MDHP_PEA
ID MDHP_PEA Reviewed; 441 AA.
AC P21528;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE EC=1.1.1.82;
DE AltName: Full=NADP-MDH;
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8223554; DOI=10.1111/j.1432-1033.1993.tb18233.x;
RA Reng W., Riessland R., Scheibe R., Jaenicke R.;
RT "Cloning, site-specific mutagenesis, expression and characterization of
RT full-length chloroplast NADP-malate dehydrogenase from Pisum sativum.";
RL Eur. J. Biochem. 217:189-197(1993).
RN [2]
RP PROTEIN SEQUENCE OF 65-441, AND DISULFIDE BOND.
RC STRAIN=cv. Kleine Rheinlaenderin;
RX PubMed=1986782; DOI=10.1016/0167-4838(91)90212-i;
RA Scheibe R., Kampfenkel K., Wessels R., Tripier D.;
RT "Primary structure and analysis of the location of the regulatory disulfide
RT bond of pea chloroplast NADP-malate dehydrogenase.";
RL Biochim. Biophys. Acta 1076:1-8(1991).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3665938; DOI=10.1111/j.1432-1033.1987.tb13466.x;
RA Fickenscher K., Scheibe R., Marcus F.;
RT "Amino acid sequence similarity between malate dehydrogenases (NAD) and pea
RT chloroplast malate dehydrogenase (NADP).";
RL Eur. J. Biochem. 168:653-658(1987).
RN [4]
RP PROTEIN SEQUENCE OF 59-74 AND 92-112, AND SUBUNIT.
RC STRAIN=cv. Kleine Rheinlaenderin;
RX PubMed=1472542; DOI=10.1016/0304-4165(92)90098-f;
RA Kampfenkel K.;
RT "Limited proteolysis of NADP-malate dehydrogenase from pea chloroplast by
RT aminopeptidase K yields monomers. Evidence of proteolytic degradation of
RT NADP-malate dehydrogenase during purification from pea.";
RL Biochim. Biophys. Acta 1156:71-77(1992).
CC -!- FUNCTION: The chloroplastic, NADP-dependent form is essential for the
CC photosynthesis C4 cycle, which allows plants to circumvent the problem
CC of photorespiration. In C4 plants, NADP-MDH activity acts to convert
CC oxaloacetate to malate in chloroplasts of mesophyll cells for transport
CC to the bundle sheath cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82;
CC -!- ACTIVITY REGULATION: Chloroplast NADP-MDH is activated upon
CC illumination. In order to be enzymatically active, disulfide bridges on
CC the protein must be reduced by thioredoxin which receives electrons
CC from ferredoxin and the electron transport system of photosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1472542}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR EMBL; X74507; CAA52614.1; -; mRNA.
DR PIR; S38346; S38346.
DR AlphaFoldDB; P21528; -.
DR SMR; P21528; -.
DR IntAct; P21528; 1.
DR MINT; P21528; -.
DR SABIO-RK; P21528; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants.
DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:EnsemblPlants.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0051775; P:response to redox state; IEA:EnsemblPlants.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR011273; Malate_DH_NADP-dep_pln.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01757; Malate-DH_plant; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Disulfide bond; NADP;
KW Oxidoreductase; Plastid; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1472542"
FT CHAIN 59..441
FT /note="Malate dehydrogenase [NADP], chloroplastic"
FT /id="PRO_0000018646"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 105..111
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 223..225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 76
FT /note="Activation of NADP-MDH"
FT SITE 81
FT /note="Activation of NADP-MDH"
FT DISULFID 76..81
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000269|PubMed:1986782"
FT DISULFID 417..429
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
FT CONFLICT 90
FT /note="E -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="C -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="P -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="N -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48264 MW; 613747E6357C325B CRC64;
MALTQLNSTC SKPQLHSSSQ LSFLSRTRTR TLPRHYHSTF APLHRTQHAR ISCSVAPNQV
QVPAAQTQDP KGKPDCYGVF CLTYDLKAEE ETKSWKKLIN IAVSGAAGMI SNHLLFKLAS
GEVFGPDQPI ALKLLGSERS IQALEGVAME LEDSLFPLLR EVVISIDPYE VFQDAEWALL
IGAKPRGPGV ERAALLDING QIFAEQGKAL NAVASRNAKV IVVGNPCNTN ALICLKNAPN
IPAKNFHALT RLDENRAKCQ LALKAGVFYD KVSNMTIWGN HSTTQVPDFL NARIDGLPVK
EVIKDNKWLE EEFTEKVQKR GGVLIQKWGR SSAASTSVSI VDAIRSLITP TPEGDWFSSG
VYTNGNPYGI AEDIVFSMPC RSKGDGDYEL VNDVIFDDYL RQKLAKTEAE LLAEKKCVAH
LTGEGIAVCD LPGDTMLPGE M
