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 16-JUN-2009, entry version 72. 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). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Aizoaceae; Mesembryanthemum. 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 RT dehydrogenase during Crassulacean acid metabolism induction by salt RT stress."; RL Photosyn. Res. 35:15-27(1993). CC -!- FUNCTION: The chloroplastic, NADP-dependent form is essential for CC the photosynthesis C4 cycle, which allows plants to circumvent the CC problem of photorespiration. In C4 plants, NADP-MDH activity acts CC to convert oxaloacetate to malate in chloroplasts of mesophyll CC cells for transport to the bundle sheath cells. CC -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = oxaloacetate + NADPH. CC -!- ENZYME REGULATION: Chloroplast NADP-MDH is activated upon CC illumination. In order to be enzymatically active, disulfides CC bridges on the protein must be reduced by thioredoxin which CC receives electrons from ferredoxin and the electron transport CC system of photosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- INDUCTION: Expression decreases transiently in the leaves after CC salt stress and then increases to levels greater than two-fold CC higher than in unstressed plants. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63727; CAA45270.1; -; mRNA. DR PIR; S33066; S33066. DR HSSP; P46489; 1CIV. DR SMR; Q05145; 72-438. DR BRENDA; 1.1.1.82; 2210. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001236; Lactate/malate_DH. 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_SF1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR23382; MDH_SF1; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR ProDom; PD003052; Mal_dehydrog; 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 Chloroplast (Potential). FT CHAIN 52 441 Malate dehydrogenase [NADP], FT chloroplastic. FT /FTId=PRO_0000018645. FT NP_BIND 104 110 NADP (By similarity). FT NP_BIND 222 224 NADP (By similarity). FT ACT_SITE 280 280 Proton acceptor (By similarity). FT BINDING 185 185 Substrate (By similarity). FT BINDING 191 191 Substrate (By similarity). FT BINDING 198 198 NADP (By similarity). FT BINDING 205 205 NAD (By similarity). FT BINDING 224 224 Substrate (By similarity). FT BINDING 255 255 Substrate (By similarity). FT SITE 75 75 Activation of NADP-MDH (By similarity). FT SITE 80 80 Activation of NADP-MDH (By similarity). FT DISULFID 75 80 In oxidized inactive NAD-MDH (By FT similarity). FT DISULFID 416 428 In oxidized inactive NAD-MDH (By FT similarity). 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 //