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NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (EC 1.6.5.-) (NAD(P)H dehydrogenase, subunit H) (NADH-plastoquinone oxidoreductase 49 kDa subunit) (NADH-plastoquinone oxidoreductase subunit H)

 D3JJE4_TYPLA            Unreviewed;       393 AA.
D3JJE4;
23-MAR-2010, integrated into UniProtKB/TrEMBL.
23-MAR-2010, sequence version 1.
27-SEP-2017, entry version 28.
RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01358};
EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01358};
AltName: Full=NAD(P)H dehydrogenase, subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000256|HAMAP-Rule:MF_01358};
AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
Name=ndhH {ECO:0000256|HAMAP-Rule:MF_01358};
Typha latifolia (Bulrush) (Broadleaf cattail).
Plastid; Chloroplast {ECO:0000313|EMBL:ADA63755.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Typhaceae; Typha.
NCBI_TaxID=4733 {ECO:0000313|EMBL:ADA63755.1};
[1] {ECO:0000313|EMBL:ADA63755.1}
NUCLEOTIDE SEQUENCE.
PubMed=18048330; DOI=10.1073/pnas.0709121104;
Jansen R.K., Cai Z., Raubeson L.A., Daniell H., dePamphilis C.W.,
Leebens-Mack J., Muller K.F., Guisinger-Bellian M., Haberle R.C.,
Hansen A.K., Chumley T.W., Lee S.B., Peery R., McNeal J.R.,
Kuehl J.V., Boore J.L.;
"Analysis of 81 genes from 64 plastid genomes resolves relationships
in angiosperms and identifies genome-scale evolutionary patterns.";
Proc. Natl. Acad. Sci. U.S.A. 104:19369-19374(2007).
[2] {ECO:0000313|EMBL:ADA63755.1}
NUCLEOTIDE SEQUENCE.
PubMed=20091301; DOI=10.1007/s00239-009-9317-3;
Guisinger M.M., Chumley T.W., Kuehl J.V., Boore J.L., Jansen R.K.;
"Implications of the Plastid Genome Sequence of Typha (Typhaceae,
Poales) for Understanding Genome Evolution in Poaceae.";
J. Mol. Evol. 70:149-166(2010).
-!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
FMN and iron-sulfur (Fe-S) centers, to quinones in the
photosynthetic chain and possibly in a chloroplast respiratory
chain. The immediate electron acceptor for the enzyme in this
species is believed to be plastoquinone. Couples the redox
reaction to proton translocation, and thus conserves the redox
energy in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01358}.
-!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01358}.
-!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of
which are encoded in the nucleus. {ECO:0000256|HAMAP-
Rule:MF_01358}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_01358}; Peripheral membrane protein
{ECO:0000256|HAMAP-Rule:MF_01358}; Stromal side
{ECO:0000256|HAMAP-Rule:MF_01358}.
-!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
{ECO:0000256|HAMAP-Rule:MF_01358, ECO:0000256|RuleBase:RU003685}.
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EMBL; GU195652; ADA63755.1; -; Genomic_DNA.
RefSeq; YP_003434031.1; NC_013823.1.
GeneID; 8774563; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
Gene3D; 1.10.645.10; -; 2.
HAMAP; MF_01358; NDH1_NuoD; 1.
InterPro; IPR001135; NADH_Q_OxRdtase_suD.
InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
InterPro; IPR022885; NDH1_su_D/H.
InterPro; IPR029014; NiFe_Hase-like.
Pfam; PF00346; Complex1_49kDa; 1.
SUPFAM; SSF56762; SSF56762; 1.
PROSITE; PS00535; COMPLEX1_49K; 1.
3: Inferred from homology;
Chloroplast {ECO:0000313|EMBL:ADA63755.1};
Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
NAD {ECO:0000256|HAMAP-Rule:MF_01358, ECO:0000256|RuleBase:RU003685};
NADP {ECO:0000256|HAMAP-Rule:MF_01358};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01358,
ECO:0000256|RuleBase:RU003685}; Plastid {ECO:0000313|EMBL:ADA63755.1};
Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01358};
Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_01358};
Transport {ECO:0000256|HAMAP-Rule:MF_01358}.
DOMAIN 124 393 Complex1_49kDa.
{ECO:0000259|Pfam:PF00346}.
SEQUENCE 393 AA; 45552 MW; F4E3655199BCB8C4 CRC64;
MTVPVTRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
IQYLPYVTRW DYLATMFTEA ITVNAPEQLE NVQVPQRASY IRVIMLELSR IASHLLWLGP
FMADIGAQTP FFYIFREREL LYDLFEAATG MRMMHNYFRI GGVAADLPYG WIDKCLDFCD
YSLTGVDEYQ KLITRNPIFL ERVEGVGIIG GEEAVNWGLS GPMLRASGIP WDLRKIDFYE
CYNEFNWEVQ WQKEGDSLAR YLVRIGEMRE SIKIIQQALE GIPGGPYENL EVRRFDRAKN
SEWNDFEYRF ISKKPSPNFE LSKQELYVRV EAPKGELGIY LIGDNSVFPW RWKIRPPGFI
NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR


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