ID A3YXR8_9SYNE Unreviewed; 116 AA.
AC A3YXR8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=WH5701_00840 {ECO:0000313|EMBL:EAQ75350.1};
OS Synechococcus sp. WH 5701.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ75350.1, ECO:0000313|Proteomes:UP000002935};
RN [1] {ECO:0000313|EMBL:EAQ75350.1, ECO:0000313|Proteomes:UP000002935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ75350.1}.
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DR EMBL; AANO01000004; EAQ75350.1; -; Genomic_DNA.
DR RefSeq; WP_006172269.1; NZ_CH724160.1.
DR AlphaFoldDB; A3YXR8; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OrthoDB; 461686at2; -.
DR Proteomes; UP000002935; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000002935};
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 116 AA; 13067 MW; FE702EA74EE4235D CRC64;
MVDASLLKST TRHVRVFTAR VEDGQLIADP SQLTLDLDPD NEFLWDAPVL GKVQQRFREL
VAASAGHELS EYNLRRIGSE LEGFIRQLLQ AGELRYNPEA RVLNYSMGLP RTPEAS
//
