NDHH_PAUCH
ID NDHH_PAUCH Reviewed; 406 AA.
AC B1X4A5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, organellar chromatophore {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=PCC_0333;
OS Paulinella chromatophora.
OG Plastid; Organellar chromatophore.
OC Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC Paulinellidae; Paulinella.
OX NCBI_TaxID=39717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA Nowack E.C.M., Melkonian M., Gloeckner G.;
RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT photosynthesis by eukaryotes.";
RL Curr. Biol. 18:410-418(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 quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
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, organellar chromatophore thylakoid
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-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; CP000815; ACB42774.1; -; Genomic_DNA.
DR RefSeq; YP_002048984.1; NC_011087.1.
DR AlphaFoldDB; B1X4A5; -.
DR SMR; B1X4A5; -.
DR PRIDE; B1X4A5; -.
DR GeneID; 6481295; -.
DR GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
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 Membrane; NAD; NADP; Organellar chromatophore; Plastid; Plastoquinone;
KW Quinone; Thylakoid; Translocase; Transport.
FT CHAIN 1..406
FT /note="NAD(P)H-quinone oxidoreductase subunit H, organellar
FT chromatophore"
FT /id="PRO_0000371959"
SQ SEQUENCE 406 AA; 46300 MW; 6350C68E830E9C4E CRC64;
MTQLETRTEP MIINFGPHHP SMHGVLRLVV TLDGEDVVDC EPVIGYLHRG MEKIAESRTA
ITFVPYVSRW DYAAGMFNEA ITVNATEKLM DLEIPRRASY IRVLMLELNR IANHLLWLGP
FLADVGAQTP FFYIFREREM IYDLWEAVTG QRLINNNYFR VGGVACDLPF GWLDKCEDFC
DWFGPKIDEY EQLITNNPIF RRRIEGLGVI SREQAINWSL SGPMLRASGV PWDLRKVDHY
ECYDDFDWDI AWAKEGDCYA RYLVRIEEMR QSLRILKQAL KMIPGGPTEN LEAQCGFDST
DTNQDLDKKR SVATGEVSGN EYTIGPKKIN LNKCPEGELY CRVESGKGEL GVFIISNGEA
NPWRWKIRAA DFNNLQILPH ILTGAKVADV MAILGSIDVI MGSVDR