ID   MDHP_SPIOL              Reviewed;         435 AA.
AC   P52426;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 129.
DE   RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE            EC=1.1.1.82;
DE   AltName: Full=NADP-MDH;
DE   Flags: Precursor;
GN   Name=MDH;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf mesophyll;
RA   Harnecker J., Scheibe R., von Schaewen A.;
RT   "Full-length cDNA sequence for chloroplast NADP-dependent malate
RT   dehydrogenase from spinach (Spinacia oleracea L.).";
RL   (er) Plant Gene Register PGR95-106(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-84, AND MUTAGENESIS.
RX   PubMed=8476924; DOI=10.1016/0167-4838(93)90272-s;
RA   Ocheretina O., Harnecker J., Rother T., Schmid R., Scheibe R.;
RT   "Effects of N-terminal truncations upon chloroplast NADP-malate
RT   dehydrogenases from pea and spinach.";
RL   Biochim. Biophys. Acta 1163:10-16(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(+) = oxaloacetate + NADPH + H(+);
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, disulfides bridges
CC       on the protein must be reduced by thioredoxin which receives electrons
CC       from ferredoxin and the electron transport system of photosynthesis (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: Removal of amino acids 57 to 76 results in the formation of
CC       active monomers, a shift of the pH optimum from 8 to 7, the loss of
CC       oxaloacetate inhibition and an increased maximal velocity.
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; X84020; CAA58848.1; -; mRNA.
DR   PIR; S52268; S52268.
DR   AlphaFoldDB; P52426; -.
DR   SMR; P52426; -.
DR   BioCyc; MetaCyc:MONOMER-17409; -.
DR   SABIO-RK; P52426; -.
DR   Proteomes; UP000813463; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0046554; F:L-malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0019674; P:NAD+ 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   CDD; cd01338; MDH_chloroplast-like; 1.
DR   FunFam; 3.90.110.10:FF:000002; Malate dehydrogenase; 1.
DR   FunFam; 3.40.50.720:FF:000144; Malate dehydrogenase [NADP]; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01757; Malate-DH_plant; 1.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   NCBIfam; NF003916; PRK05442.1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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..45
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:8476924"
FT   CHAIN           46..435
FT                   /note="Malate dehydrogenase [NADP], chloroplastic"
FT                   /id="PRO_0000018649"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..104
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..218
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   SITE            69
FT                   /note="Activation of NADP-MDH"
FT                   /evidence="ECO:0000250"
FT   SITE            74
FT                   /note="Activation of NADP-MDH"
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..74
FT                   /note="In oxidized inactive NAD-MDH"
FT                   /evidence="ECO:0000250"
FT   DISULFID        410..422
FT                   /note="In oxidized inactive NAD-MDH"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  47488 MW;  D68AA5D3ED7946A9 CRC64;
     MAVAELSPCY QTQIVKPPHL SWLSNNHKLN LLGLPKASRI TEICCSLAPN QVQTPVAVPT
     GAQSIKPECY GVFCWTYDLK KEEETRSWKK MITIAISGAA GTISNHLLFK LASGVVFGPD
     QPIALKLLGS EKSFHALEGV AMELEDSLYP LLREVSIGID PYEVFEDAEW ALLIGAKPRG
     PGMERADLLD INGKIYAEQG KALNAVASPN VKVIVVGNPC NTNALICLKN PPNIPAKNFH
     SLTRLDENRA KCQLALKAGV FYDKVSNVTI WGNHSTTQVP DFVNAQIGGV PVKEVIKAQK
     WLEEEFTEKV RKRGGVLIQK WGRSSAASTA VSIVDAINPL ITPTPPGDWF PSGVYTNGNP
     YGIAEDLIYS MPCRSKGDGD YELVKDVIFD DYLRKRIKTS EEELLAEKRC TAHLTGEGIA
     VCDLPAGDTM LPGEM
//