NDHH_MICAN
ID NDHH_MICAN Reviewed; 394 AA.
AC B0JY10;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H {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 subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
DE Short=NDH-H {ECO:0000255|HAMAP-Rule:MF_01358};
GN Name=ndhH {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=MAE_52260;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC and/or the photosynthetic chain. The immediate electron acceptor for
CC the enzyme in this species is believed to be plastoquinone. Couples the
CC redox reaction to proton translocation, and thus conserves the redox
CC energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC inorganic carbon-concentration. {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-1 can be composed of about 15 different subunits;
CC different subcomplexes with different compositions have been identified
CC which probably have different functions. {ECO:0000255|HAMAP-
CC Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01358}; Cytoplasmic 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; AP009552; BAG05048.1; -; Genomic_DNA.
DR RefSeq; WP_002760089.1; NC_010296.1.
DR AlphaFoldDB; B0JY10; -.
DR SMR; B0JY10; -.
DR STRING; 449447.MAE_52260; -.
DR PaxDb; B0JY10; -.
DR EnsemblBacteria; BAG05048; BAG05048; MAE_52260.
DR GeneID; 66705659; -.
DR KEGG; mar:MAE_52260; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_3; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
DR BioCyc; MAER449447:MAE_RS22725-MON; -.
DR Proteomes; UP000001510; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
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 Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..394
FT /note="NAD(P)H-quinone oxidoreductase subunit H"
FT /id="PRO_0000371889"
SQ SEQUENCE 394 AA; 45425 MW; 3BF80B5C781C7281 CRC64;
MAKIETRTEP MVLNMGPHHP SMHGVLRLIV TLDGEDVIDC EPVIGYLHRG MEKIAENRTN
VMYVPYVSRW DYAAGMFNEA ITVNAPEKLA DIAVPKRAQY IRVIMLELNR IANHLLWLGP
FMADVGAQTP FFYIFREREM IYDLWEAATG MRLINNNYFR IGGVAVDLPY GWVDKCVDFC
DYFDPKVDEY EKLITNNPIF RRRIEGIGCI TRDEAINWGL SGPMLRASGV KWDLRKVDHY
ECYDDFDWEV HWETAGDCFA RYLVRIREMR ESVKIIRQAL KGLPGGPYEN LEAKRMAEGK
KSAWNDFDYQ YIAKKVAPTF KIPKGEHYVR LESGKGELGI FIVGNDDVFP WRWKIRAADF
NNLQILPHIL KGVKVADIMA ILGSIDIIMG SVDR
