MDHP_MAIZE
ID MDHP_MAIZE Reviewed; 432 AA.
AC P15719;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE EC=1.1.1.82;
DE AltName: Full=NADP-MDH;
DE Flags: Precursor;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Metzler M., Rothermel B.A., Nelson T.;
RT "Maize NADP-malate dehydrogenase: cDNA cloning, sequence, and mRNA
RT characterization.";
RL Plant Mol. Biol. 12:713-722(1989).
RN [2]
RP PROTEIN SEQUENCE OF 58-84.
RX PubMed=3403553; DOI=10.1016/s0021-9258(18)37852-9;
RA Decottignies P., Schmitter J.-M., Miginiac-Maslow M., le Marechal P.,
RA Jacquot J.-P., Gadal P.;
RT "Primary structure of the light-dependent regulatory site of corn NADP-
RT malate dehydrogenase.";
RL J. Biol. Chem. 263:11780-11785(1988).
RN [3]
RP PROTEIN SEQUENCE OF 41-62.
RX PubMed=16668822; DOI=10.1104/pp.98.4.1506;
RA Agostino A., Jeffrey P., Hatch M.D.;
RT "Amino acid sequence and molecular weight of native NADP malate
RT dehydrogenase from the C4 plant Zea mays.";
RL Plant Physiol. 98:1506-1510(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.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X16084; CAA34213.1; -; mRNA.
DR PIR; S04859; DEMZMC.
DR RefSeq; NP_001105420.1; NM_001111950.1.
DR AlphaFoldDB; P15719; -.
DR SMR; P15719; -.
DR STRING; 4577.GRMZM2G129513_P01; -.
DR PaxDb; P15719; -.
DR PRIDE; P15719; -.
DR GeneID; 542374; -.
DR MaizeGDB; 40092; -.
DR eggNOG; KOG1496; Eukaryota.
DR OrthoDB; 1118998at2759; -.
DR BRENDA; 1.1.1.82; 6752.
DR SABIO-RK; P15719; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P15719; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; Reference proteome; Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16668822"
FT CHAIN 41..432
FT /note="Malate dehydrogenase [NADP], chloroplastic"
FT /id="PRO_0000018643"
FT REGION 18..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 96..102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 67
FT /note="Activation of NADP-MDH"
FT SITE 72
FT /note="Activation of NADP-MDH"
FT DISULFID 67..72
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000269|PubMed:3403553"
FT DISULFID 408..420
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 46860 MW; 45531DEF8BBF79FD CRC64;
MGLSTVYSPA GPRLVPAPLG RCRSAQPRRP RRAPLATVRC SVDATKQAQD GVATAVATEA
PASRKECFGV FCTTYDLKAE DKTKSWRKLV NVAVSGAAGM ISNHLLFKLA SGEVFGQDQP
IALKLLGSER SFQALEGVAM ELEDSLYPLL REVSIGIDPY VVFQDVDWAL LIGAKPRGPG
MERAALLDIN GQIFADQGKA LNAVASRNDE VLVVGNPCNT NALICLKNAP NIPAKNFHAL
TRLDENRAKC QLALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEVIKDTKWL
EEEFTLTVQK RGGVLIQKWG RSSAASTAVS IVDAIRSLVT PTPEGDWFST GVYTTGNPYG
IAEDIVFSMP CRSKGDGDYE LASDVLMDDF LWERIKKSEA ELLAEKKCVA HLTGEGNAFC
DLPEDTMLPG EV
