ID MDHP_MEDSA Reviewed; 437 AA. AC O48902; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 75. DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic; DE EC=1.1.1.82; DE AltName: Full=NADP-MDH; DE Flags: Precursor; GN Name=MDH1; Synonyms=P1MDH; OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; OC Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Saranac; TISSUE=Root nodule; RX MEDLINE=98388648; PubMed=9721676; RX DOI=10.1046/j.1365-313X.1998.00192.x; RA Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.; RT "Alfalfa malate dehydrogenase (MDH): molecular cloning and RT characterization of five different forms reveals a unique nodule- RT enhanced MDH."; RL Plant J. 15:173-184(1998). 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 (By similarity). 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 (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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; AF020269; AAB99753.1; -; mRNA. DR HSSP; P46489; 1CIV. DR SMR; O48902; 69-434. DR BRENDA; 1.1.1.82; 815. 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 49 Chloroplast (Potential). FT CHAIN 50 437 Malate dehydrogenase [NADP], FT chloroplastic. FT /FTId=PRO_0000018644. FT NP_BIND 101 107 NADP (By similarity). FT NP_BIND 219 221 NADP (By similarity). FT ACT_SITE 277 277 Proton acceptor (By similarity). FT BINDING 182 182 Substrate (By similarity). FT BINDING 188 188 Substrate (By similarity). FT BINDING 195 195 NADP (By similarity). FT BINDING 202 202 NAD (By similarity). FT BINDING 221 221 Substrate (By similarity). FT BINDING 252 252 Substrate (By similarity). FT SITE 72 72 Activation of NADP-MDH (By similarity). FT SITE 77 77 Activation of NADP-MDH (By similarity). FT DISULFID 72 77 In oxidized inactive NAD-MDH (By FT similarity). FT DISULFID 413 425 In oxidized inactive NAD-MDH (By FT similarity). SQ SEQUENCE 437 AA; 47835 MW; 9C7C5377DBA5454A CRC64; MALTQLNNTC SKTQLHSSSQ LSFLSRTLPR HHHCTLAPLH RTQHARISCS VAPNQVQAPA VQTQDPKSKP DCYGVFCLTY DLKAEEETKS WKKLITIAVS GAAGMISNHL LFKLASGEVF GPNQPIALKL LGSERSLQAL EGVAMELEDS LFPLLREVVI SIDPYEVFQD AEWALLIGAK PRGPGMERAA LLDINGQIFA EQGKALNAVA SRNVKVIVVG NPCNTNALIC LKNAPNIPAK NFHALTRLDE NRAKCQLALK AGVFYDKVSN MTIWGNHSTT QVPDFLNARI DGLPVKEVIK DHKWLEEEFT EKVQKRGGAL IQKWGRSSAA STSVSIVDAI RSLIIPTPEG DWFSTGVYTT GNPYGIAEDI VFSMPCRSKG DGDYELVKDV IFDDYLRQKL AKTEAELLAE KKCVAHLTGE GIAVCDLPGD TMLPGEM //