ID A0A089N272_9POAL Unreviewed; 159 AA. AC A0A089N272; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 26-FEB-2020, entry version 36. 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; 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: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain CC and possibly in a chloroplast respiratory chain. The immediate electron CC acceptor for the enzyme in this species is believed to be CC plastoquinone. Couples the redox reaction to proton translocation, and CC thus conserves the redox energy in a proton gradient. CC {ECO:0000256|SAAS:SAAS01103434}. 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 plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561, CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192; CC Evidence={ECO:0000256|SAAS:SAAS01132539}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561, CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192; CC Evidence={ECO:0000256|SAAS:SAAS01132535}; 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|SAAS:SAAS01103425}. 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}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|SAAS:SAAS01103439}; CC Peripheral membrane protein {ECO:0000256|SAAS:SAAS01103439}; Stromal CC side {ECO:0000256|SAAS:SAAS01103439}. 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 EMBL; MF035984; ASJ66555.1; -; Genomic_DNA. DR EMBL; MF035985; ASJ66638.1; -; Genomic_DNA. DR RefSeq; YP_009073183.1; NC_025235.1. DR GeneID; 20523994; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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 Chloroplast {ECO:0000256|SAAS:SAAS01103429, ECO:0000313|EMBL:ASJ66555.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01357}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003456}; KW NADP {ECO:0000256|SAAS:SAAS01119003}; KW Plastid {ECO:0000313|EMBL:AIQ79709.1}; KW Plastoquinone {ECO:0000256|SAAS:SAAS01119008}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357}; KW Thylakoid {ECO:0000256|SAAS:SAAS01119018}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003456}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01357}. FT DOMAIN 31..149 FT /note="Complex1_30kDa" 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 //