ID A0A089N272_9POAL Unreviewed; 159 AA. AC A0A089N272; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 29-MAY-2024, entry version 49. 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=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; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Arundinoideae; Molinieae; Molininae; 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. RN [2] {ECO:0000313|EMBL:ASJ66555.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Teisher97 {ECO:0000313|EMBL:ASJ66555.1}, and Teisher99 RC {ECO:0000313|EMBL:ASJ66638.1}; RX PubMed=28645142; RA Teisher J.K., McKain M.R., Schaal B.A., Kellogg E.A.; RT "Polyphyly of Arundinoideae (Poaceae) and evolution of the twisted RT geniculate lemma awn."; RL Ann. Bot. 0:0-0(2017). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|ARBA:ARBA00003257}. 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 CC ubiquinone. 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 -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00000766}; CC -!- SUBUNIT: NDH-1 is composed of 14 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|ARBA:ARBA00007569, ECO:0000256|HAMAP-Rule:MF_01357, CC 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 EMBL; MF035984; ASJ66555.1; -; Genomic_DNA. DR EMBL; MF035985; ASJ66638.1; -; Genomic_DNA. DR RefSeq; YP_009073183.1; NC_025235.1. DR AlphaFoldDB; A0A089N272; -. DR GeneID; 20523994; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 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 PANTHER; PTHR10884:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL; 1. DR PANTHER; PTHR10884; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3; 1. DR Pfam; PF00329; Complex1_30kDa; 1. DR SUPFAM; SSF143243; Nqo5-like; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01357}; KW Chloroplast {ECO:0000313|EMBL:ASJ66555.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01357}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01357}; KW Plastid {ECO:0000313|EMBL:AIQ79709.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01357}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01357}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01357}. FT DOMAIN 31..149 FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit" FT /evidence="ECO:0000259|Pfam:PF00329" SQ SEQUENCE 159 AA; 18697 MW; 1FBF7521F050D4BE CRC64; MQQGWLSNWL VKHEVVHRSL GFDHRGIETL QIKAGDWDSI AVILYVYGYN YLRSQCAYDV APGGSLASVY HLTRIQYGID NPEEVCIKVF AQKDNPRIPS VFWVWRSADF QERESYDMVG ISYDNHPRLK RILMPESWIG WPLRKDYITP NFYEIQDAH //