(data stored in ACNUC29543 zone)

SWISSPROT: NDHM_SYNR3

ID   NDHM_SYNR3              Reviewed;         116 AA.
AC   A5GQI1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 61.
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=SynRCC307_0237;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor,
CC       via FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       respiratory and/or the photosynthetic chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       plastoquinone. Couples the redox reaction to proton translocation,
CC       and thus conserves the redox energy in a proton gradient.
CC       Cyanobacterial NDH-1 also plays a role in inorganic carbon-
CC       concentration. {ECO:0000255|HAMAP-Rule:MF_01352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol
CC         + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62192; Evidence={ECO:0000255|HAMAP-Rule:MF_01352};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol
CC         + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62192; 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
CC       identified which probably have different functions.
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01352}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01352}; Cytoplasmic side
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
CC   -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01352}.
DR   EMBL; CT978603; CAK27140.1; -; Genomic_DNA.
DR   RefSeq; WP_011934655.1; NC_009482.1.
DR   SMR; A5GQI1; -.
DR   STRING; 316278.SynRCC307_0237; -.
DR   EnsemblBacteria; CAK27140; CAK27140; SynRCC307_0237.
DR   KEGG; syr:SynRCC307_0237; -.
DR   eggNOG; ENOG4105GHY; Bacteria.
DR   eggNOG; ENOG4111NC5; LUCA.
DR   HOGENOM; HOG000069835; -.
DR   KO; K05584; -.
DR   OMA; PDNEFLW; -.
DR   OrthoDB; 1815256at2; -.
DR   BioCyc; SSP316278:G1GJL-233-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0042651; C: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;
DR   PRODOM; A5GQI1.
DR   SWISS-2DPAGE; A5GQI1.
KW   Complete proteome; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transport.
FT   CHAIN         1    116       NAD(P)H-quinone oxidoreductase subunit M.
FT                                /FTId=PRO_0000352206.
SQ   SEQUENCE   116 AA;  13057 MW;  A5AF91784F41AC88 CRC64;
     MSDTPLKCTT RHVRIFTATV EDNGELKASS DKLTLDLDPD NEFEWDQPVL AKVQQRFAEL
     VDAAAGTELS DYNLRRIGTD LEGFIRQLLQ AGELRYNLGA RVLNYSMGLP RTPETL
//

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