ID A0A089N272_9POAL Unreviewed; 159 AA. AC A0A089N272; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 22-JUL-2015, entry version 8. 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=ndhJ {ECO:0000313|EMBL:AIQ79709.1}; GN Synonyms=nuoC {ECO:0000256|HAMAP-Rule:MF_01357}; GN ORFNames=Hama_g24 {ECO:0000313|EMBL:AIQ79709.1}; OS Hakonechloa macra. OG Plastid {ECO:0000313|EMBL:AIQ79709.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Arundinoideae; Molinieae; Hakonechloa. OX NCBI_TaxID=29678 {ECO:0000313|EMBL:AIQ79709.1}; RN [1] {ECO:0000313|EMBL:AIQ79709.1} RP NUCLEOTIDE SEQUENCE. RA Cotton J.L., Duvall M.R.; RT "Resolving deep PACMAD relationships: a Phylogenomic Approach."; RL Submitted (MAY-2014) 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 ubiquinone. 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: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000256|HAMAP-Rule:MF_01357}. CC -!- SUBUNIT: NDH-1 is composed of 14 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 --------------------------------------------------------------------------- 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; KJ920232; AIQ79709.1; -; Genomic_DNA. DR RefSeq; YP_009073183.1; NC_025235.1. DR GeneID; 20523994; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01357; NDH1_NuoC; 1. DR InterPro; IPR010218; NADH_DH_suC. 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 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 Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Plastid {ECO:0000313|EMBL:AIQ79709.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01357}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01357}. SQ SEQUENCE 159 AA; 18697 MW; 1FBF7521F050D4BE CRC64; MQQGWLSNWL VKHEVVHRSL GFDHRGIETL QIKAGDWDSI AVILYVYGYN YLRSQCAYDV APGGSLASVY HLTRIQYGID NPEEVCIKVF AQKDNPRIPS VFWVWRSADF QERESYDMVG ISYDNHPRLK RILMPESWIG WPLRKDYITP NFYEIQDAH //