MDHP_MESCR
ID MDHP_MESCR Reviewed; 441 AA.
AC Q05145;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE EC=1.1.1.82;
DE AltName: Full=NADP-MDH;
DE Flags: Precursor;
GN Name=MDH1;
OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Aizoaceae; Mesembryanthemum;
OC Mesembryanthemum subgen. Cryophytum.
OX NCBI_TaxID=3544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf, and Root;
RA Cushman J.C.;
RT "Molecular cloning and expression of chloroplast NADP-malate dehydrogenase
RT during Crassulacean acid metabolism induction by salt stress.";
RL Photosyn. Res. 35:15-27(1993).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: Expression decreases transiently in the leaves after salt
CC stress and then increases to levels greater than two-fold higher than
CC in unstressed plants.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR EMBL; X63727; CAA45270.1; -; mRNA.
DR PIR; S33066; S33066.
DR AlphaFoldDB; Q05145; -.
DR SMR; Q05145; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..441
FT /note="Malate dehydrogenase [NADP], chloroplastic"
FT /id="PRO_0000018645"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 104..110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 222..224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 75
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250"
FT SITE 80
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250"
FT DISULFID 75..80
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
FT DISULFID 416..428
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 48004 MW; 77AFB169F1488FA7 CRC64;
MAVAELSPSY KTQLKTCQQL SSSLSTRLSD HRKFSLRLLP RPVSVRGGIR CSVAPNQVQA
PVAVPAEGQT GKPECYGIFC LTYDLKAEEE TKTWKKMITI AVSGAAGMIS NHLLFKLASG
EVFGPDQPIA LKLLGSERSF NALEGVAMEL EDSLYPLLRA VSIGIDPYDI FQDAEWALLI
GAKPRGPGME RADLLDINGQ IFAEQGKALN AVASRNVKVI VVGNPCNTNA LICLKNAPNI
PAKNFHGLTR LDENRAKCQL ALKAGVFYDK VSNMTIWGNH STTQVPDFLN AKIDGLPVKT
VIKDHKWLEE EFTVMIQKRG GALIQKWGRS SAASTAVSIA DAIKSLVTPT PEGDWFSSAV
YTNGNPYGIA EDLVFSMPCR SKGDGDYELV KDVVFDDYLR QRIKKSEEEL LAEKRCTAHL
TGEGVAVCDL PAGDTMLPGE M
