ID A0A3G2Z2K8_9LILI Unreviewed; 159 AA. AC A0A3G2Z2K8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 07-OCT-2020, entry version 12. 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: 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:ARBA00002539}. 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; MH603426; AYP33703.1; -; Genomic_DNA. 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:UniProtKB-EC. 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01357}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003456}; KW Plastid {ECO:0000313|EMBL:AYP33703.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003456}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01357, KW 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 //