ID A0A3G2Z2K8_9LILI Unreviewed; 159 AA. AC A0A3G2Z2K8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 11-DEC-2019, entry version 9. 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; Magnoliopsida; 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=.1002/ajb2.1178; RA Givnish T.J., Zuluaga A., Spalink D., Soto Gomez M., Lam V.K.Y., RA Saarela J.M., Sass C., Iles W.J.D., de Sousa D.J.L., Leebens-Mack J., RA Chris Pires J., Zomlefer W.B., Gandolfo M.A., Davis J.I., Stevenson D.W., RA dePamphilis C., Specht C.D., Graham S.W., 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 model RT for the origin of monocots."; RL Am. J. Bot. 105:1888-1910(2018). 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 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; 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: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}; 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:AYP33703.1}; 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; 18880 MW; 7AB5EA4C545A4902 CRC64; MQQDRLSDWL VKHELVHRSL GFDCRGIETL QIKTEDWDSI AVISYVYGYN YLRSQCAYDV APGGFLASVY HLTRIQYGID KPEEVCIKVF APRNNPRIPS VFWIWRSADF QERESYDMLG ISYDNHPRLK RILMPESWIG WPLRKDYITP NFYEIQDAH //