NDHM_SYNE7
ID NDHM_SYNE7 Reviewed; 110 AA.
AC Q31LQ7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
GN OrderedLocusNames=Synpcc7942_1982;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000100; ABB58012.1; -; Genomic_DNA.
DR RefSeq; WP_011244424.1; NC_007604.1.
DR AlphaFoldDB; Q31LQ7; -.
DR SMR; Q31LQ7; -.
DR STRING; 1140.Synpcc7942_1982; -.
DR PRIDE; Q31LQ7; -.
DR EnsemblBacteria; ABB58012; ABB58012; Synpcc7942_1982.
DR KEGG; syf:Synpcc7942_1982; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OMA; PDNEFLW; -.
DR OrthoDB; 1815256at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_1982-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_1982-MON; -.
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; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..110
FT /note="NAD(P)H-quinone oxidoreductase subunit M"
FT /id="PRO_0000352197"
SQ SEQUENCE 110 AA; 12697 MW; EA6F975C60507082 CRC64;
MLLKSTTRHI RIFTAEIEGN ELQPSDTVLT LDVDPDNEFN WNEEALQKVY RQFDDLVESY
AGQELSEYNL RRIGSELEVL LRQMLQAGEI SYNLNCRVLN YSMGVPQAVV
