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Database: UniProt
Entry: X5JW66_9NOST
LinkDB: X5JW66_9NOST
Original site: X5JW66_9NOST 
ID   X5JW66_9NOST            Unreviewed;       119 AA.
AC   X5JW66;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   31-JAN-2018, entry version 13.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            EC=1.6.5.- {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=RintRC_6632 {ECO:0000313|EMBL:CDN15205.1};
OS   Richelia intracellularis.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Richelia.
OX   NCBI_TaxID=1164990 {ECO:0000313|EMBL:CDN15205.1, ECO:0000313|Proteomes:UP000019767};
RN   [1] {ECO:0000313|EMBL:CDN15205.1, ECO:0000313|Proteomes:UP000019767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC01 {ECO:0000313|EMBL:CDN15205.1,
RC   ECO:0000313|Proteomes:UP000019767};
RA   Hilton J.;
RL   Submitted (JAN-2014) 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:0000256|HAMAP-Rule:MF_01352}.
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
CC       plastoquinol. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01352}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01352}; Cytoplasmic side
CC       {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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDN15205.1}.
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DR   EMBL; CBZS010000626; CDN15205.1; -; Genomic_DNA.
DR   EnsemblBacteria; CDN15205; CDN15205; RintRC_6632.
DR   Proteomes; UP000019767; Unassembled WGS sequence.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019767};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01352};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01352};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019767};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01352}.
SQ   SEQUENCE   119 AA;  13499 MW;  5983E1F4E8E57F3D CRC64;
     MDNSMLLKST TRHIHIFAAE IDQDGELVSS NQVLTLDIDP DNEFNWNEDA LQNVYRKFDE
     LVEASSGEDL TDYNLRRIGS DLEHYVRSLL QKGEITYNLS SRVNNYSMGL PQVATGEAS
//
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