NDHH_ARATH
ID NDHH_ARATH Reviewed; 393 AA.
AC P56753;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
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}; OrderedLocusNames=AtCg01110;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [2]
RP INTERACTION WITH CNP60B4, AND FOLDING.
RX PubMed=21483722; DOI=10.1371/journal.pbio.1001040;
RA Peng L., Fukao Y., Myouga F., Motohashi R., Shinozaki K., Shikanai T.;
RT "A chaperonin subunit with unique structures is essential for folding of a
RT specific substrate.";
RL PLoS Biol. 9:E1001040-E1001040(2011).
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 (By similarity). Interacts with the
CC chaperonin CNP60B4 subunit. {ECO:0000255|HAMAP-Rule:MF_01358,
CC ECO:0000269|PubMed:21483722}.
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 -!- MISCELLANEOUS: Folded specifically by a chaperonin Cpn60 complex
CC containing at least 1 Cpn60 beta 4 subunit.
CC {ECO:0000305|PubMed:21483722}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR EMBL; AP000423; BAA84443.1; -; Genomic_DNA.
DR RefSeq; NP_051115.1; NC_000932.1.
DR PDB; 7WFG; EM; 4.33 A; H=1-393.
DR PDB; 7WG5; EM; 3.89 A; H=1-393.
DR PDBsum; 7WFG; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; P56753; -.
DR SMR; P56753; -.
DR BioGRID; 29993; 4.
DR STRING; 3702.ATCG01110.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; P56753; -.
DR PaxDb; P56753; -.
DR PRIDE; P56753; -.
DR ProteomicsDB; 251142; -.
DR EnsemblPlants; ATCG01110.1; ATCG01110.1; ATCG01110.
DR GeneID; 844805; -.
DR Gramene; ATCG01110.1; ATCG01110.1; ATCG01110.
DR KEGG; ath:ArthCp080; -.
DR Araport; ATCG01110; -.
DR TAIR; locus:504954734; ATCG01110.
DR eggNOG; KOG2870; Eukaryota.
DR HOGENOM; CLU_015134_1_2_1; -.
DR InParanoid; P56753; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 444312at2759; -.
DR BioCyc; ARA:ATCG01110-MON; -.
DR PRO; PR:P56753; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56753; baseline and differential.
DR Genevisible; P56753; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; TAS:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone;
KW Quinone; Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..393
FT /note="NAD(P)H-quinone oxidoreductase subunit H,
FT chloroplastic"
FT /id="PRO_0000118598"
SQ SEQUENCE 393 AA; 45503 MW; 9782AD7CC942966B CRC64;
MKRPVTGKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRAI
IQYLPYVTRW DYLATMFTEA ITVNGPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP
FMADIGAQTP FFYIFREREF VYDLFEAATG MRMMHNFFRI GGIAADLPYG WIDKCLDFCD
YFLTEVVEYQ KLITRNPIFL ERVEGVGIIG GEEAINWGLS GPMLRASGIP WDLRKIDRYE
SYDEFEWEIQ WQKQGDSLAR YLVRLSEMTE SIKIIQQALE GLPGGPYENL ESRGFDRKRN
PEWNDFEYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDQSGFPW RWKIRPPGFI
NLQILPELVK RMKLADIMTI LGSIDIIMGE VDR
