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NDHH_MAIZE
ID   NDHH_MAIZE              Reviewed;         393 AA.
AC   P25709;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 121.
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   Zea mays (Maize).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2249254; DOI=10.1007/bf00318388;
RA   Maier R.M., Doery I., Igloi G., Koessel H.;
RT   "The ndhH genes of gramminean plastomes are linked with the junctions
RT   between small single copy and inverted repeat regions.";
RL   Curr. Genet. 18:245-250(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73;
RX   PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA   Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT   "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT   of divergence and fine tuning of genetic information by transcript
RT   editing.";
RL   J. Mol. Biol. 251:614-628(1995).
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; X56521; CAA39868.1; -; Genomic_DNA.
DR   EMBL; X86563; CAA60354.1; -; Genomic_DNA.
DR   PIR; S13600; S13600.
DR   RefSeq; NP_043093.1; NC_001666.2.
DR   AlphaFoldDB; P25709; -.
DR   SMR; P25709; -.
DR   STRING; 4577.GRMZM5G853723_P01; -.
DR   PaxDb; P25709; -.
DR   PRIDE; P25709; -.
DR   GeneID; 845187; -.
DR   KEGG; zma:845187; -.
DR   MaizeGDB; 69245; -.
DR   eggNOG; KOG2870; Eukaryota.
DR   HOGENOM; CLU_015134_1_2_1; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 444312at2759; -.
DR   Proteomes; UP000007305; Chloroplast.
DR   Genevisible; P25709; ZM.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
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   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transport.
FT   CHAIN           1..393
FT                   /note="NAD(P)H-quinone oxidoreductase subunit H,
FT                   chloroplastic"
FT                   /id="PRO_0000118602"
SQ   SEQUENCE   393 AA;  45687 MW;  41666743B3EC5279 CRC64;
     MSLSLKRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRSI
     IQYLPYVTRW DYLATMFTEA ITVNAPEFLE NIQIPKRASY IRVIMLELSR IASHLLWLGP
     FMADLGAQTP FFYIFREREL IYDLFEAVTG MRMMHNYFRI GGVAADLPYG WMDKCLDFCD
     YFLQGVVEYQ ELITQNPIFL ERVEGVGFIS GEEAVNWGLS GPMLRASGIQ WDLRKIDPYE
     SYNQFDWKVQ WQKEGDSLAR YLVRVGEMRE SIKIIQQAVE KIPGGPYENL EARRFKKAKN
     PEWNDFEYRF LGKKPSPNFE LSKQELYVRV EAPKGELGIY LVGDDSLFPW RWKIRPPGFI
     NLQILPQLVK KMKLADIMTI LGSIDIIMGE VDR
 
 
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