ID   A0A6B9M6U7_9ROSA        Unreviewed;       393 AA.
AC   A0A6B9M6U7;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   08-NOV-2023, entry version 13.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NAD(P)H dehydrogenase, subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
GN   Name=ndhH {ECO:0000256|HAMAP-Rule:MF_01358,
GN   ECO:0000313|EMBL:QHB74265.1};
OS   Ficus hirta.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QHB74265.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Ficeae; Ficus.
OX   NCBI_TaxID=309429 {ECO:0000313|EMBL:QHB74265.1};
RN   [1] {ECO:0000313|EMBL:QHB74265.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Liu Y., Chen W., Li F., Li C., Xie X., Chao Z., Tian E.;
RT   "The complete chloroplast genome sequence of Ficus hirta (Moraceae).";
RL   Mitochondrial DNA Part B Resour 4:4041-4042(2019).
RN   [2] {ECO:0000313|EMBL:QOH91506.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hirta _ GX {ECO:0000313|EMBL:QOH91506.1};
RA   Shi Y.-C.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_01358}.
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|HAMAP-Rule:MF_01358};
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|HAMAP-Rule:MF_01358};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01358}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000256|HAMAP-
CC       Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC       ECO:0000256|RuleBase:RU003685}.
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DR   EMBL; MN364706; QHB74265.1; -; Genomic_DNA.
DR   EMBL; MT934444; QOH91506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6B9M6U7; -.
DR   SMR; A0A6B9M6U7; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:QHB74265.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Plastid {ECO:0000313|EMBL:QHB74265.1};
KW   Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01358};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358}.
FT   DOMAIN          124..393
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   393 AA;  45648 MW;  46766E176571577F CRC64;
     MNIPATRKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
     IQYLPYVTRW DYLATMFTEA ITVNGPELLG NIQVPKRASY IRAIMLELSR IASHLLWLGP
     FMADIGAQTP FFYIFREREL VYDLFEDATG MRMMHNYFRI GGVAADLPHG WIDKCLDFCD
     YFLIGVTEYQ KLITRNPIFL ERVEGVGIIG REEVINWGLS GPMLRASGIQ WDLRKVDRYE
     CYDEFDWEVQ WQNEGDSLAR YLVRIGEMTE SIKIIQQALE GIPGGPYENL EIRYFDRERN
     PEWNDFDYRF ISKKPSPTFE LPKQELYVRV EAPKGELGIF LIGDLSGFPW RWKIRPPGFI
     NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR
//