NDHH_TRISU
ID NDHH_TRISU Reviewed; 393 AA.
AC B8R4B1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NAD(P)H dehydrogenase subunit H;
DE AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
GN Name=ndhH {ECO:0000255|HAMAP-Rule:MF_01358};
OS Trifolium subterraneum (Subterranean clover).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=3900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19018585; DOI=10.1007/s00239-008-9180-7;
RA Cai Z., Guisinger M., Kim H.-G., Ruck E., Blazier J.C., McMurtry V.,
RA Kuehl J.V., Boore J., Jansen R.K.;
RT "Extensive reorganization of the plastid genome of Trifolium subterraneum
RT (Fabaceae) is associated with numerous repeated sequences and novel DNA
RT insertions.";
RL J. Mol. Evol. 67:696-704(2008).
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-
CC Rule:MF_01358}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR EMBL; EU849487; ACF20563.1; -; Genomic_DNA.
DR RefSeq; YP_002456482.1; NC_011828.1.
DR AlphaFoldDB; B8R4B1; -.
DR SMR; B8R4B1; -.
DR GeneID; 7256626; -.
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; -; 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; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..393
FT /note="NAD(P)H-quinone oxidoreductase subunit H,
FT chloroplastic"
FT /id="PRO_0000371958"
SQ SEQUENCE 393 AA; 45691 MW; BC3420FB971B450C CRC64;
MNVPARIKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRTI
IQYLPYVTRW DYLATMFTEA ITVNGPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP
FMADIGAQTP FFYIFREREL IYDLFEAATG MRMMHNYFRI GGVAADLPYG WIDKCFDFCN
YFLTRVIEYQ KLITRNPIFL ERVEGVGVVG REEVLTWGLS GPMLRASGIQ WDLRKVDNYE
CYDEFDWEVQ WQKEGDSLAR YLVRIGEMME SIKIIQQALE GIPGGPYENL EIRSFDREKE
PEWNDFEYRF IGKKSSPTFE LPKQELYVRV EAPKGELGIF LIGDHNGFPW RWKIRPPGFI
NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR