NDHM_POPJC
ID NDHM_POPJC Reviewed; 203 AA.
AC A9PJQ8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 36.
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};
OS Populus jackii (Balm of Gilead) (Populus deltoides x Populus balsamifera).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=640484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. H11-11; TISSUE=Leaf;
RA Ralph S.G., Chun H.J.E., Cooper D., Kirkpatrick R., Palmquist D.,
RA Wynhoven B., Kolosova N., Oddy C., Jancsik S., Douglas C.J., Liu J.,
RA Butterfield Y.S.N., Stott J., Yang G., Holt R.A., Siddiqui A.,
RA Jones S.J.M., Marra M.A., Ritland K., Bohlmann J.;
RT "The poplar transcriptome: analysis of ca. 4,700 sequence-verified full-
RT length cDNAs.";
RL Submitted (NOV-2006) 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; EF148649; ABK96611.1; -; mRNA.
DR AlphaFoldDB; A9PJQ8; -.
DR SMR; A9PJQ8; -.
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 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 Thylakoid; Transit peptide; Translocase; Transport.
FT TRANSIT 1..21
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 22..203
FT /note="NAD(P)H-quinone oxidoreductase subunit M,
FT chloroplastic"
FT /id="PRO_0000352664"
FT REGION 34..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 23538 MW; 2D0A655F9A998D2F CRC64;
MAASSSYMAC AKFSMLGWLG GRRELKMRRV ISVSPQEQAE VQESQEVNAQ EEEKVKQPVQ
PRPVEPQVNV KSKNMGREYG GQWLSSVTRH VRIYAAYIDP ETCEFDQTQT DKLTLILDPT
DEFVWTDETC YKVYSYFQEL VDHYEGAPLT EYTLRLIGSD IEHYIRKLLY DGEIKYNMNA
RVLNFSMGKP RILFNNDGQL QDV