NDHM_PHYPA
ID NDHM_PHYPA Reviewed; 204 AA.
AC A9THA7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit M, chloroplastic {ECO:0000305};
DE EC=7.1.1.- {ECO:0000305};
DE AltName: Full=NAD(P)H dehydrogenase subunit M {ECO:0000305};
DE Short=NDH subunit M {ECO:0000305};
DE Short=NDH-M {ECO:0000250|UniProtKB:Q2V2S7};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit M {ECO:0000305};
DE Flags: Precursor;
GN Name=ndhM {ECO:0000305}; Synonyms=NDH-M {ECO:0000250|UniProtKB:Q2V2S7};
GN ORFNames=PHYPADRAFT_170083;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Villersexel 2003; TISSUE=Protonema;
RG DOE Joint Genome Institute Physcomitrella patens EST project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient. {ECO:0000305}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Part of the chloroplast NDH complex, composed of a mixture of
CC chloroplast and nucleus encoded subunits. Component of the NDH
CC subcomplex A, at least composed of ndhH, ndhI, ndhJ, ndhK, ndhL, ndhM,
CC ndhN and ndhO. {ECO:0000250|UniProtKB:Q2V2S7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250|UniProtKB:Q9CAC5}; Peripheral membrane protein
CC {ECO:0000305}; Stromal side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NDH complex subunit M family. {ECO:0000305}.
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DR EMBL; DS545119; EDQ57191.1; -; Genomic_DNA.
DR EMBL; FC386429; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_001777978.1; XM_001777926.1.
DR AlphaFoldDB; A9THA7; -.
DR SMR; A9THA7; -.
DR STRING; 3218.PP1S230_42V6.1; -.
DR EnsemblPlants; Pp3c1_14910V3.1; Pp3c1_14910V3.1; Pp3c1_14910.
DR EnsemblPlants; Pp3c1_14910V3.2; Pp3c1_14910V3.2; Pp3c1_14910.
DR Gramene; Pp3c1_14910V3.1; Pp3c1_14910V3.1; Pp3c1_14910.
DR Gramene; Pp3c1_14910V3.2; Pp3c1_14910V3.2; Pp3c1_14910.
DR eggNOG; ENOG502QUN1; Eukaryota.
DR HOGENOM; CLU_1345188_0_0_1; -.
DR InParanoid; A9THA7; -.
DR OrthoDB; 1404408at2759; -.
DR Proteomes; UP000006727; Chromosome 1.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0010258; P:NADH dehydrogenase complex (plastoquinone) assembly; IEA:EnsemblPlants.
DR InterPro; IPR018922; NdhM.
DR PANTHER; PTHR36900; PTHR36900; 1.
DR Pfam; PF10664; NdhM; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Transit peptide; Translocase; Transport.
FT TRANSIT 1..27
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 28..204
FT /note="NAD(P)H-quinone oxidoreductase subunit M,
FT chloroplastic"
FT /id="PRO_0000352666"
SQ SEQUENCE 204 AA; 23130 MW; 8177DB752172EDCE CRC64;
MASTSMSLTR ACKVHAVLAC SIPSVSSAFL TTNVTFLGQP VEMPSQRWSQ RRCSRPGPVT
VRAEEVKEVT QAKGLSRESG GQWLSCTTRH VRIYAGYVDP ETQVMDQSQL DKLTLMLDPD
NEFEWPEEMV EKVYDKYREL VETYAGADLT EYTLRLIGSD LEHYIRKLLL AGELKYNLDC
RVLNFSMGKP RIDPADLDDV EVEE
