ID A0A076HB38_9SYNE Unreviewed; 115 AA.
AC A0A076HB38;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01352};
DE AltName: Full=NAD(P)H dehydrogenase I subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE Short=NDH-1 subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE Short=NDH-M {ECO:0000256|HAMAP-Rule:MF_01352};
GN Name=ndhM {ECO:0000256|HAMAP-Rule:MF_01352};
GN ORFNames=KR49_07570 {ECO:0000313|EMBL:AII46303.1};
OS Synechococcus sp. KORDI-49.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=585423 {ECO:0000313|EMBL:AII46303.1, ECO:0000313|Proteomes:UP000028589};
RN [1] {ECO:0000313|EMBL:AII46303.1, ECO:0000313|Proteomes:UP000028589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-49 {ECO:0000313|EMBL:AII46303.1,
RC ECO:0000313|Proteomes:UP000028589};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequences of Synechococcus sp. KORDI-49.";
RL Submitted (JUN-2013) 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:0000256|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:0000256|ARBA:ARBA00001230, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00001558, ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-
CC Rule:MF_01352}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01352}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01352}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01352}.
CC -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01352}.
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DR EMBL; CP006270; AII46303.1; -; Genomic_DNA.
DR RefSeq; WP_043693228.1; NZ_CP006270.1.
DR AlphaFoldDB; A0A076HB38; -.
DR STRING; 585423.KR49_07570; -.
DR KEGG; synr:KR49_07570; -.
DR PATRIC; fig|585423.3.peg.1438; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OrthoDB; 461686at2; -.
DR Proteomes; UP000028589; 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; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT M, CHLOROPLASTIC; 1.
DR PANTHER; PTHR36900:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT M, CHLOROPLASTIC; 1.
DR Pfam; PF10664; NdhM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01352};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01352};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01352};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW Rule:MF_01352};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01352};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01352};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01352}.
SQ SEQUENCE 115 AA; 12912 MW; B47376DBC0659B65 CRC64;
MADTLLKCTT RHVRLFTARV ENDDLVPDPE QLTLDLDPDN EFIWSDSALT CVQQRFKGLV
DASAGGELSD YSLRRIGTEL EGEIRRLLQA GELSYNPDGR VTNYSMGLPR TPELL
//
