NDHM_MICAN
ID NDHM_MICAN Reviewed; 109 AA.
AC B0JPD8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01352};
DE AltName: Full=NAD(P)H dehydrogenase I subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE Short=NDH-1 subunit M {ECO:0000255|HAMAP-Rule:MF_01352};
DE Short=NDH-M {ECO:0000255|HAMAP-Rule:MF_01352};
GN Name=ndhM {ECO:0000255|HAMAP-Rule:MF_01352}; OrderedLocusNames=MAE_06270;
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_01352}.
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_01352};
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_01352};
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_01352}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01352}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01352}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01352}.
CC -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01352}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009552; BAG00449.1; -; Genomic_DNA.
DR RefSeq; WP_002738864.1; NC_010296.1.
DR AlphaFoldDB; B0JPD8; -.
DR SMR; B0JPD8; -.
DR STRING; 449447.MAE_06270; -.
DR PaxDb; B0JPD8; -.
DR EnsemblBacteria; BAG00449; BAG00449; MAE_06270.
DR GeneID; 66706173; -.
DR KEGG; mar:MAE_06270; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OMA; PDNEFLW; -.
DR OrthoDB; 1815256at2; -.
DR BioCyc; MAER449447:MAE_RS02790-MON; -.
DR Proteomes; UP000001510; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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 HAMAP; MF_01352; NDH1_NDH1M; 1.
DR InterPro; IPR018922; NdhM.
DR PANTHER; PTHR36900; PTHR36900; 1.
DR Pfam; PF10664; NdhM; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..109
FT /note="NAD(P)H-quinone oxidoreductase subunit M"
FT /id="PRO_0000352183"
SQ SEQUENCE 109 AA; 12697 MW; 6B85D8CF8ACB0992 CRC64;
MLLKSTTRHI RIYTAEVKNN QLIESNNVLT LDVDPDNEFN WEEVALNKVY SKFDELVESY
NGEELSEYNL RRIGSDLEHF IRSLLQKGEI SYNLNARVQN YSMGLPKLG
