ID   A0A4D6Q2N8_9ERIC        Unreviewed;       120 AA.
AC   A0A4D6Q2N8;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   31-JUL-2019, entry version 2.
DE   RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394};
DE   AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE   AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE   AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394};
GN   Name=ndhC {ECO:0000313|EMBL:QCF39501.1};
GN   Synonyms=nuoA {ECO:0000256|HAMAP-Rule:MF_01394};
OS   Vaccinium oldhamii.
OG   Plastid {ECO:0000313|EMBL:QCF39501.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; Ericales; Ericaceae; Vaccinioideae;
OC   Vaccinieae; Vaccinium.
OX   NCBI_TaxID=190543 {ECO:0000313|EMBL:QCF39501.1};
RN   [1] {ECO:0000313|EMBL:QCF39501.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim S.-C., Baek S.-H., Lee J.-W., Hyun H.J.;
RT   "Complete chloroplast genome of Vaccinium oldhamii and phylogenetic
RT   analysis.";
RL   Mitochondrial DNA Part B Resour 4:902-903(2019).
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_01394}.
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_01394};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC       complex. {ECO:0000256|HAMAP-Rule:MF_01394}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01394}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01394}.
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DR   EMBL; MK049537; QCF39501.1; -; Genomic_DNA.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.1610; -; 1.
DR   HAMAP; MF_01394; NDH1_NuoA; 1.
DR   InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; PTHR11058; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Plastid {ECO:0000313|EMBL:QCF39501.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01394}.
FT   TRANSMEM     12     34       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01394}.
FT   TRANSMEM     62     83       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01394}.
FT   TRANSMEM     89    112       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01394}.
SQ   SEQUENCE   120 AA;  13858 MW;  67E01A5BDF93DAF8 CRC64;
     MFLLYEYDIF WTFLLISSLI PVLAFLISGV LAPLSKGPEK LSIYESGIEP VGDAWLQFQI
     RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFIEAFIF VLILIVGSVY AWRKGALEWF
//