MDHP_FLABI
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 03-AUG-2022, entry version 123.
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}.
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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 PRIDE; 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 Gene3D; 3.90.110.10; -; 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 PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01757; Malate-DH_plant; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 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
