ID B7A861_THEAQ Unreviewed; 206 AA. AC B7A861; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 29-SEP-2021, entry version 66. DE RecName: Full=NADH-quinone oxidoreductase subunit C {ECO:0000256|HAMAP-Rule:MF_01357}; DE EC=7.1.1.- {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; 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., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., Brettin T.S., RA 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-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be a CC menaquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01357}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01357, CC ECO:0000256|RuleBase:RU003582}; CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits. Subunits NuoB, C, CC D, E, F, and G constitute the peripheral sector of the complex. CC {ECO:0000256|HAMAP-Rule:MF_01357}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01357}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01357}; CC Cytoplasmic side {ECO:0000256|HAMAP-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 EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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; COG0852; Bacteria. 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 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 Membrane {ECO:0000256|HAMAP-Rule:MF_01357}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003456}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003582}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01357}. FT DOMAIN 28..154 FT /note="Complex1_30kDa" FT /evidence="ECO:0000259|Pfam: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 //