ID MDHP_FLABI Reviewed; 453 AA. AC P46489; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-SEP-2023, entry version 127. DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic; DE EC=1.1.1.82; DE AltName: Full=NADP-MDH; DE Flags: Precursor; OS Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC Heliantheae alliance; Tageteae; Flaveria. OX NCBI_TaxID=4224; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RA Trevanion S.J., Ashton A.R.; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP CRYSTALLIZATION. RX PubMed=9761865; DOI=10.1107/s0907444997015655; RA Macpherson K.H., Ashton A.R., Carr P.D., Trevanion S.J., Verger D., RA Ollis D.L.; RT "Crystallization and preliminary crystallographic studies of chloroplast RT NADP-dependent malate dehydrogenase from Flaveria bidentis."; RL Acta Crystallogr. D 54:654-656(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT. RC TISSUE=Leaf; RX PubMed=10196131; DOI=10.1016/s0969-2126(99)80058-6; RA Carr P.D., Verger D., Ashton A.R., Ollis D.L.; RT "Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent RT regulation of activity by thiol oxidation and reduction."; RL Structure 7:461-475(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:10196131}. 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; L40958; AAA63907.1; -; mRNA. DR PDB; 1CIV; X-ray; 2.80 A; A=69-453. DR PDBsum; 1CIV; -. DR AlphaFoldDB; P46489; -. DR SMR; P46489; -. DR EvolutionaryTrace; P46489; -. 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..68 FT /note="Chloroplast" FT CHAIN 69..453 FT /note="Malate dehydrogenase [NADP], chloroplastic" FT /id="PRO_0000018642" FT ACT_SITE 293 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 117..123 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10196131" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 211 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 218 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10196131" FT BINDING 235..237 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10196131" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT SITE 88 FT /note="Activation of NADP-MDH" FT /evidence="ECO:0000250" FT SITE 93 FT /note="Activation of NADP-MDH" FT /evidence="ECO:0000250" FT DISULFID 88..93 FT /note="In oxidized inactive NAD-MDH" FT DISULFID 429..441 FT /note="In oxidized inactive NAD-MDH" FT TURN 90..93 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:1CIV" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 121..131 FT /evidence="ECO:0007829|PDB:1CIV" FT TURN 132..136 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 153..164 FT /evidence="ECO:0007829|PDB:1CIV" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:1CIV" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 204..225 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 239..248 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 263..277 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 318..323 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 325..329 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 332..338 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 345..360 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 369..374 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 384..393 FT /evidence="ECO:0007829|PDB:1CIV" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:1CIV" FT HELIX 410..429 FT /evidence="ECO:0007829|PDB:1CIV" FT TURN 430..435 FT /evidence="ECO:0007829|PDB:1CIV" SQ SEQUENCE 453 AA; 49515 MW; 7CD3A0F9F2A7B539 CRC64; MAVVKLSPWA NYSSSKSEIK SSSSSSSSKS SLSAYVINVS SSPRLSFYNP YPRRLHHQRL SSPASIRCSV TSSDQIQAPL PAKQKPECFG VFCLTYDLKA EEETKSWKKI INVAVSGAAG MISNHLLFKL ASGEVFGPDQ PISLKLLGSE RSFAALEGVA MELEDSLYPL LRQVSIGIDP YEIFQDAEWA LLIGAKPRGP GMERADLLDI NGQIFAEQGK ALNAVASPNV KVMVVGNPCN TNALICLKNA PNIPPKNFHA LTRLDENRAK CQLALKAGVF YDKVSNVTIW GNHSTTQVPD FLNAKIHGIP VTEVIRDRKW LEDEFTNMVQ TRGGVLIKKW GRSSAASTAV SIVDAIRSLV TPTPEGDWFS TGVYTNGNPY GIAEDIVFSM PCRSKGDGDY EFVKDVIFDD YLSKKIKKSE DELLAEKKCV AHLTGEGIAV CDLPEDTMLP GEM //