NDHM_SYNJB
ID NDHM_SYNJB Reviewed; 121 AA.
AC Q2JNM8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, 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}; OrderedLocusNames=CYB_0644;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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}.
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DR EMBL; CP000240; ABD01631.1; -; Genomic_DNA.
DR RefSeq; WP_011432289.1; NC_007776.1.
DR AlphaFoldDB; Q2JNM8; -.
DR SMR; Q2JNM8; -.
DR STRING; 321332.CYB_0644; -.
DR KEGG; cyb:CYB_0644; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OMA; PDNEFLW; -.
DR OrthoDB; 1815256at2; -.
DR Proteomes; UP000001938; Chromosome.
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; PTHR36900; 1.
DR Pfam; PF10664; NdhM; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..121
FT /note="NAD(P)H-quinone oxidoreductase subunit M"
FT /id="PRO_0000352204"
SQ SEQUENCE 121 AA; 13946 MW; EF335E2D3D13C572 CRC64;
MLKCTTRHVH IFAGEVTADN NFVPRDDLFT LDVDPDNELV WTDAALQKVY ARFEELVEEY
RGRDLTEYNI RRIGSDLEHF IRSLLKQGEI AYNLQGRAPN FSMGFPQIPA EEIVGQYIPK
G
