NDHH_SOLLC
ID NDHH_SOLLC Reviewed; 393 AA.
AC Q2MI44;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. LA3023;
RX PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA Tomkins J., Jansen R.K.;
RT "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT lycopersicum and comparative analyses with other Solanaceae genomes.";
RL Theor. Appl. Genet. 112:1503-1518(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. IPA-6;
RX PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT solanaceous plastid genomes.";
RL J. Mol. Evol. 63:194-207(2006).
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; DQ347959; ABC56357.1; -; Genomic_DNA.
DR EMBL; AM087200; CAJ32451.1; -; Genomic_DNA.
DR RefSeq; AP_004985.1; AC_000188.1.
DR RefSeq; YP_008563145.1; NC_007898.3.
DR AlphaFoldDB; Q2MI44; -.
DR SMR; Q2MI44; -.
DR STRING; 4081.Solyc01g011410.1.1; -.
DR PaxDb; Q2MI44; -.
DR PRIDE; Q2MI44; -.
DR GeneID; 3950453; -.
DR KEGG; sly:3950453; -.
DR eggNOG; KOG2870; Eukaryota.
DR InParanoid; Q2MI44; -.
DR OrthoDB; 444312at2759; -.
DR Proteomes; UP000004994; Chloroplast.
DR ExpressionAtlas; Q2MI44; baseline.
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 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_0000277416"
SQ SEQUENCE 393 AA; 45605 MW; 87EEB08FF1DBBB88 CRC64;
MTAPTTRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRTI
IQYLPYVTRW DYLATMFTEA ITINGPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP
FMADIGAQTP FFYIFREREL IYDLFEAATG MRMMHNYFRI GGVAADLPYG WIDKCLDFCD
YFLTGVAEYQ KLITRNPIFL ERVEGVGIIG RDEALNWGLS GPMLRASGIE WDLRKVDHYE
SYDEFDWQVQ WQREGDSLAR YLVRIGEMTE SIKIIQQALE GIPGGPYENL EMRRFDRLKD
PEWNDFEYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDQSVFPW RWKIRPPGFI
NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR
