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 24-JAN-2024, entry version 133. 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) (Lathyrus oleraceus). 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}. 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; 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: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 CDD; cd01338; MDH_choloroplast_like; 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 PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1. DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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; 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 //