ID NDHM_SYNSC Reviewed; 115 AA.
AC Q3AH04;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 79.
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=Syncc9605_2396;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
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., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB36128.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000110; ABB36128.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q3AH04; -.
DR SMR; Q3AH04; -.
DR STRING; 110662.Syncc9605_2396; -.
DR KEGG; syd:Syncc9605_2396; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OrthoDB; 461686at2; -.
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; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..115
FT /note="NAD(P)H-quinone oxidoreductase subunit M"
FT /id="PRO_0000352202"
SQ SEQUENCE 115 AA; 12810 MW; 88DBE95D0F9B2611 CRC64;
MADTLLKCTT RHVRLFTAAL QEEDLVPSDD QLTLDLDPDN EFLWDAASLA KVQGRFKELV
DAAAGGELSD YTLRRIGTDL EGFIRQLLQA GELSYNPDGR VQNFSMGLPR TPELL
//
