVYHLLSTKKNHRLRVKLFVEESHLIVPSVHHLWKSANWFEREAYDLYGILFDGHPDLRRLLTDYGFIGHPFRKDFPLSGEVEMRYDAKLQKVIYAPVDIVPRIVVPKVIRNDNRYIGNEGSKND | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26533
Sequence Length: 227
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
B1ZA44 | MEAITTNGITLRRTVAAAQGDDALRAMGERITGALGPAVTDWSIAHGELTLIVQGSDIVYALTYLRDDPNCAFRCFIDICGVDYPQRARRFDVVYHLLSLRHNMRVRVKVQTDAATPVPSAIPVFPAANWFERETYDLYGILFSGHPDLRRLLTDYGFEGHPLRKDFPLTGFVEVRYDQDEARVVYEPVKLTQEFRNFDFLSPWEGTDYVLPGDEKKSS | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24837
Sequence Length: 219
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
Q2RJU5 | MDNFIQELQRLFPDLEVREGVDVPALVVPADQLLALMTELKEKRGFNFLADLTAVDYPEDERIEMVYHLLSVPGMAEIRVKVNLDRQHPEVPSLTALWPAANVQEREAFDLMGVKFPGHPDLKRILCPDDFVGHPLRKDFRLQTEGGE | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16890
Sequence Length: 148
Subcellular Location: Cell membrane
EC: 7.1.1.-
|
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