ID A0A3G2Z2K8_9LILI Unreviewed; 159 AA. AC A0A3G2Z2K8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 08-MAY-2019, entry version 3. 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:AYP33703.1}; GN Synonyms=nuoC {ECO:0000256|HAMAP-Rule:MF_01357}; OS Heliconia meridensis. OG Plastid {ECO:0000313|EMBL:AYP33703.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Zingiberales; Heliconiaceae; OC Heliconia. OX NCBI_TaxID=1932260 {ECO:0000313|EMBL:AYP33703.1}; RN [1] {ECO:0000313|EMBL:AYP33703.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=13772 {ECO:0000313|EMBL:AYP33703.1}; RX PubMed=30368769; DOI=10.1002/ajb2.1178; RA Givnish T.J., Zuluaga A., Spalink D., Soto Gomez M., Lam V.K., RA Saarela J.M., Sass C., Iles W.J., de Sousa D.J., Leebens-Mack J., RA Chris Pires J., Zomlefer W.B., Gandolfo M.A., Davis J.I., RA Stevenson D.W., dePamphilis C., Specht C.D., Graham S.W., RA Barrett C.F., Ane C.; RT "Monocot plastid phylogenomics, timeline, net rates of species RT diversification, the power of multi-gene analyses, and a functional RT model for the origin of monocots."; RL Am. J. Bot. 105:1888-1910(2018). CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via CC FMN and iron-sulfur (Fe-S) centers, to quinones in the CC photosynthetic chain and possibly in a chloroplast respiratory CC chain. The immediate electron acceptor for the enzyme in this CC species is believed to be plastoquinone. Couples the redox CC reaction to proton translocation, and thus conserves the redox CC energy in a proton gradient. {ECO:0000256|SAAS:SAAS01103434}. 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: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol CC + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:62192; Evidence={ECO:0000256|SAAS:SAAS01132539}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol CC + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192; 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, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|HAMAP-Rule:MF_01357}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of CC which are encoded in the nucleus. {ECO:0000256|SAAS:SAAS01103425}. 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}. Plastid, chloroplast thylakoid membrane CC {ECO:0000256|SAAS:SAAS01103439}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS01103439}; Stromal side CC {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; MH603426; AYP33703.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. 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 Chloroplast {ECO:0000256|SAAS:SAAS01103429}; 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:SAAS01082837}; KW Plastid {ECO:0000313|EMBL:AYP33703.1}; KW Plastoquinone {ECO:0000256|SAAS:SAAS01082843}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357}; KW Thylakoid {ECO:0000256|SAAS:SAAS01082847}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01357}. FT DOMAIN 31 149 Complex1_30kDa. {ECO:0000259|Pfam: FT PF00329}. SQ SEQUENCE 159 AA; 18880 MW; 7AB5EA4C545A4902 CRC64; MQQDRLSDWL VKHELVHRSL GFDCRGIETL QIKTEDWDSI AVISYVYGYN YLRSQCAYDV APGGFLASVY HLTRIQYGID KPEEVCIKVF APRNNPRIPS VFWIWRSADF QERESYDMLG ISYDNHPRLK RILMPESWIG WPLRKDYITP NFYEIQDAH //