ID B7A861_THEAQ Unreviewed; 206 AA. AC B7A861; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 16-JAN-2019, entry version 56. DE RecName: Full=NADH-quinone oxidoreductase subunit C {ECO:0000256|HAMAP-Rule:MF_01357}; DE EC=1.6.5.11 {ECO:0000256|HAMAP-Rule:MF_01357}; DE AltName: Full=NADH dehydrogenase I subunit C {ECO:0000256|HAMAP-Rule:MF_01357}; DE AltName: Full=NDH-1 subunit C {ECO:0000256|HAMAP-Rule:MF_01357}; GN Name=nuoC {ECO:0000256|HAMAP-Rule:MF_01357}; GN ORFNames=TaqDRAFT_4257 {ECO:0000313|EMBL:EED10448.1}; OS Thermus aquaticus Y51MC23. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=498848 {ECO:0000313|EMBL:EED10448.1, ECO:0000313|Proteomes:UP000005403}; RN [1] {ECO:0000313|EMBL:EED10448.1, ECO:0000313|Proteomes:UP000005403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y51MC23 {ECO:0000313|EMBL:EED10448.1, RC ECO:0000313|Proteomes:UP000005403}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., RA Brettin T.S., Mead D.; RT "Sequencing of the draft genome and assembly of Thermus aquaticus RT Y51MC23."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be a menaquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_01357}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC EC=1.6.5.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01357, CC ECO:0000256|RuleBase:RU003582}; CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits. Subunits CC NuoB, C, D, E, F, and G constitute the peripheral sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_01357}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01357}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01357}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_01357}. CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003456}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EED10448.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ABVK02000004; EED10448.1; -; Genomic_DNA. DR RefSeq; WP_003046180.1; NZ_CP010822.1. DR STRING; 498848.TaqDRAFT_4257; -. DR EnsemblBacteria; EED10448; EED10448; TaqDRAFT_4257. DR KEGG; taq:TO73_1578; -. DR eggNOG; ENOG4105CYU; Bacteria. DR eggNOG; COG0852; LUCA. DR KO; K00332; -. DR OrthoDB; 1735902at2; -. DR Proteomes; UP000005403; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.460.80; -; 1. DR HAMAP; MF_01357; NDH1_NuoC; 1. DR InterPro; IPR010218; NADH_DH_suC. DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS. DR Pfam; PF00329; Complex1_30kDa; 1. DR ProDom; PD001581; NADH_UbQ_OxRdtase_30kDa_su; 1. DR SUPFAM; SSF143243; SSF143243; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01357}; KW Complete proteome {ECO:0000313|Proteomes:UP000005403}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01357}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003456}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003582}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01357}. FT DOMAIN 28 154 Complex1_30kDa. {ECO:0000259|Pfam: FT PF00329}. SQ SEQUENCE 206 AA; 23531 MW; 5419879E036F2CED CRC64; MRLSRVLEEA RAKGYPVEDN GLGNLWVVLP REGFKAAMAH YRDLGFNYLA DIVGLDYLTY PDPKPERFAV VYELVSLPGW KDGDGSRFFV RVYVPEKDPR LPTVTDLWGS ANFLEREVYD LFGIVFEGHP DLRKILTPED LEGHPLRKDF PLGETPTLFR EGRYIIPSEF RAAITGKDPG LTFYRGGSRK GYRALWADLM KAKEAK //