ID MDHP1_SORBI Reviewed; 429 AA. AC P17606; P19796; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 24-JAN-2024, entry version 164. DE RecName: Full=Malate dehydrogenase [NADP] 1, chloroplastic; DE EC=1.1.1.82; DE AltName: Full=NADP-MDH-1; DE Flags: Precursor; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. INRA 450; TISSUE=Leaf; RX PubMed=2373367; DOI=10.1016/0378-1119(90)90003-a; RA Luchetta P., Cretin C., Gadal P.; RT "Structure and characterization of the Sorghum vulgare gene encoding NADP- RT malate dehydrogenase."; RL Gene 89:171-177(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Tamaran FNK 140; TISSUE=Leaf; RX PubMed=2209586; DOI=10.1111/j.1432-1033.1990.tb19227.x; RA Cretin C., Luchetta P., Joly C., Decottignies P., Lepiniec L., Gadal P., RA Sallantin M., Huet J.-C., Pernollet J.-C.; RT "Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA RT sequence. Homology with malate dehydrogenase (NAD)."; RL Eur. J. Biochem. 192:299-303(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT. RX PubMed=10194350; DOI=10.1021/bi982876c; RA Johansson K., Ramaswamy S., Saarinen M., Lemaire-Chamley M., RA Issakidis-Bourguet E., Miginiac-Maslow M., Eklund H.; RT "Structural basis for light activation of a chloroplast enzyme: the RT structure of sorghum NADP-malate dehydrogenase in its oxidized form."; RL Biochemistry 38:4319-4326(1999). 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:10194350}. 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; M31965; AAA34047.1; -; Genomic_DNA. DR EMBL; X53453; CAA37531.1; -; mRNA. DR PIR; JH0151; JH0151. DR PIR; S13588; S13588. DR RefSeq; XP_002445670.1; XM_002445625.1. DR PDB; 7MDH; X-ray; 2.40 A; A/B/C/D=55-429. DR PDBsum; 7MDH; -. DR AlphaFoldDB; P17606; -. DR SMR; P17606; -. DR EnsemblPlants; EES15165; EES15165; SORBI_3007G166300. DR GeneID; 8057802; -. DR Gramene; EES15165; EES15165; SORBI_3007G166300. DR KEGG; sbi:8057802; -. DR eggNOG; KOG1496; Eukaryota. DR HOGENOM; CLU_040727_3_0_1; -. DR OMA; ASRHAEC; -. DR OrthoDB; 312003at2759; -. DR BRENDA; 1.1.1.82; 5768. DR SABIO-RK; P17606; -. DR EvolutionaryTrace; P17606; -. DR ExpressionAtlas; P17606; baseline and differential. 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 3D-structure; Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid; KW Transit peptide. FT TRANSIT 1..40 FT /note="Chloroplast" FT /evidence="ECO:0000250" FT CHAIN 41..429 FT /note="Malate dehydrogenase [NADP] 1, chloroplastic" FT /id="PRO_0000018647" FT ACT_SITE 269 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 93..99 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 187 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 211..213 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT SITE 64 FT /note="Activation of NADP-MDH" FT SITE 69 FT /note="Activation of NADP-MDH" FT DISULFID 64..69 FT /note="In oxidized inactive NAD-MDH" FT DISULFID 405..417 FT /note="In oxidized inactive NAD-MDH" FT CONFLICT 226..228 FT /note="APD -> PPH (in Ref. 2; CAA37531)" FT /evidence="ECO:0000305" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:7MDH" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 97..107 FT /evidence="ECO:0007829|PDB:7MDH" FT TURN 108..112 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 129..140 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 147..154 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 156..159 FT /evidence="ECO:0007829|PDB:7MDH" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 180..201 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 207..210 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 239..252 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 294..306 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 308..315 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 321..336 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 345..350 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 360..369 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 386..405 FT /evidence="ECO:0007829|PDB:7MDH" FT HELIX 407..410 FT /evidence="ECO:0007829|PDB:7MDH" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:7MDH" SQ SEQUENCE 429 AA; 46455 MW; 17D9E0A34A67F1FF CRC64; MGLSTAYSPV GSHLAPAPLG HRRSAQLHRP RRALLATVRC SVDAAKQVQD GVATAEAPAT RKDCFGVFCT TYDLKAEDKT KSWKKLVNIA VSGAAGMISN HLLFKLASGE VFGQDQPIAL KLLGSERSFQ ALEGVAMELE DSLYPLLREV SIGIDPYEVF EDVDWALLIG AKPRGPGMER AALLDINGQI FADQGKALNA VASKNVKVLV VGNPCNTNAL ICLKNAPDIP AKNFHALTRL DENRAKCQLA LKAGVFYDKV SNVTIWGNHS TTQVPDFLNA KIDGRPVKEV IKDTKWLEEE FTITVQKRGG ALIQKWGRSS AASTAVSIAD AIKSLVTPTP EGDWFSTGVY TTGNPYGIAE DIVFSMPCRS KGDGDYELAT DVSMDDFLWE RIKKSEAELL AEKKCVAHLT GEGNAYCDVP EDTMLPGEV //