ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q37704 | MIKWLCLFFSYILMVSSHSWLGLWLSMEMNSLSFIPIMIEESKENSLKYFLIQSVASVIFLASILNQSFSFLIPFALLIKIGAAPFHMWLVSISKSMSWKVLSLLMTFQKIGPLLGLAMLQFTNSFFIFISAFIGGLGGINQSNLRLIMAFSSVSHLSWLMVNMSSFFLMLVYYVTYLAILYFAVILLQQSGMYSLAQMNSNASLIYKASISFNLLSLAGLPPFLGFFIKWMSLEMNILSPLLVLALVVSSCFSVYFYFSIAMSSLLFPSEVKSKKMEIPGILSMGFNIFLPLFFL | 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): 33448
Sequence Length: 296
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P15688 | MLSLTIKGKARRRKERAFGDRDFLTFSSKTKKTENVNLSFEKGTRFFDRGGMIFGPSPRSARWPIGIAAFGLCLLFLIKNSGSARESAGNNRKEGVHVAAASAPFLVNRAAGSATTTKERIHFKITNASAMAACGMAGSDLFGYIIQVESGVTGTAGLMENNFHGSVQRALFSLRILRSLRVNSLARIQNFWGPSIPSSSPAKTPLPFGLNIFFDSYMWAPDIYEGSPTPVTAFFSIAPERSISANILRVFIYGSYGATLQQIFFFCSIALRLRSTGAMANEGKASSSIGQLDYGGLYFVLVLMWNREGIQSLLIGLFIYASMDDRCFAIVSALRQTRVKYIADLGALAKTNPISAITFSITMFSYAGIPPLAGFCSKFYLFFAALGCGAYFLAPVGVVTSVIGCWAAGRLPRVSQFGDRRQFSVHRTRSLPNQLRHGWECMLRKIGSSLIHQPSVYSISLYESTITTRDEPWFGEFELALGVIGLPVTAHDRILRCSPPVVGTTRAGPGLNSER | 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): 56275
Sequence Length: 515
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P19044 | MFLLHEYDIFWTFLIIASLIPILVFWISGLLAPVSEGPEKLSSYESGIEPMGGAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFIEAFIFVLILVVGLVYAWRKGALEWS | 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): 13860
Sequence Length: 120
Subcellular Location: Plastid
EC: 7.1.1.-
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B2J6S7 | MFVLSGYEYLLGFFIICSLVPALALSASKLLRPSGYAPERRTTYESGMEPIGGAWIQFNIRYYMFALVFVVFDVETVFLYPWAVAFHRLGLLAFIEALVFIAILVVALVYAWRKGALEWS | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13644
Sequence Length: 120
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
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P48913 | MLNYFVYPYGIENDIGIKFYMILVPIISIVLIIINYIITNKSDNNINKTGPYECGFDSFRQSRTTYSIKFILIAILFLPFDLELTSILPYTLSIYNLNIYGLFILLYFLLPLIIGFIIEINLKAIYITKIFNRNVKSITSYVKYNNKI | 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): 17312
Sequence Length: 148
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q9B6C7 | MNTFIIFIILIPIVGFALLAVNILLAVYKPYNEKLGAFECGLTSFNQTRLAFNAAFILVAILFLPFDLEISTLLPYVMSIYLVSNYGFTIVLLFLLILIIGFVYEINTNALKINKHNKPNTDSLIYKL | 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): 14470
Sequence Length: 128
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q00244 | MQLQYFLLIAAALFCIGVYGLVTSRNAVRVLMSIELMLNAVNLNLMAFSNYLDPQEIKGQMFTIFVITIAAAEAAVGLAIVLAIYRNRDTVDMEQFNLLKW | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11336
Sequence Length: 101
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
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P48914 | MTYLILLGASICLFPFWEVTMLTLAFIIPMSLTYLNINFTFSFSSELIWLTPIGTALIFLTLMVTLLVLIGTYNIKNYKYIGCLSSLNLVLMMAFCVCDFLTFYVMFEVSLIPTLLLILLWGYQPERMQAGFYLMLYTVTASLPLLLLLLYLYYTVGSLNFYIIMVYYSFNNNPLMLVGLMMAFLVKLPIYTCHLWLPKAHVEAPLGGSMVLAGVLLKLGGYGLYMLINFIISKSSSLVISVIITLSLWGAVIASIICIQQVDIKALVAYSSVAHMSLVSAGILMMSNWSYTCAKMTMIAHGYTSSALFVLANLSYLKIKSRSLMFMKGLLAIFPAMAFYWFLFSCMNMAAPPTLNFIGELLIIPSMYIASYMLLILMCIIMFISAGYSLYMYMTVNHGELGLYITPSIQLKNVDYHVLTAHLLPTFILLIPQLFSV | 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): 49160
Sequence Length: 437
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P51898 | SLVGGVLISLVCLRQTDLKALIAYSSVAHMGIVLSGLLTMTYWGLTGSYALMIAHGLCSSGLFCLANISYERMGSRSLLINKGLLNFMPTLSLWWFLLCSGNMAAPPTLNLLGEISLLNSIVSWSWITMIMLSFLSFFSAAYSLYLFAYSQHGKIYSGVYFFSVGTTREFLLLMLHWLPLNLLILKSNFCMLWIYLNSLKKMLICGVNDMKLFILDRELFS | 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): 24798
Sequence Length: 221
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P34852 | MLKFIFMLMFMFPLSFLKNFYWTVQNLIFLLTFMFMINLSSLNYFNYISYYFGLDMVSYGLILLSFWICGLMLMASEKVFSTNNYEKLFVFMILFLLFMLVLTFSSMSVFMFYLFFEASLIPTLFLILGWGYQPERLQAGVYLLFYTLLASLPLLIGIFYILNSKNTLSFTLLLNYSFSNFNLLYLSLVFAFLVKMPMFLVHLWLPKAHVEAPVSGSMILAGILLKLGGYGLLRMFSLLQISGVKYNYWWISISLVGGVLISLVCLRQTDLKALIAYSSVAHMGIVLSGLLTMTYWGLTGSYALMIAHGLCSSGLFCLANISYERMGSRSLLINKGLLNFMPTLSLWWFLLCSGNMAAPPTLNLLGEISLLNSIVSWSWITMIMLSFLSFFSAAYSLYLFAYSQHGKIYSGVYFFSVGTTREFLLLMLHWLPLNLLILKSNFCMLWI | 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): 51280
Sequence Length: 447
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P34853 | MYLLLLLIMLNMLMMSMIYLFMLFMNKMKNNLNLIIGNLIIINLLLNLFNLNWIDWIYIFCNLSFNMYSYGLIMLTLWIFGLIFISLNNNSLNCLFMNLLLMISLLLVFLSMNLLLFYLFYEFGLLLIFYLVVKWGYSENRWLSGFYLMFYTMIFSLPMLYIIYYIYLIDYSLNFMLMEMLNLNLNMMLFIYLLMSFLVKIPIYLFHGWLLKAHVEAPYYGSMILASIMLKLGGYGMLRLMIIYKNEFILIQKILVMINSFGVLILSLMCLSQFDMKSIIAISSIVHMGLMIMSMMTFLKISLIGGYLMMISHGLSSSGLFFLVNVIYSQTNSRLMFINKGMINFMPSMSLLWFMLCSSNMGSPVSLNLISEVMLLIGMISWLKFMMLILMMYCLFSFIYSIYLFMFINHGKIFIMFKIKNGILVEYFVLLLHWIPLNLMFLKLYFI | 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): 52896
Sequence Length: 447
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P93313 | MLEHFCECYFNLSGLILCPVLGSIILLFIPNSRIRLIRLIGLCASLITFLYSLVLWIQFDSSTAKFQFVESLRWLPYENINFYLGIDGISLFFVILTTFLIPICILVGWSGMRSYGKEYIIAFLICEFLMIAVFCMLDLLLFYVFFESVLIPMFIIIGVWGSRQRKIKAAYQFFLYTLLGSLFMLLAILLILFQTGTTDLQILLTTEFSERRQIFLWIAFFASFAVKVPMVPVHIWLPEAHVEAPTAGSVILAGILLKFGTYGFLRFSIPMFPEATLCFTPFIYTLSAIAIIYTSLTTLRQIDLKKIIAYSSVAHMNLVTIGMFSLNIQGIGGSILLMLSHGLVSSALFLCVGVLYDRHKTRLVRYYGGLVSTMPNFSTIFFFFTLANMSLPGTSSFIGEFLILVGAFQRNSLVATLAALGMILGAAYSLWLYNRVVSGNLKPDFLHKFSDLNGREVFIFIPFLVGVVWMGVYPKVFLDCMHTSVSNLVQHGKFH | 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): 55942
Sequence Length: 495
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P19046 | LFVLLWLTFTTQSFILFYVFFECSLIPTIILILGWGYQPERLPASYYFLFYTLLSSLPLLFIIMLTRVFIR | 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): 8524
Sequence Length: 71
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q37711 | MLMYKLMSEFHLEWGITLLTLNFSYFLFNSYQIKANWPLSYSTILVSLFVLLWLTFTTQSFILFYVFFECSLIPTIILILGWGYQPERLPASYYFLFYTLLSSLPLLFIIIAHTSIYSSSFLQFWGNFMDKMIFLLAILSFLVKLPVYFAHIWLPKAHVEAPVTGSMVLAAILLKLGGYGLYLVQVLNIYSETTLMGVCLMGGIFSCLICLRQSDVKSLIAYSSVAHMSFVILGMLMSCTYTNMSSILMMVSHGICSSGLFYLSYLFYARIWSRSFLLTRSMISLFPYLCFWWLSLSFLNMGLPPSLNFFSEMYFFIGAFSLDWMVVGLSGILCFLSSCYCIYLYSSTSHGESLYIFKLISMQLKGMYNRKSSSDSVTDFNFRLLL | 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): 44425
Sequence Length: 386
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P85928 | SGSIIHSMEANVGYSPDKSQNMVLMGGLK | 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): 3051
Sequence Length: 29
Subcellular Location: Plastid
EC: 7.1.1.-
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Q6L3E3 | MEHTYQYAWVIPLLPLPVIMLMGFGLFLIPTATKNLRRIWAFPSILLLSIAMVFSLHLSIQQINGSSIYQYLWSWTINNDFSLEFGYLVDPLTSIMLILITTVGILVLIYSDDYMSHDEGYLRFFVYISFFNTSMLGLVTSSNLIQIYFFWELVGMCSYLLIGFWFTRPIAASACQKAFVTNRVGDFGLLLGILGFFWITGSLEFRDLFKIANNWIPNNGINSLLTTLCAFLLFLGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLLARLLPLFISLPLLMSFISLVGTITLFLGATLALAQRDIKRSLAYSTMSQLGYMMLALGIGSYQAALFHLITHAYSKALLFLGSGSVIHSMEPLVGYSPDKSQNMVLMGGLRKYVPITRTTFLCGTLSLCGIPPLACFWSKDEILSNSWLYSPFFGIIASFTAGLTAFYMFRIYLLTFDGYLRVHFQNYSSTKEGSLYSISLWGKSISKGVNRDFVLSTMKSGVSFFSQNIPKIPANTRNKIGSFSTPFGAKKTFVYPHETGNTMLFPLLILLLFTLFIGSIGIPFDNGVKDNRILELTILSKWLTPSINLFQENSNSSINSYEFLTNAISSVSLAIFGLFIAYIFYGSAYSFFQNLNFQNSLVKKNPKKSFLDEVKKKIYSWSYNRGYIDFFYTRVFILGIRRLAELTHFFDKGVIDGIINGVGLAGFCIGEEIKYVGGGRISSYLFFFLCYVSLFLFFIP | 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): 82930
Sequence Length: 738
Subcellular Location: Plastid
EC: 7.1.1.-
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Q32516 | MEQTYEYAWIIPFIPLPVPMLIGAGLILFPTATKRFRRMWAFQSVLLLSIVMIFSIYLSIQQINSSSVYQYVWSWIINNDFSLDFGYLIDPLTSIMSILITTVGIMVLIYSDNYMAHDQGYLRFFAYMSFFSTSMLGLVTSSNLIQIYIFWELVGLCSYLLIGFWFTRPVAANACQKAFVTNRVGDFGLLLGILGFYWITGSFEFRDLFEIFNNLIYNNELNFLFVTLCAVLLFAGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFRVIPYIMYLISVIGIITVLLGATLALAQKDIKRGLAYSTMSQLGYMMLALGMGSYRSALFHLITHAYSKALLFLGSGSIIHSMETIVGYSPAKSQNMGLMGGLRKHVPITKITFLLGTLSLCGIPPLACFWSKDEILNDSWLYSPIFAIIAWATAGLTAFYMFRIYLLTFEGHLNAHFQNYGGKQKIPFYSISLWGKNGVKKNSCLLTMNNNESTYFLSKTKYPIAKNGRKMTRPFMTIAHFKHKAVSSYPYESDNTMLFPIFVLGLFTLFVGAIGIPFNQEGVNLDILSKWLAPSINLLHPKSNNSLDWNEFLKDAVVSVSIAYFGIFIASFLYKPIYSSLKNLEFINSFVKKGPKRILWDKILNGIYDWSYNRAYIDAFYTRFFVGGIRGLAEFTHFVDRRVIDGMTNGVGVISFIVGEGIKYIGGGRISSYLFLYLAYVSVFLLVYYLLF | 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): 83283
Sequence Length: 737
Subcellular Location: Plastid
EC: 7.1.1.-
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P48922 | MMSLTFMAGLIFPVFMMLKGINPMSLLLALLTLSLCAVLWLGSFMSSWYAYILFIVYIGGILVLFIYVCMISSNYIASQHMYKSLLYAWGAVMLMSLTMETDTFIILGSNMMYTSVNIPMTILIFLSIYLLIVFFAVVNLMVNMTSILMVESSQV | 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): 17496
Sequence Length: 155
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q08084 | MMSLSFMLGLIFPVFFMFTLANPMSLLLLLLIMSLCAVLWLGSIMSSWFAYILFIVYIGGILVLFIYVCMISSNYITGLYKYKTLLYVGMVVALMS | 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): 10896
Sequence Length: 96
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q06059 | MTYFVFFLGICFVVGVLGVASNPSPYYGVVGLVLASVAGCGWLLSLGVSFVALVLFMVYFGGMLVVFVYSVALAAEPFPEA | 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): 8511
Sequence Length: 81
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q33635 | MTKLIIMTLCLIMSFIFMQMKHPLSMGLMLLIQTFLTCLITSIYVKTFWFSYVLFLIFLGGMLILFIYVTSLSSNEMFSMSFSLTLISLIIFSIFTIVFFMIDKSLIEQFITNMEMEKLSNMNNLINENILSLNKMYNFPTNLITLLLINYLFLTLLVTVKITKKFYGPLRPMN | 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): 20357
Sequence Length: 174
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P34857 | MMLTIIMLSKIFMSSLISMILTIYLNNIFNSPSMLLIYLISYSIYMSLMMFTMCSMNSLLILMILIVFLSGMLIMFSYFISLINEPLKLKMKPFIQTLFLIIITMKIYNKLSQNEHYFNYFKNIDLMYLYMKMNSTLFFIMILMLIITLILMTKITYIEKKTLRKKK | 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): 19971
Sequence Length: 167
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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P60497 | MILSVLSSLALVSGLMVVRAKNPVHSVLFFILVFCDTSGLLLLLGLDFFAMIFLVVYIGAIAVLFLFVVMMFHIQIAEIHEEVLRYLPVSGIIGLIFWWEMFFILDNESIPLLPTQRNTTSLRYTVYAGKVRSWTNLETLGNLLYTYYFVWFLVSSLILLVAMIGAIVLTMHRTTKVKRQDVFRRNAIDFRRTIMRRTTDPLTIY | 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): 23669
Sequence Length: 205
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q37712 | MLGSIVVISMFMLLMNHPLAFTLSLFVQTLLICVMLKNVSLWISLILFLIFLGGILVMFIYVSSLSANEKFAVDLTSFMWVVPTIVLSFLVLNKNFMFMSPSSGYLYPTDFVIINFNVNSLTMLAYSFMVVYLFLALLLVIDFLNSNKKPLRSMI | 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): 17624
Sequence Length: 155
Subcellular Location: Mitochondrion membrane
EC: 7.1.1.2
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Q7QGS3 | MLDKVKHIILVLSGKGGVGKSTVSTQLALTLAEADHKVGLLDIDLCGPSVPYLLGLEDRDVHQCDEGWVPVYTSAEKRLAVMSIGFLLKNRSDAVIWRGPKKTAMIKQFLEDVNWDELDYLIIDTPPGTSDEHITVMECLKTVRTEGAIIVTTPQEMALEDVRKEVTFCKKTGIPILGIVENMSGFVCPNCSECTNIFSSGGGHSLAELAKVPHLGTLPIDPRVGELAGTGKACVKELPDCTTSEVLRELVRTLTTVGQ | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of Nubp1 and two labile, bridging clusters between subunits of the Nubp1-Nubp2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The Nubp1-Nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Sequence Mass (Da): 28057
Sequence Length: 259
Subcellular Location: Cytoplasm
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Q5ZKV4 | MEEVVAERSNLGGVRHILLVLSGKGGVGKSTISTELALSLRHSGKKVGILDVDLCGPSIPRMFKVQDNDVHQCDAGWVPVFVDQEKSISLMSIGFLLEKPDDAVVWRGPKKNALIKQFVADVAWGELDFLIVDTPPGTSDEHISTVEALRPYKPLGAILVTTPQAVSVGDVRRELTFCKKTGLRVLGIVENMSGFVCPHCSECTNIFSKGGGEELAKHAGVPFLGSVPLDPQLSQSLEEGRDFIQEFPKSSAFPALTRIAQQILDGALQRSS | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Sequence Mass (Da): 29359
Sequence Length: 272
Subcellular Location: Cytoplasm
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Q76NZ7 | MDKIKHKILVLSGKGGVGKSTVSSQLALYLSHIGYKVGLLDVDLCGPSIPKMMGLESKDVHKSTKGWVPVYTDESQKLGVISIQFLLGDKDTPVIWRGPKKNSMIKQFIDDVNWGEIDFLIIDTPPGTSDEHISVTEELLKHNPDGAILVTTPQAVSISDVKKEISFCNAMKLPIIGIIENMSGYVCPHCSECTNIFSSEGGKLLAEQCNIKFLGKLPIDPNLSICSERGINYFTEYPNSSTLASLKSFVDNFNFKSSTTTTATN | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nubp1 and two labile, bridging clusters between subunits of the nubp1-nubp2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nubp1-nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Sequence Mass (Da): 28962
Sequence Length: 265
Subcellular Location: Cytoplasm
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Q9VPD2 | MLDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDESQTLAVMSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEVGCHGAIIVTTPQEVALDDVRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDSTTAEVLTHIVEKLKTMLVS | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of Nubp1 and two labile, bridging clusters between subunits of the Nubp1-Nubp2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The Nubp1-Nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Sequence Mass (Da): 28250
Sequence Length: 260
Subcellular Location: Cytoplasm
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B4KY56 | MLDKVKNVIVVLSGKGGVGKSTVSTQLALALRATGHKVGLLDIDLCGPSVPHLLGLEGRDIYQCDDGWVPIYTDESKTLAVMSIGFLLKNRNDPVIWRGPKKTMMIKQFLTDVKWEDLDYLIIDTPPGTSDEHITVMECMREVPCNGAIIVTTPQGVALDDVRKELTFCKKTGIKVLGIVENMSGFVCPHCSDCTNIFSSFGGAELAQLAQVPLLGTLPIDPRVGVLAGSTASVLNELADSSTAQVLRSIVQHLDGLTALPTSA | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of Nubp1 and two labile, bridging clusters between subunits of the Nubp1-Nubp2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The Nubp1-Nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Sequence Mass (Da): 28272
Sequence Length: 264
Subcellular Location: Cytoplasm
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Q9Y5Y2 | MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPACLP | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure.
Sequence Mass (Da): 28825
Sequence Length: 271
Subcellular Location: Nucleus
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Q9R061 | MEAAAGERAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDQEQSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALRPYRPLGALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVVHRMSALCS | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure .
Sequence Mass (Da): 29518
Sequence Length: 275
Subcellular Location: Nucleus
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A4WD46 | MSLKIEIIKDKILSDNYFVLRNITYDLTRKNGEVIRHKREVYDRGNGATILLYNREKQSVVLIRQFRVATWVNGNPDGRLIETCAGLLDNDAPEVCIRKEAIEETGFAVGEVKKLFELYMSPGGVTELVYFFIAEYTDAQRANAGGGVEDEDIDVLEIPFEQALEMIKTGEIQDGKALILLQYLQISGLMA | Function: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP-mannose as its preferred substrate, yielding GMP and mannose-1-phosphate.
Catalytic Activity: GDP-alpha-D-mannose + H2O = alpha-D-mannose 1-phosphate + GMP + 2 H(+)
Sequence Mass (Da): 21553
Sequence Length: 191
Domain: In the dimer, the N-terminal domains are swapped between the two monomers, such that residues of both chains contribute to the active site.
EC: 3.6.1.-
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Q6D8X4 | MSSPIDIVEKKLLSDHWFILHKYVFDLKRKNGGVVRQIREVYDRGDGATILLYNRAKGTVILTRQFRIPTYVNGNESGMLLEACAGLLDDYSPEECIRNEAIEETGYAVGNVEKLFDAYMSPGGVTERLHFFAAEYDESLRDNSGGGVEDEDIEVLELPFSEAIAMMNDGRIKDGKTIMLLQHAIIRGWFAKG | Function: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP-mannose as its preferred substrate, yielding GMP and mannose-1-phosphate.
Catalytic Activity: GDP-alpha-D-mannose + H2O = alpha-D-mannose 1-phosphate + GMP + 2 H(+)
Sequence Mass (Da): 21713
Sequence Length: 193
Domain: In the dimer, the N-terminal domains are swapped between the two monomers, such that residues of both chains contribute to the active site.
EC: 3.6.1.-
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A9MHR4 | MSQNITLIKDKILSDNYFTLRNITYDLTRRNGKVIRHKREVYDRGNGATILLYNSTKKTVVLVRQFRVATWVNGNEDGMLIETCAGLLDNDEPEVCIRKEAIEETGYDVGEVRKIFELYMSPGGVTELIHFFIAEYRDSERASTGGGVEDEDIEVLELPFSRALEMARSGEIRDGKTVLLLNYLHMSHLMG | Function: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP-mannose as its preferred substrate, yielding GMP and mannose-1-phosphate.
Catalytic Activity: GDP-alpha-D-mannose + H2O = alpha-D-mannose 1-phosphate + GMP + 2 H(+)
Sequence Mass (Da): 21769
Sequence Length: 191
Domain: In the dimer, the N-terminal domains are swapped between the two monomers, such that residues of both chains contribute to the active site.
EC: 3.6.1.-
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A6H1R4 | MQSNQLDYLPIFMQMGLAVGFVVLTIIGSSFLGPKRSSVNKDKNFESGIESIGNARVPFSVKYFLVAILFVLFDVEVIFLYPWAINFQELGMQGMIKMVIFMSLLLVGFFYIIKKKALEWD | 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: Multi-pass membrane protein
Sequence Mass (Da): 13804
Sequence Length: 121
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A9HNA0 | MLAMSDFCTQHPLFSYAVAIVVLLAAMLGLGAVSGTRRVGAARGRSMDLPFESGVLPVGSAHLRIPVQYYLVAMLFVIFDVESVFLFSWAPVAVGAGWRGYGAVVVFVASLAAALAYVWRWGALDWGPVPRRRIDYRRAGDASCAGR | 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): 15854
Sequence Length: 147
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A9B477 | MLTNYAFIGIFALAAITFPLLPLVLSAFLRPNRPTPVKLSTYECGLEAIGDIWVQFKVQYYLYALAFVIFDIETVFLYPWAVAYGQLGLFALFEMVVFLAILTIGLVYAWKKGALEWI | 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): 13397
Sequence Length: 118
Subcellular Location: Cell membrane
EC: 7.1.1.-
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Q67P21 | MSADGVFRDQGGFVTTTVDSFLRWAQSNSIWPLTFGLACCAIEMMNLASGPRYDIARFGSEAFRASPRQADLIFISGRVSNKMAPVIKRVYSQMLEPKWVVAFGACASSGGIFDNYAIMQGVDNLLPVDIYVPGCPPTPEAVIYAVQKLRDRIRKEDPRGGIIVRG | 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): 18213
Sequence Length: 166
Subcellular Location: Cell membrane
EC: 7.1.1.-
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B5YKI3 | MIHVVDTVTEPVEIEQGIKIVPAANTIITTLDKIASWGRCSSLWPLTFGLACCAIEMMATAASHYDLDRFGIIMRATPRQADVMIIAGTVTKKMAPVIVNLYHQMPEPRYVIAMGSCACSGGIFNTYSTVQGVDEILPVDVYIPGCPPRPEALIEGLLKLQEKIKTEPHKKTGCLSGVCLIDKSQRRCSYESCRDNKKD | 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): 21846
Sequence Length: 199
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q2IL09 | MAARMDPGIGGEVTLLHTSQLDNLINLARASSLYYLTFGLACCGIELMQTGGPRADLMRFGAIPRASPRQADFMIVAGTLTYKMAERARLLYDQMPEPKYVISMGSCSNCGGLFQLGYSVCKGVDKVIPVDVYVPGCPPRPEALTEGLLRLQEIVRSEPWSTKRRPAAQAEGA | 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): 18786
Sequence Length: 173
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A1K3P1 | MQTPTLHGDGFLLTRLDTLCDMVRSNSMWYLTFGLACCAVEMMQAAASRYDMDRFGMIPRASPRQADLIIVAGTLTNKMAPAIRKIYDQMAEPRYVISMGSCANGGGYYHYSYSVARGCDRILPVDIYIPGCPPTAEALLYGLIQLQNKLKRPPAVIAR | 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): 17621
Sequence Length: 159
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A3MFR5 | MANHPLTLEKDGFIVTTLDAAMAAAQKNSLWYMTFGLACCAVEMMHAAGARYDMDRFGMIPRASPRQCDLMIVAGTLTNKMAPAMRRVYDQMAEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGLMQLQRKVAERSTHSRPKLFARP | 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): 18469
Sequence Length: 167
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q3JNA0 | MANHPLTLEKDGFIVTTLDAAMAAAQKNSLWYMTFGLARCAVEMMHAAGARYDMDRFGMIPRASPRQCDLMIVAGTLTNKMAPAMRRVYDQMAEPRYVVSMGSCANGGGYYHYGYSVVRGCDRIVPVDVYVPGCPPTAEALVYDLMQLQRKVAERSTHSRPKLFARP | 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): 18550
Sequence Length: 167
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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B9L170 | MGMSAAQSHPNIITTTADWLFSWARRSSLWWLQFGLACCAIEMISSAMPRFDLAERFGMLYRASPRQADLMIVAGTVTKKMAPVVRQLYDQMADPKWVISMGSCANVGGPFDTYAVVQGVDQVIPVDIYVPGCPPVPEALYYGVLELQNRIIRYERLKERYGPEAAEAYREEERQAARSALGPRS | 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): 20729
Sequence Length: 185
Subcellular Location: Cell membrane
EC: 7.1.1.-
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A9AFY9 | MASKIETLKANLEAALGARVVSLTEAIGELTLVVKASDYLDVATTLRDDPKLRFEQLIDLCGVDYQTYGDGAYDGPRFAAVTHLLSVTNNWRLRLRVFAPDDDLPIVPSLVDIWNSANWYEREAFDLYGIVFEGHPDLRRILTDYGFIGHPFRKDFPVSGYVEMRYDPEEKRVVYQPVTIEPREITPRVIREDRYGGLKH | 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): 22879
Sequence Length: 200
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q9A6X2 | MSEALELLGQDIVARAPGVLGHSVAFGELTIVARAASVIDTLTFLRDDAACRFHQLIDLTGVDYPERAARFDVVYHLLSLVKNHRIRLKVSTDEDTPVPSVTPVFPVADWFEREAFDMYGIFFDGHPDLRRILTDYGFHGHPLRKDFPMTGYVEVRYDDELKRVVYEPVKITEFRAFDFLSPWEGAKYALPGDEKAQ | 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): 22435
Sequence Length: 197
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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B1ZUJ2 | MIASKESNSAATPATSAPTLRTTAEIAATAAMGHAPHETFTINLGPQHPAAHGVLRVLMRMDGEWVENAEPVIGYIHRMHEKMGENRTWAKFLPNTSRIDYLSAMHYTHAWVGVVERGLKIEVPERAEYIRVITSELNRIASHQVWWGALLLDLGGFTPILYAFDDREKILDLLEGLCGARLTYCYYRFGGLYNDADDDFLKGTREFVKYMRPRLKMYRDLVTDNVILRQRLTGIGPISADTCRKYGATGPVIRGSGVAYDVRRAEPYSVYPKLQFKIPTYPECDSMARYLVRMDEMEESLNIIEQCLDLIQPGPFMAPKVPRVIRLPAGDYTYAVEAARGRFMVRVVSDGKENPYRARLRTPSFGNLSLFEETSRGMLLPDALAMMGSLDLVIPDIDR | 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): 45035
Sequence Length: 399
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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P56908 | MTEVTELMRPEGEALNTKEVLLNLGPQHPSTHGVLRLVLQLDGEYVERVDPHIGYLHRGTEKLAESFTYTQIFPLTDRLDYLCPPSNNLAFALAVEKLLGIEAPIRAQYIRVMMAELARISGHLLITGALPMDLGAMTALLYAMREREMIMDLLEMITGARMHTSYCRVGGVREDLPDGFLPKIREFCEIFPNRIRDYERLIENNRVFLSRTQGVGVISATDAIDLGLSGPNLRASGVDWDIRRDEPYEIYDRLDFDVITREEGDCYSRWLCRVDEMRESIRLIEQCMEQMPEGPFQVDIPTIAFPVDKERVHCSMEALIQHFDLSAYGFDVPAGEVYSVIEAPKGELGFYIISDGSPKPFRMKVRAPSFVNLQALFGVTNARYLADMIAVLGSLDPVMAEVDK | 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): 45702
Sequence Length: 404
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A7NL07 | MLQTQELQINIGPQHPSTHGVFRMIVTVDGETIIDLKPVFGYLHRNHEQLAEVSTYIQSMPYTDRLDYFNSMANNHALALAVEKLAGISVPQRAEYIRVLMVELTRILNHASAVGFLLNDMGAWQTPLMFGMREREKILDLFEMASGARMMCNYFRFGGVWRDLPPEFIPQLKELMQGLPSFFDEFERLLRENEILLSRTVNVGILPKEVAVSYSVTGPVLRASGIPYDVRRAEPYSVYGDLDFDIPIGSVGDVYDRFLIRIEEMRQSYRILQQVIERLPDTTGGHINPAMANIGKQKALRPPPGDAYARIESPKGELGFYLVSDGSERPYRYKVRAPSFINLTPLGDMCRGHKVADVVVILGSIDIVMGEVDR | 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): 42313
Sequence Length: 374
Subcellular Location: Cell membrane
EC: 7.1.1.-
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A9G9T3 | MSQVIFSVDRGGAEPGAEMDDEMTLNMGPHHPSTHGVLRFVISTDGEIIRKAVPDVGYLHRSIEKIGERCTYSGFMPYTDRVDYIAAMFANEAWASACEKLMGIEVPKRAQYLRVISCELNRIGSHMIALGAMAMDVGAVTPFPWALREREYINDFIEELCGARLTFNYHRIGGVSFDMPKGWADKVKHWLDRFEPIMVEFDRLISLNDIFIKRLANVAVVTAEEAKDWGLVGPNLRGSGVKWDLRKEDAYSVYPELEFDVPVGRGRYGTVGDCWDRFYVRVEECRESAKILRQALDKIDEHPEDDILGKLPKKMRPDGEAYARIESARGDMGCYVIGRGAEEAYRARFRTGSFTAMAMIEAKSPGLFLADLVALIASFDVVAPEIDR | 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): 43669
Sequence Length: 388
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q67KN9 | MNVERTQELLVNMGPQHPSTHGVLRLMIKLDGEQVTWCEPDIGYLHRCFEKLAEQKTYPQVIPFTDRTDYLAAMLNELCYVEAVEKLFGDAIQVPERAQYIRVMLAELQRITSHLLALGSMAMDLGATTPFLYCWRDREKLYSLFERITGGRMLYNYLRIGGVRNDLPEGILGTPQDGEDKADKTIWGFINYFDSYVYPEWKALVTGNRIFQYRTKNIGVLTAEQAIAYSCSGAVLRGSGVKWDLRKNLPYAIYDRFEFDIPVGQNGDSFDRWWVRQEEMYQSSRIVKQCLEWLAENPGPVMAPKMPRVLKPPKGEVYHRIEGARGEVACYVVSDGSTNPYKVKWRSPAFTHLQLMPLLCPGHKIADIIAILGSIDVVLGEVDR | 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): 43902
Sequence Length: 384
Subcellular Location: Cell membrane
EC: 7.1.1.-
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B5YL34 | MGETEIEKVSDTTFVLQMGPHHPATHGVLKLLCEFEGERVINIKPDVGYLHRGVEKLSESKTYPGAMTLTDRLDYISSMTNNIGYCLAVERLMGIEPPPRAKFIRTMVSEMTRLSSHLLWLATHALDIGAMTVFLYAFREREQILQFFEKICGARLTVSYPRIGGVRVDIKEHVLDEIYKFMDLMLIRVDEYETLLTENRIWIARTRGVGVIAPEDAVLLGLTGPALRGSGVYYDIRKQIPYDAYSEIDFEVPLGEKGDTYDRYLCRIREMRQSVLIVKQCIEKMPEGKILSDKSPDIDLPHQAKRKIEPGDSLWNGFIAFSEEKQEIMPKGEIYSAIEAPKGELGFYIVSDGSGRPYRMRVRAPSFIHISAIPKLCEGHLLADVIAIIGTLDIVMGEADR | 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): 45377
Sequence Length: 401
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q9EV66 | MELIVALGVIVFKVALVIAILLLLPLPLTWLERKIAGHMQQRMGPMRVGWHGLLQPVADGIKLLTKEDHIPAEADRFLFKLAPILALAPPFVVFAAIPFGESVSVLGNEITLYISNLNVALLFVFAVIGLEVYGVIFGGWAANSKYAVLGSLRTCAQMISYEIPMGFAVIGVVMLAQSMSLLDIVRAQTDVWNVVYQPIGFFVFFVAGLAEAQRIPFDLAEAEGDLGAGFHTEYSGIRFALFMVSEYVVMVLVSVLTVILFFGGWNGVLIPLPPLLWFLLKVAFFVYLFMWFRFTFPRYRYDQLMAIGWKVLLPLSLANIIISGVVFS | 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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36387
Sequence Length: 328
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q6N1Z4 | MIGMIITATISVALIMVLLVLAGTFTWVERRLLGFVQERYGPNRVGPFGSLQWVADTVKILTKEDRPPPGADKLLYILAPAVAATPVLAGFGVVAIGDGWALSSVDVGLLFLLGMLGLTAYAAVLGAWASNNRFSLLGGMRAAAQMLAYEVFLGLSLMGVVMIAGSFSMAEIVEAQRGVWFVVLQPLGMALFTIAGIAAAHRLPFDLPESENDLIAGFITEYTGMSFGLFFLGEYLAVLLVSALAVTLFFGGWLGPWLPGPVWFGLKTAVIAVAFVWIRATLPRPRYDQLLSFAWKVALPLSLLNLMLTGIVVVARSAS | 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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34127
Sequence Length: 319
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q01UN2 | METVLNHPLFMPVLVTLVIIAAFPLVAGYIVLVERKVLADFQVRLGPMRCGPHGLLQPIADALKLLLKEDIIPTDSDKAIFWFAPCISTITGLVAFAVIPFARKIYVADVNVGLLVISATSAVGILGIILGGWSSNSHYSLLGALRSAAQLVSYEVALAFALLSGVMVAGTLSMQGIVQSQADRGVWGIFANYGFMVVPFVLYIIAATAETNRAPFDLPEAESELVAGFHTEYSGFRWALYFLAEYANIFVISSVAVTLFWGGWLRPFSSVAWLEKPLNYGVPVILFVGSGLLTFTLIRKVVDPMQQKVLLGVVVLLVLIGAIMAIPMVNDAMIGLFWFLVKVSVIIYTMIWFRGTFPRYRYDQLMNIGWKIAIPVGMASVMVNAVLGMLGKH | 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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42911
Sequence Length: 393
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q67KP0 | MMEWWNSLSPTVQVWLGGVLKASLILVWGLINFYLCLMLERKLSAWMQNRVGPWRVGLWGWIQPVADLIKLWVKEYIRPNNVDKWLYLIAPFIGFVSANLVWLIVPFGDKLIATDFEIGIIFIAAVMGYDVIATFMAGWGSNNKYSMLGAMRGAAQLISYEVTMVMAVIGVVMMAGSLRLSDIVLAQQQRGFLGWFLFPQIIGFIVYLIASLAELNRAPFDLAEAEQELVAGHHTEYSGFRWAMFMLAEYIHLAAWSAIAATLFLGGWSGPTLGQVAAGLGNVLNGFGAFTNPVGTAVLNWGLAISGSTILNWVAGVFWLVLKTYFFVFLAMWIRWTLPRVRIDQLMDLGWKFLLPVSMFNIFLTGTLRYLAVAFDGVPISIGSFTLRLLGWWL | 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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44177
Sequence Length: 394
Subcellular Location: Cell membrane
EC: 7.1.1.-
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Q5YWD4 | MPDLSLFGHDPFWLVVAKSVFLFVYIILIPLVAVLAERKVVARMQMRVGPNRVGPFGSLQSIADGVKMAFKEDLVPAIVDKPIYLLAPVVSVIPAFMAFAVIPLGGEVSVAGNTTALQLTDMPVGVLYILAITSIGVYGIVLAGWASGSTYPLLGGLRSTAQVISYEIAMALCFAAVFLHAGTMATSGIVGAQHPTWFVFLLLPSFLIYCVSMVGETNRAPFDLPEAEGELVGGFHTEYSSLKFAMFMLAEYVNMGTVSALATTLFLGGWSAPWPFNLIPGADAGWWGLLWFTAKVWTFMFVFVWLRGTLPRLRYDQFMRLGWQLLIPVSLLWVMLVATARLLRADGHAWATGAQVVVGVALTAAMIGLFLRAGRRPAAPPEPEPEPSGEAVFLGFPTPPVPADAHRVDNPKGGLLEPLAGFAVTAATMFKKPNTEFYPEQKVPTAPRYHGRHQLNRHPDGLEKCIGCELCAWACPADAIYVEGADNTEDERYSPGERYGRVYQINYLRCIGCGLCIEACPTRALTMTNDYELTDDNRADLIYEKDRLLAPLAPGMVAPPPAMAPGTTEADYYLGAVTGGAPAAEQPAPAGAKGGAR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64393
Sequence Length: 597
Subcellular Location: Cell membrane
EC: 7.1.1.-
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A0QU29 | MTHPDPTLFGHDPWWLMLAKAVAIFVFLLLTVLSAILIERKLLGRMQMRFGPNRVGPAGLLQSLADGIKLALKEGLVPAGVDKPIYLLAPVISVIPAFVAFSVIPLGGAVSVFGHRTPLQLTDLPVAVLFILAATSIGVYGIVLAGWASGSTYPLLGGLRSSAQVVSYEIAMGLSFVAVFLYAGTMSTSGIVAAQDRTWFVFLLLPSFLVYVVSMVGETNRAPFDLPEAEGELVGGFHTEYSSLKFAMFMLAEYVNMTTVSALATTMFLGGWHAPFPFNLIDGANSGWWPLLWFTAKVWTFMFLYFWLRATLPRLRYDQFMALGWKVLIPVSLLWIMVVAITRSLRQHGEGTWAAWLLTAAVVVVVALIWGLATSLRRRTVQPPPPQSTGAYPVPPLPSVGTKETADA | 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 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. This subunit may bind ubiquinone (By similarity).
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44447
Sequence Length: 408
Subcellular Location: Cell membrane
EC: 7.1.1.-
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Q82TV0 | MDSLQPLFEQLFGSEWGGPLFLLIKNLLLILAIVIPLLLAVAYLTFAERKIIAYMQVRVGPNRVTFFDIPWLRGWGQPIADAVKAIMKEIIIPTGANKFLFLLAPVLAIGPALAAWAVVPFSPELVLADINAGLLYILAMTSLGVYGVIIAGWASNSKYAFLGAMRSAAQVVSYELAMGFALVCVLMMSSSLNLGDIVAGQQGGSFLNWYLIPLFPMFLVYFISGVAETNRAPFDVAEGESEIVAGFHVDYSGMAFTVFFLAEYANMILVATLASIMFLGGWLPPVDIAPFNLIPGMVWLLLKIAFMLFFFLWFRATFPRYRYDQIMRLGWKVFIPLTLVWIVVLGMVMQLPEVVRQSFPLNLWFN | 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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40726
Sequence Length: 366
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q01ZR8 | MANPIEEILGTAAAIAKGMGITFKEMMGPTVTDDYPDAPPKFEERFRGVHVLQRDVNGMEKCVACFLCAAACPSNCIYIEAAENTDKIRMSGGERYAKVYNIDYNRCIFCGYCVEACPTDAITHGHGFEAASYNTSTLVKRKEDMLVPVPPGAKPPSMADEVPAGAH | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 18088
Sequence Length: 167
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q9XAR2 | MDHKGTDPGFMNPVAGFGVTFKAMFKKRLTEQYPEQQKTTAPRFHGRHQLNRHPDGLEKCVGCELCAWACPADAIYVEGADNTDEERYSPGERYGRVYQINYARCILCGLCIEACPTRALTMTNEFELADSSRANLIFTKEQLLAGLEEGMVDSPHAIYPGTDEQDYYRGLVTEAAPGTVQQVAHSKGEVVQEGDSTFGATEPASEEVIRR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 23403
Sequence Length: 211
Subcellular Location: Cell membrane
EC: 7.1.1.-
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Q67P14 | MNGVAAIAKGMATTLKVLFRKPVTVDYPYVKRPRAPRFRGRHELRTYENGLEMCVGCELCQVACPAAAITVQAAENDPDNPHSPGERYGYKYQVDLLRCIFCGMCEEACPTDCLHLTQEFELADFTRESLILQKEQLVNRNPSGFKVPMNVYPPFRRKAVNA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 18288
Sequence Length: 162
Subcellular Location: Cell membrane
EC: 7.1.1.-
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A0LEQ3 | MGNLKEILEGGWSLVEGMRVTFRRLLRPVVTVQYPREVVTLSPAFRGHIELKSFADTGTHKCIACGTCERMCPSNVIKVQGTKAQPKGAKVATHYVIDFTRCSLCGICVESCPTGTLQYSTEYELAGESRWDGVIDLMQRFEARRPQSL | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 16615
Sequence Length: 149
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q2IL14 | MPQTVRAYTGAIRDTVKSFWHGLSITLSYLARRPTTVQYPDRTPMPVRDMLPPRYRGFLEVDSGICTGCQACERACPIGCIQISLEKDAANPKQRVVTQFDIDEAKCMFCGLCVEPCPTGSIQHTREFEGTHKHIRNLVFRWADPMNPFPVYKVDKNAEYYPRVPLGSLVRQRLETMAWDRSAPQFLPPEPPKPAEAKPAAKAAPAAKPAAAAPAAPAAAAPAAAPAPAKPAAAPAPAAAAAPAAPAAEAPAAPAAPAANPESK | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 28065
Sequence Length: 264
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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O67386 | MIKKVAAKPLSWLERIFFIDFIKGLRITLKNALRKTITTHYPYEKITPPKRFRGYFAHKVVDGTEPQPAFQEWVNRYNILVEYGKSRCVVCLRCKRACPVPQLFEIEGKKLPNGKRVVSVFNMNMLLCTYCGFCVDACPVDCLYQTDIHENASYTRKDAVLTLEILEQIGRDWQRRREREPDRIWIDDEQRMKLWGENNVKLPKPEEV | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 24572
Sequence Length: 208
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q3J1Q2 | MKGILDSILRVGRMIFAPTKTVQYPEEKLPLAPRTRGRIVLTRDPDGQERCVACNLCAAACPVDCIDVVKAETPDGRWYPESFRINFARCIFCGYCEEACPTSAIQLTPDVELADYRRGFLQYEKEDLLISGEGKHPGYRYWDVAGKAIAGKAQDPVDPKDLCP | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 18316
Sequence Length: 164
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q92YN8 | MSRALDKAGRWIGWAFFADLANGLALTFGYMFSRPVTMQYPDKEKWLPYSRYRGHHFLKRDDEGEIKCVACELCARICPCDCIEVVPYEDEKGNRRPAKFEIDTARCLFCGLCEDACPADAIALGQQYEFSSFSSRDLVIGRDDLLAKPGKAMTGGGVVAARLNTERDVLVEASEPRGYNWWRNIRRK | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 21361
Sequence Length: 188
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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O25858 | MAKQEYKQLPKRAEVHSATEQFKDTVKTSLGLDLFKGLGLTIKEFFSPSVTIHYPMEQLPLSPRYRAVHNLQRLLDSGSERCIGCGLCEKICTSNCIRIITHKGEDNRKKIDSYTINLGRCIYCGLCAEVCPELAIVMGNRFENASTQRSQYGSKSEFLTSEQDAKNCSHAEFLGFGAVSPNYNERMQATPLDYVQEPSKEESQEETPTNPESNKGDENV | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 24715
Sequence Length: 220
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q5ZRU6 | MKKVYHYIIHYVRTYLLLELLAGLWLTVKYFFRKKITVQFPEEQTPLSPRFRGLLALRRYPNGEERCIACKLCEAVCPALAITIESEQRDDGSRRTTRYDIDMFKCINCGLCEESCPVDSIVVTPIHHYHISERGQNIMTKEKLLAVGDLMESQLAADRAADEKYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 19291
Sequence Length: 166
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q72VZ9 | MGTVNVVRVASRHKLSWYEKFYFYSIGKGLWITLKHFIKAAILRKAVTIEFPEKKRKYSTRFRGMHTMKRDEQGRERCTSCFCCMWICPADAIYIEAAEVTPEIQHLHPEDKYAKKFEIDLLRCIFCGMCEEACPKGAIYLDGPGEMATDNREDLILTKERMMQLVGGPIIGERQ | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 20324
Sequence Length: 175
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q5LPS9 | MTQIDYTRAAKYFLLQDFWVGMKLGLKYFFSPKATINYPHEKGPLSPRFRGEHALRRYPNGEERCIACKLCEAICPAQAITIDAEPREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETREELFYDKEKLLSNGDRWEAEIARNLELDAPYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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): 19042
Sequence Length: 164
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q8KEB6 | MLTQQLLSIGVNHFLTISVILFGLGMFAVMTRKNAIVILMGVELILNAANINFLTFSKYNGGMEGVMFSLFVIVLAAAEAAIALAIVINIFKTFKTVDVSSVDTMKE | 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: Multi-pass membrane protein
Sequence Mass (Da): 11590
Sequence Length: 107
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q0KCS0 | MLSLAHFLVLGAILFAISIVGIFLNRKNVIVLLMAIELMLLAVNINFVAFSHYLGDLAGQVFVFFILTVAAAESAIGLAILVVLFRNLDTINVDDMDTLKG | 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): 10951
Sequence Length: 101
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q9RU97 | MPEMVPTSYYLALSGVLFALGLIGVMTRRTAILIFLSVELMLNAANIALVAFARSWGDLMGQTAVFIVMTLAAAEVAIGLAIIVAIFRGRETTNVDDLAQLRG | 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: Multi-pass membrane protein
Sequence Mass (Da): 11002
Sequence Length: 103
Subcellular Location: Cell membrane
EC: 7.1.1.-
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P57262 | MSIIFFIILFPLIGFLFLSTIQDFIFKRYTLNIGIFSIFISFFITCFYGVSILKNNNQVFTQILWKWLSINEFKIDFGFFLDGLSLSMLFVITGVGLLIHIFSSWYMRYKEGQSRFFAYTNLFIASMSVLVLADNFLFMYLGWEGVSVCSYLLIGFYYTELKNNLCAFKAFILTRVSDVFLMIGMFLIYREFNSFNFQEIKFLSSFLNVENFYYLDYITLFLLLGVIGKSAQLPLQTWLSDAMVGPTPVSALIHAATMVTAGVYLIARTHFLFLLTPGILYLVGLIGTLTILVSSISALVQKDIKRILAYSTMSQIGYMFLALGVKAWSAAITHLIMHAIFKALLFLSAGSLIKSCKNEKNIFKMGGLRKQLPFLYISFIVGGASLVSFPLITAGFYSKGNILFSVLKSGCIDFFIIGLFCSFLTAIYTFRMIFVIFHGKNIHTADSSTNLQHNIPLFVLLLLSTVFGSYISPPLSDVFPLSYTPIDHKFAFEIICSILSLSGIYLSYYIWIKNLYVLDKIFQFKFMRYLYYFFLKGWGFNWFYKISFVYFYLYISKRLSADPLNKIINYFLKVTQIFNFYLLKTSNGYVRWYVASMILGINFIFLLMLFFYFN | 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: Multi-pass membrane protein
Sequence Mass (Da): 70882
Sequence Length: 614
Subcellular Location: Cell membrane
EC: 7.1.1.-
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Q89AT6 | MNFVYLVVLCPLVSFCLLLFFIDYLPKMLVKKIGIVSIFISMIITFYSLFDFLNCGKQCVFYIPLWVWISIDYLKIDFNFMLDGLSITMLTMTTSIGFLIHLFSSWYIKLQDEYTRFFSYMNLFIASMVLLLLADNLLVMYIGWEGVGLCSYLLVGFYYSKINSGYAAIKGFIITRIGDIFLILAIFFIYKNFGTLNFRELKLIFETTNVVENFKFLNYVSLFLLIAAIAKSAQVPLQTWLIDAMAGPTPASALIHSSTMVTAGVYLIARMNFLFSLSPIILYILGIISCLTIIMSCLSALVQKNIKCILAYSTMGQVGYMFLALAMKEWTLAINHLVTHAIFKTLLFLSAGAVIILLNNEKNIFNMGGLRKKFPMLYFSFLIGGASLASFPILTSGFYSKGNILFSALENNYYLFLVLGLLGSVLTSIYTFRMIFLVFCGAQKYRAHYVFFSRTLANTLPLLILILLSTVIFVLIHLPLSSVFSKTTPSFLINNNKLLFEIGCSVLSLLGMFISYYLFLVNRMLVDLLLNTKLGNFIYNFWYDSWGFNSLYNILCVNPYLYVAKRLKHDPINIFMSIPITFCFFVSKNLKYIHNGYLRVYVFSIMFGLFLFILMAIRLYK | 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: Multi-pass membrane protein
Sequence Mass (Da): 71078
Sequence Length: 621
Subcellular Location: Cell membrane
EC: 7.1.1.-
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Q9PMA7 | MQNLALISLFSPFVAFLFASCFALSEKKQFVGIICSLLVALSAFCSLYLLFCNEAFNVSLFEWFAGVNFGFDIDAISLTMMSVVGIVATCVHFYSIFYMAHDEGFNKFFAYLGLFVFSMLFLVMSDNFLGLFVGWEGVGLCSWLLIGFWYKNDTYSFAANEAFIMNRIADLGMLLGIFWLYLQAGTLKYDEVFSMAQSLDHNALILIATCLFIGAMGKSAQFPFHTWLADAMAGPTPVSALIHAATMVTAGVYLVIRASTLYDLVPEVSYIIALLGAFVAIFAASMALVVRDLKRIIAYSTLSQLGYMFVAAGLGAYGIALFHLATHAFFKSLLFLGAGNVMHAMNDKLDIKKMGGLFKPLKITAILMCIGSLALAGIYPFAGFFSKDLILGYSFISFHHGIFLVLLIAAFLTAFYSFRLLMLVFFTPARHDEHPHEASKIALLAMSPLMVLAIIAGFFEHSFFEYLSTKLVFIDAQNQIVMICASVAAILGAILAIFAYKNSWFKESIEENKIHKLLSNDYFIPQFYHQFIVSKYESLCAILKHCDLYIFDRIVEKIALYSQNISQKMIMPNSLNLMLRFLVAAFVILLILVWMV | 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 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 (By similarity).
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66528
Sequence Length: 596
Subcellular Location: Cell membrane
EC: 7.1.1.-
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P33607 | MNMLALTIILPLIGFVLLAFSRGRWSENVSAIVGVGSVGLAALVTAFIGVDFFANGEQTYSQPLWTWMSVGDFNIGFNLVLDGLSLTMLSVVTGVGFLIHMYASWYMRGEEGYSRFFAYTNLFIASMVVLVLADNLLLMYLGWEGVGLCSYLLIGFYYTDPKNGAAAMKAFVVTRVGDVFLAFALFILYNELGTLNFREMVELAPAHFADGNNMLMWATLMLLGGAVGKSAQLPLQTWLADAMAGPTPVSALIHAATMVTAGVYLIARTHGLFLMTPEVLHLVGIVGAVTLLLAGFAALVQTDIKRVLAYSTMSQIGYMFLALGVQAWDAAIFHLMTHAFFKALLFLASGSVILACHHEQNIFKMGGLRKSIPLVYLCFLVGGAALSALPLVTAGFFSKDEILAGAMANGHINLMVAGLVGAFMTSLYTFRMIFIVFHGKEQIHAHAVKGVTHSLPLIVLLILSTFVGALIVPPLQGVLPQTTELAHGSMLTLEITSGVVAVVGILLAAWLWLGKRTLVTSIANSAPGRLLGTWWYNAWGFDWLYDKVFVKPFLGIAWLLKRDPLNSMMNIPAVLSRFAGKGLLLSENGYLRWYVASMSIGAVVVLALLMVLR | 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): 66438
Sequence Length: 613
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q9K1B0 | MNDMTLYLIIALVPLAGSLIAGLFGNKIGRAGAHTVTILGVAVSAVLSAYVLWGFIDGSRAKFDENVYTWLTMGGLDFSVGFLVDTMTAMMMVVVTGVSLMVHIYTIGYMHDEKVGYQRFFSYISLFTFSMLMLIMSNNFIQLFFGWEAVGLVSYLLIGFYFKRPSATFANLKAFLINRVGDFGFLLGIGLVLAYFGGSLRYQDVFAYLPNVQNATIQLFPGVEWSLITVTCLLLFVGAMGKSAQFPLHVWLPDSMEGPTPISALIHAATMVTAGLFMVSRMSPIYEMSSTALSVIMVIGAITALFMGFLGVIQNDIKRVVAYSTLSQLGYMTVALGASAYSVAMFHVMTHAFFKALLFLAAGSAIIGMHHDQDMRHMGNLKKYMPVTWLTMLIGNLSLIGTPFFSGFYSKDSIIEAAKYSTLPGSGFAYFAVLASVFVTAFYAFRQYFMVFHGEEKWRSLPEHHSDGHGEEHHGLGKNDNPHESPLVVTLPLILLAVPSVIIGYIAIEPMLYGDFFKDVIFVNADAHPTIHIMKEEFHGALAMVSHSLHSPVLYLAIAGVLSAWLLYVKLPHLPAKIAQTFRPIYVLFENKYYLDALYFNVFAKGTRALGTFFWKVGDTAIIDNGIVNGSAKLVGAIAAQVRKAQTGFIYTYAAAMVFGVLVLLGMTFWGLFR | 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 (By similarity).
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74229
Sequence Length: 674
Subcellular Location: Cell membrane
EC: 7.1.1.-
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P50939 | MTTIILLAPLLGALIGGFGWRLITEKGALVVTTGLLFLSCILSWVVFLTLPAETQHIHLLDWIRSGALDTSWGIRLDRLTAIMLIVVTTVSALVHLYSWGYMAHDENWTHHEAYKARFFAYLSFFTFAMLMLVTSDNLVQMFFGWEGVGVASYLLIGFYYKKPSANAAAIKAFVVNRVGDFGFALGIMGLFFLTDSIDMDVIFASAPELAKTELHFLAWEFNAANLLAVLLFIGAMGKSAQLFLHTWLPDAMEGPTPVSALIHAATMVTAGVFLVCRMSPLFEYAPEAKMMVVYVGAVTAFFAATVGLVQNDIKRVIAYSTCSQLGYMFVAAGSGVYSVAMFHLLTHAFFKAMLFLGAGSVIHAMHHEQDMRNYGGLRKKIPFTFAIMMIGTLAITGVGIPFFSIGGVPVGFAGYLSKDAIIESAFASGNGFAFYVLVAAAGMTSFYSWRLIFLTFYGEARGDHHKHDHAHESPAVMLAPLALLAVGSVLAGMVWYHSFFGDKVASFFNLPAAAHGEAHGTEHATEGHVPEAAMTAEAAHEAAMAGTMAMAEPAAEHAVAKAPQGAIFMAETNHVIHDAHGVPDWVKLSPFGAMVTGFFFAWLYYIGDKPLPGRTARALPGLYRFLLNKWYFDELFDLLFVNPAKSLGRKLWKGGDGAVIDGAINGLALGWIPFFTRVAGRIQSGYLFHYAFAMVLGIVALMFWVVRTGGMN | 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): 77532
Sequence Length: 712
Subcellular Location: Cellular chromatophore membrane
EC: 7.1.1.-
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Q92G97 | MMYQNICIMIIMLPLASSIINGLFLRVIDKKLAQVIATGFLSLSALFSLIIFCDTGLDGNIIHIKLLPWIEVGTFKVNWSIYIDQLTSIMFIAVTWVSSIVHIYSLGYMAEDKGIIRFLSFLSLFTFFMLMLVSSDNFLQLFFGWEGVGVCSYLLIGFWYSKESANKAAIKAFIINRASDFAFILGVITIIVYCGSANYKDVLSSAELLSNIKIFLHFSILDIICLLLFIGCMGKSAQIGLHVWLPDAMEGPTPVSALIHAATMVTAGVFLVARCSYLFEYSPLILQFITIIGGVTCLFAASIAIMHSDIKKIIAYSTCSQLGYMFMACGVSAYNSGIFHLVTHAFFKALLFLSAGSVIHAVHEQDIFKMGDLRNKMPVTYGNFLIGSLALIGIYPLAGFYSKDSILEAAYSSGSFMFIFGIAAAILTAIYSMKIIMLVFHGKTKLEKDVFEHAHEPAKVMNNPLILLVVGSFFSGMIGYYLLAMDKPNGYFHASLFNLHIYKLLISHPPLYIKLLPMAVGIVGIVTGIYLYKSSTVMSFPQKRKSSKNIKNAWILRSSRGMTPLVLISNILRNKYYFDEIYNCLIVKPINCLASLFYLGDQQIIDRFGPNGFSRVVNCFSVLTGKIQTGYVFNYALYIVSFIVVTISYFVWKNIMY | 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: Multi-pass membrane protein
Sequence Mass (Da): 73327
Sequence Length: 657
Subcellular Location: Cell membrane
EC: 7.1.1.-
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A7HY36 | MENAISTVPEFLPALPEILLAVGAMALLMYGVFRKDCDARETSLGALALFALVGAFLIIEPNAYVETFGGMFVIDGFTKFMKLLILLAAAAAIVMSLTFIRREGMDRFEYPVLIILATLGMFMMVSANGLISLYMGLELQSLSLYVIAAFHRDNTRATEAGLKYFVLGALASGMLLYGASLIYGFTGSVQFGSIATVLQADGTNIGVIFGIVFVLAGLAFKISAVPFHMWTPDVYEGAPTPVTAFFAGAPKVAAMALILRVLFVAFPSMESEWQQIIVFIAIASMVLGAFAAIGQSNIKRLMAYSSISHMGFAMVGLAAGTPEGVRGVLIYLVIYVVMNAGVFCCILAMQRKEGYVENISDLAGLSRNQPMVAFMMAMLMFSLAGVPPLAGFFGKFYVFMAAVEAGLYPLAVIGVLASVVGAFYYLRIVKIMYFDEAAEPFIQPMPGELTAVLGISGVFTLFFFVYPAPLILASQAAVRALLP | 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): 51828
Sequence Length: 483
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q6MDQ3 | MNPTLTLTDFISIGPLLIVLMTALIIILIESFSENCSKKWSSLISIGGLTLSIFAVWGGISSNHSSLLNPWIHFDTLARFFTVFFLVIGIGASLLATAFFQRFKASHGEYFFLLQSAVFGLILIGAAADLLTLFLGIETLSISLYVLCGYMKKWEISHESSFKYFLMGSIVAGFLLYGIALVYGAIGTTRLDVLLSSYQTISLTTEKVLFFSGIAMITLGLAFKAALVPFHTWSPDVYAGASNPVTAFMAVGTKVGVFAAFVRLFFEALPQFDAAWNQVIDTLVYATLIYANFVALKQIQLRRFFAYSSISHAGFLMIPVVIGNQEALSALTFYLVIYAIATFGCFAVLAYLDQNQEGVHFSDLHGLFSRSPWLASLLSICLLTLAGIPPTAGFLAKFYVFKVAFQAGYYGLVIVGLLTTILSSYYYLRIIGILFSESKNDEKLPYSMPAAIVGTTSFIAIIILSFYPAPFLKVLSHLSN | 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): 52626
Sequence Length: 480
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A1ALQ2 | MATDLLYGLLPEHILLGLILVLMLLEILSVDKRAGSALFIASLLAGAGVLVMQLQTGYTADIVMNEIRIDRFSEIGRLIIVSCGAILGVYSLSSEAGHKYWILIASSLLGAMIILDSAGFISLFMGIEILSLPGFALMVLNNGKSTASEGSIKYLLLSSVATALVLFGLSLVYGSTGNLNISSFTAAVATGGVQNLAASVMILSGFFLKASVFPFHGWAPDAYSSARLPVTAFLASIVKAAVVLGLVRILGNAVLNPEAVTVIALLSMLSMFYGNITAIHQTAFKKMLAYSSISHAGYMMFALVDNTGARTEALLYYVAVYAVTTITACACFSILSGEDDNLDNLNGIFRKKPVAAILLSLCVLSLAGIPPLPGFLAKFFVFKTVIASGHLTVAVLAFVASYIGTFFYLGVVLRMFRSDAETVEQPANATCLCWTWGGALLGTLALALFMLLPNIFHWVMTGI | 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): 49096
Sequence Length: 463
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q4FM78 | MDNLNFILPEIFISLSIMFLLLLGVYKKNSSNIVHNLAVGSLLITGILIFNNPLDQNISLFNDGYVVDNLSSFMKILTILGGAFVLSISTRYLKIFKIFLIEYPVLILSSILGMMVMISSNDLMVFYIGLELQSLALYVLASFNRDQLKSSESGLKYFVLSALSSGLLLYGCSLVYGFSGSTNFNVIGDLMNSSHYGLTFGIVFILVGLAFKISAVPFHMWAPDVYEGSPTAVTLFFAIVPKVAALTVFIRFLYIPFVNMIDQWQPILIFLSIASMIFGAIAAIGQNNLKRLIAYSSIGHMGYALAGLSTGSNEGIQSSIVYMSIYLVMNLAFFSCLLMLKRNDAYYETIDDLSGLSKNHPILSLSLLAILFSLAGIPPLAGFFAKFYIFKAVIEQSMYFLAIVGLLSTVIAAFYYLKIIKVIYFDKEKESYDTDHNIWLKGSLTFSTLLILLYFIFPSKLLEIVSRINII | 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): 52378
Sequence Length: 471
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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C0QR92 | MSILQQLVSGIGVPNFGVILPEIIILITAFILLVVELLIRSRVVISAITVTGLILAAASVFLIKKGDVTFYGLYVVDMFSLIFKLFLILTTLFVVINLKPYLDSKKSYYGEYYYIILFALIGMMIMVSSPNLVTFYIGLELSAVSIYILAGTFRKDYRSKEGAFKYLIMGGMGTAIISYAIALIYGRTGSFDFYTIASLINSNNIDVGISGALILLIIGLALKAAAVPFHFWTPDAYEGAPTPITAFMAVAAKIATFAVILRVMVEAFPFISKEWSFAWAILAAASMIIGNIIALRQENVKRMLAYSSVAHTGYILAAIAAPTGMGFSALIFYSLIYIFMGIGGFILLSALEKNHNWSNHIDDFKGLAKRSPMMALFMLIFMFSMLGIPPTVGFMGKLGVFLALIGSDIWWLAVTLVVMSIVSAGYYLRVVIYMYMYEPVSKARLNFAMTEMFTVAFMAVFVLILGIYPTVFWGISTTLSSLLIAGIGR | 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): 53710
Sequence Length: 489
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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A1VM73 | MIDKLSWIAVYPELVLLVMACLIALVDLGVKSPRRTLTYALTLLTLGAVAVMEASYALGGQTFYGFGNMVVVDPMGSWLKCFSSIALMITVVYGRPYAADRDMLRGGEFFTLSLFALLGMFVMISGHNFLVLYMGLELMTLCSYALVALRRDDAQATEAAMKYFVLGALASGFLLYGLSMLYGATGSLNINEVFNAIASRQVKHQVLVFGLVFIVAGLAFKLGAVPFHMWLPDVYQGAPTAVTLIIGGAPQLAAFAMTIRLLVEGLLPLAIDWQQMLALMAIGSLVIGNLAAVAQTNLKRMLAFSTISQMGFLLLGLLAGVVNGNQLHTESAYGAAMFYALTYVLTTLAAFGIILLLARAGHESEEITDLSGLNQRSPLYAGVMAMSMFSLAGLPPLVGFYAKLGVLQALISSGQTSYLVLAVFAVFMSLIGAFYYLRVIKVMYFDAPHSHNAQPISAPADAQIVLAINGALLLVLGIAPSSLMTLCAQSINSIVNSLGV | 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): 53393
Sequence Length: 500
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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B1XUL1 | MQAFDLYAILPELVLLIATCLLLVASVYVPERVTPTLGVEQDVFHTPRGVGFVYFFTIIMLVYLVFAFVGRMGDPALVAMNGLFQSDPFSNLLKACSCIAVLISLIYSKQYLMDRDLFRSDFIVLALLALLGQFVLISGANLLTLYLGLELMALPTYALVAMRHNSEKSVEAGIKYFILGALASGFLLYGMSMLYGVTGSLDLIEIFKVVADPRVNHLVMAFGLVFIVAGLAFKLSVVPFHMWVPDVYQGTPTAVTLMIAAAPKLAAFALLFRLLVNTLLPLLGDWQPMLVLLAVLSLVVGNVTAIAQTNVKRMLAYSAIAQMGFVLLGMLSVFDDHAFSASMFYAITYVLTTLGTFGLLMVLSRKGYDCETLDGLKGLNKKHPWFAFISLVMMFSLAGIPPTVGFVAKLGVLEALVDAEHSFIAVIAVIASLIGAFYYLRVIKVMYFDEPEHEVTVSGSGFAKGVLSLNSILVLAIGIVPAGLMSLCLDAMRRTLLGS | 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): 54192
Sequence Length: 499
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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B4EZ47 | MTITPEQLIAMLPLLVVILTVVVVMLSIAWRRDHFTIATLTATGFIIALGSLYYVNALGVVDVTTLYHVDGYSSFFTALTIIAGLGTVAFAYPWLEGYQDNKEEFYMLVAIAVIGGILLSSAHHLASMFIGIELLTLPLFGLIGYAFQQRPSLEASIKYMLLSAAASSFLLFGMALLYAEAGNLSFTAMGQSLSDSNIHKPLVLAGLGMMLVGIGFKLSLFPFQLWTPDVYQGAPAPTGAFLATASKIGIFAVVMRLFLEAPAADSETLRMILGFMAIASILFGNIMALTQKNVKRLLGYSSVSHLGYLLVALIVLQYSPILAQETAEIYLAGYLFASLGAFGAIAVASSPYNKGELESLEDYRGLFWRRPVAAVVMSLMMLSLAGVPITLGFIGKLYVILAGIDSSLWWLTGMVVLGSAIGLFYYLRAAAIVFLRKPDNDNAPAVTTTSQNMATLITLVCAIIVIVLGVWPQPLIELTRFAIIAPAIN | 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): 52650
Sequence Length: 489
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q9I0I9 | MTFTIQHFIALLPLLITSATLVVVMLAVAWKRNHSFTATLSVIGLNLALLSLLPVLGVTPIEVTPLVLVDNYACFYMALVLVSALACVTLAHAYMESYPGNREELYLLLLLATAGGLVLVSAQHLASLFIGLELLSVPVYGMVAYAFFNKRSLEAGIKYTVLSAAGSAFLLFGMALLYAESGTLGFAGLGAKVAEHVLSGPLVSVGVGMMLVGLGFKLSLVPFHLWTPDVYEGAPAPVSAFLATASKVAVFAVLLRLFQIAPAALDNQLLNISLSVIAVASILFGNLLALTQSNIKRLLGYSSIAHLGYLLVALIASKGMAVEAVGVYLATYVLTSLGAFGVITLMSTPYSGRDADALFEYRGLFWRRPVLTAVMTVMMLSLAGIPLTAGFIGKFYVIAVGVESHLWWLIGALVLGSAIGLYYYLRVMVTLFLVEPGIRQHDAPFNWGQRAGGIMLVAIALLAFFLGVYPQPLLEILQHSGLALAG | 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): 51720
Sequence Length: 486
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q4FU52 | MNDFTMNDLMGLLPYAPIIAVVITVLVVMIAITMKRSHMVTGTISVVGLNIGLFILLGQMAGIIDSGSLVPAAEQLFVIDNFAQFNMVIIFICALACCTLSYAYLADLKDHKEELYLLMLLSTVGALLMVCAQHLASFFMSLEMLSIPLYGMLSYTYMRTRSLESGLKYLVLSATASATLLMGMAFIYAEVGSLAFKPISLTLADTFESPLLILGAAMMMFGIAFKLSAAPFHIWTPDVYEGAPAPIATYLASVSKVAMMALAVRFLIDTSLLALPSVQMLLMVMATLSILLGNLLAVRQTSLKRLLGYSSIAHMGYVLIVIVSIGSAADSISSMYMAIYAFTSIGAFGVVTLMSSPYRLSGEADELTHYQGLFWRRPVLTAVMTIMMLSLAGIPLTAGFITKLFAILAAVQGTNWFLAAMIILGSAIGLFYYLRVLLTLFKRPKQFIEFDVSKQWGLRTGGIMVIAVTAIIVFFGVLPNSMIEWASLARIW | 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): 53521
Sequence Length: 492
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
Q2K9R9 | MTAETILLSLHLSAPELILAVGALVLLMVGVFSGERSGLVVTGLAIVLLLASGLWLLFVPAEGLAFGGVYMADGFSRFMKLVALIGSLVALFMTMGHARENQLDKFEFPVLLVLATLGILLMISANDLISLYLALELQSLALYVVAAINRDSLKSTEAGLKYFVLGALSSGMLLYGMSLVYGFTGHTHFTEIAQALSVEGARSLGLIFGLVFILAGIAFKISAVPFHMWTPDVYEGAPTPVTAFFAAAPKVAAMAMLTRIVITAFQPVLADWQQVVVFISIASMLLGSFAAIGQKNIKRLMAYSSIGHMGYALVGLAAGNQTGVSGVMLYMVIYMIMTLGTFAIIMSMRRKDGTVVEDVNDLAGLSATNPFMAVVLTALMFSLAGIPPLAGFFAKYFVFVAAIEAKLYALAIIGVLASVVGAYYYLRVIKLMWFDEATGEFARVSSALRLVFGLSGLFVTAYVLIGGPIGGAAELAAATLF | 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): 50999
Sequence Length: 481
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
A5VAN3 | MSMTASLALTVPELILSVGALLLLLVAAFGGDGFARAIGWGAVALFAAAGFSLTGPAGNGGPGFDGLYIADSFAAFAKLLIYIAAAVSVAVAPGFFSRTGGGYRAEYPVLILLSGVGMGMMVSAGDLLTLYVGLELQSLSAYVLASFMRRDTRSAEAGLKYFVLGALASGILLYGISLLYGFTGTTLFAGISDSLAKGMGTGQMFGMVFVFAGLAFKISAVPFHMWTPDVYEGAPTPVTAFFASAPKVAGMALLLRVAIEAMGSGTDTWRQIVVFAALASTILGAVAAIGQTSMKRLLAYSSINNVGFALFGLAAGSADGVAATMTYMAVYVAMTLGSFICVLQMRGQDGQPVETIASLSGLSRSRPGLAAAFAIFMFSLAGIPPLFGFWPKFLVFDALVRAGFWPLAMVGIATSVIGAFYYLKIVKTIYFDDPAPAEFAPAASKLEGGLITLAALAVSPLGYLAIPLLDATSMAAARSLF | 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): 49576
Sequence Length: 481
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
P50973 | MTKAEFSLVLPEVLLAIYAMGVLLFGVWTGKDRVAKPILWASAVTMLALALIIGLGTGNDTAFGGLFIADGFARFSKVVILVSAAAVLAMSSDYMGRRGLLRFEYPILIVLAVVGMMMMVSAGDLMSLYIGLELQSLALYVVAALRRDSAVSSEAGLKYFVLGSLSSGLLLYGASLVYGFAGTTTFSGIITVVEQGHLPIGLLFGLVFLLAGLAFKVSAVPFHMWTPDVYEGSPTPVTAFFATAPKLAAMALIARVVHDAFGQVPGEWGQILAALALASMYLGAIAGIGQRDIKRLMAYSSISHMGFGLLGLAAGTAAGVESMLLYMTIYIVMNVGTFAFILSMERDGKPVTEIAALNMLSKTDPVKAFALLVLLFSLAGVPPMLGFFAKFAVIKAAIGAGFVWVPVAAVVASVIGAFYYLRIVYFMYFGEKSAPLDGRMPALQFAFLVLAAVAMLGGAINMAGVEGAAQAAAASLVN | 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): 50128
Sequence Length: 478
Subcellular Location: Cellular chromatophore membrane
EC: 7.1.1.-
|
B6ISW8 | MVAIPDFLPALPEMFLACAAMALLMLGVFRGADSTRLVSWLAVGAALVAGVLVLAASGDRAVTFAGMFIADDFAVFAKVLILTATALTVVLSVNYLEREQMDRFEYPVLMLLATVGMMLMVSANDLISLYVGLELQSLSLYVIAAFRRDYAKSSEAGLKYFLLGSLSSCILLYGASLIYGFSGTTNFERLAVMFSSDVPAATGVVVGLVFVAAGLAFKISAVPFHMWTPDVYEGAPTSVTAFFAVAPKVAALALFVRVLVDPFGELLAQWQQVVWFSAVASMLLGSLAAIQQRNIKRMMAYSSIGHIGYALVGLAAGTEEGVRGVLIYLAIYLAMNVGTFAVILSMRVNGRMVENIDDLSGLSRSHPMMALAMAFFMFSLGGVPPMAGFFGKLYVFMAAIEAQLYVLAVIGVLTSVISLFYYLRIVKVMWFDDLMETIERPARASALVIGGTALFVFPVFYVFSEGILNGAAAAASTLFLR | 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): 51636
Sequence Length: 481
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
|
O60356 | MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR | Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses . Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A . Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation . Negatively regulates apoptosis through interaction with PTMA . Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter . Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) . Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 . Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation . Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion . Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity).
PTM: Phosphorylated in vitro by PKA and CK. Phosphorylation promotes DNA-binding activity.
Sequence Mass (Da): 8873
Sequence Length: 82
Subcellular Location: Nucleus
|
Q9WTK0 | MATLPPTANPSQQPLNLEDEDGILDEYDQYSLAHPCVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR | Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses . Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation . Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter . Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 . Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion . Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities . Also required for LHB expression and ovarian maturation . Exacerbates CNS inflammation and demyelination upon cuprizone treatment .
PTM: Phosphorylated. Phosphorylation promotes DNA-binding activity.
Sequence Mass (Da): 8901
Sequence Length: 80
Subcellular Location: Nucleus
|
O54842 | MATLPPTAHTSQQPVNIEDEDGILDEYDQYSLAQSYVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR | Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses . Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (By similarity). Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter . Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway . Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (By similarity). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity).
PTM: Phosphorylated. Phosphorylation promotes DNA-binding activity.
Sequence Mass (Da): 8955
Sequence Length: 80
Subcellular Location: Nucleus
|
Q759K4 | MPKHHTFATKLEDLVLTSMSFRMSKHQAHPIEPEDVIREESEDFYSDEEEYKETWSRWALQLLSSSPYDLYLIVNENFESINWDLKAKTLARPLGGTMTFLFFTVRLLQDNVIKPNYHKINRTTDGFDFSRSATLREYDYFSKYQHGASWSSANWRVNSLSILDTLLKCLYILLLVSNSVLTYKFLFGYFLKYSLFHSAQPPASNNLTKKSLHDLAYRSATDVSRGSLWTLIRYTFFQRGRVQEEKPTDEFYYEIKKWCPSSFLTALFASFPPISVWFMAFSDITFVSLLPVILTQYLFWYVIFDCYEDRIKDELAIFKGMAAEYNNKVMKPKLSAQTQDAMVDATMYGQEFVQFYPSYSTARSGVFITHSLCGDVIKEKYNQRTKAFEDIPTGSHSQNIIRYSRNERLYHSVFPQNPLKKINGAAMSVNPMSFNRSPTYGGRYGTPPSRSHGSGQTYSSTSAPTSPMLKNRRAIPTDHSTGGNISGGNYVEYTSNDVHGEPPRRHSTSPLKRDITSSAGREDNHLAFGVNSPNIRSRTVDVKKNLHTHTTVVCPKSDLDTSQLSSKQSSISPFKLSRRGSIESRPPFR | Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67521
Sequence Length: 589
Subcellular Location: Nucleus membrane
|
Q6FL09 | MFSWLIPDIPELFLTISVWFRLQGWEDNTKLGFIIGNTLTTIFYILRLAQDTLLAGVSRKLIRDYELFDLSKSETLLSDPAFSSYHDVLFNKHHSTANASSYNKRVRKVTSTVYWSTYFLLLLSCYTCYRLFNTYKVYRIYYLKDLNLDKHPSLKKIEPDYEVDEKLLKTSLKSKLLSRFIRLLQLQDEVETELPKVTEHYTLNKWDPSKLIISLSTSFSPTIIICLMYTNVTFLTVIPIIIHQGIFYFMIWNRYEERFKDDALLMRENYLQYDTKYVKPLKQIMYQDVMTDTATISDGGFTKFFPVSKSTLFKHHEMSGDVIIERYNKKSREFENVTDIIKPHHHINNTVKILPPTIRKDHKTNRYDHRQQSILKDRKFNIDSNEPQIINALTTAIPSRSFFNNNPSGSNDDNCSGIKVRSSPTRETFFPATPLRKK | Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51561
Sequence Length: 438
Subcellular Location: Nucleus membrane
|
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