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Database: UniProt
Entry: NDHM_SYNY3
LinkDB: NDHM_SYNY3
Original site: NDHM_SYNY3 
ID   NDHM_SYNY3              Reviewed;         121 AA.
AC   P74338;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   07-NOV-2018, entry version 100.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M;
DE            EC=1.6.5.-;
DE   AltName: Full=NAD(P)H dehydrogenase I subunit M;
DE            Short=NDH-1 subunit M;
DE            Short=NDH-M;
GN   Name=ndhM; OrderedLocusNames=slr1623;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-19, AND CHARACTERIZATION AS A MEMBER OF THE
RP   NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX.
RX   PubMed=8325373; DOI=10.1016/0014-5793(93)81800-F;
RA   Berger S., Ellersiek U., Kinzelt D., Steinmueller K.;
RT   "Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-
RT   oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803.";
RL   FEBS Lett. 326:246-250(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-8, CHARACTERIZATION AS A MEMBER OF THE
RP   NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX   PubMed=15102833; DOI=10.1074/jbc.M401107200;
RA   Prommeenate P., Lennon A.M., Markert C., Hippler M., Nixon P.J.;
RT   "Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803:
RT   identification of two new ndh gene products with nuclear-encoded
RT   homologues in the chloroplast Ndh complex.";
RL   J. Biol. Chem. 279:28165-28173(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 52-71; 73-82 AND 90-107, AND SUBCOMPLEXES OF
RP   NDH-1.
RX   PubMed=15548534; DOI=10.1074/jbc.M410914200;
RA   Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M.;
RT   "Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M
RT   complexes of Synechocystis sp. PCC 6803.";
RL   J. Biol. Chem. 280:2587-2595(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16287171; DOI=10.1002/pmic.200500111;
RA   Srivastava R., Pisareva T., Norling B.;
RT   "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT   6803.";
RL   Proteomics 5:4905-4916(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
CC       plastoquinol.
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   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000305|PubMed:16287171}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:16287171}; Cytoplasmic side
CC       {ECO:0000305|PubMed:16287171}.
CC   -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC       {ECO:0000305}.
DR   EMBL; BA000022; BAA18432.1; -; Genomic_DNA.
DR   PIR; S76173; S76173.
DR   IntAct; P74338; 3.
DR   STRING; 1148.SYNGTS_1858; -.
DR   PaxDb; P74338; -.
DR   PRIDE; P74338; -.
DR   EnsemblBacteria; BAA18432; BAA18432; BAA18432.
DR   KEGG; syn:slr1623; -.
DR   InParanoid; P74338; -.
DR   KO; K05584; -.
DR   OMA; PDNEFLW; -.
DR   PhylomeDB; P74338; -.
DR   Proteomes; UP000001425; 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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Membrane; NAD; NADP;
KW   Oxidoreductase; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Transport.
FT   CHAIN         1    121       NAD(P)H-quinone oxidoreductase subunit M.
FT                                /FTId=PRO_0000352209.
SQ   SEQUENCE   121 AA;  14078 MW;  857E12852DE8656A CRC64;
     MLVKSTTRHV RIFSAEVQGN ELIPSNNVLT MDVDPDNEFV WNEDALQQVY RRFDELVESY
     SGEDLTDYNL RRIGSDLEHF IRDLLQAGKV SYNLDCRVLN YSMGLPKVEN QETAGKYWLD
     N
//
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