NDHM_THEVB
ID NDHM_THEVB Reviewed; 111 AA.
AC Q8DLN5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit M;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase I subunit M;
DE Short=NDH-1 subunit M;
DE Short=NDH-M;
GN Name=ndhM; OrderedLocusNames=tll0447;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15910282; DOI=10.1042/bj20050390;
RA Zhang P., Battchikova N., Paakkarinen V., Katoh H., Iwai M., Ikeuchi M.,
RA Pakrasi H.B., Ogawa T., Aro E.-M.;
RT "Isolation, subunit composition and interaction of the NDH-1 complexes from
RT Thermosynechococcus elongatus BP-1.";
RL Biochem. J. 390:513-520(2005).
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC {ECO:0000305}.
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DR EMBL; BA000039; BAC07999.1; -; Genomic_DNA.
DR RefSeq; NP_681237.1; NC_004113.1.
DR RefSeq; WP_011056300.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; M=1-111.
DR PDB; 6KHI; EM; 3.00 A; M=1-111.
DR PDB; 6KHJ; EM; 3.00 A; M=1-111.
DR PDB; 6L7O; EM; 3.20 A; M=1-111.
DR PDB; 6L7P; EM; 3.60 A; M=1-111.
DR PDB; 6NBQ; EM; 3.10 A; M=1-111.
DR PDB; 6NBX; EM; 3.50 A; M=1-111.
DR PDB; 6NBY; EM; 3.10 A; M=1-111.
DR PDB; 6TJV; EM; 3.20 A; M=1-111.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBQ; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DLN5; -.
DR SMR; Q8DLN5; -.
DR IntAct; Q8DLN5; 1.
DR STRING; 197221.22294168; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC07999; BAC07999; BAC07999.
DR KEGG; tel:tll0447; -.
DR PATRIC; fig|197221.4.peg.471; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR OMA; PDNEFLW; -.
DR OrthoDB; 1815256at2; -.
DR Proteomes; UP000000440; 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 1: Evidence at protein level;
KW 3D-structure; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..111
FT /note="NAD(P)H-quinone oxidoreductase subunit M"
FT /id="PRO_0000352198"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6TJV"
FT STRAND 14..24
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6TJV"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6L7O"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6NBQ"
FT HELIX 67..86
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6NBQ"
SQ SEQUENCE 111 AA; 12567 MW; AE906E9BE85CB0BE CRC64;
MLLKSTTRHV HIYAGHVVDG EVHPDTETLT LNVDPDNELE WNEAALAKVE AKFRELVANA
AGEDLTEYNL RRIGSDLEHF IRSLLMQGEI GYNLNSRVRN YSLGIPRVNH S
