MDHP2_SORBI
ID MDHP2_SORBI Reviewed; 432 AA.
AC P37229;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Malate dehydrogenase [NADP] 2, chloroplastic;
DE EC=1.1.1.82;
DE AltName: Full=NADP-MDH-2;
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=1896015; DOI=10.1007/bf00260642;
RA Luchetta P., Cretin C., Gadal P.;
RT "Organization and expression of the two homologous genes encoding the NADP-
RT malate dehydrogenase in Sorghum vulgare leaves.";
RL Mol. Gen. Genet. 228:473-481(1991).
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:0000250}.
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; X54404; CAA38270.1; -; Genomic_DNA.
DR EMBL; S55884; AAB19835.2; -; Genomic_DNA.
DR PIR; S17781; S17781.
DR PIR; S20743; S20743.
DR AlphaFoldDB; P37229; -.
DR SMR; P37229; -.
DR STRING; 4558.Sb07g023910.1; -.
DR eggNOG; KOG1496; Eukaryota.
DR HOGENOM; CLU_040727_1_0_1; -.
DR BRENDA; 1.1.1.82; 5768.
DR ExpressionAtlas; P37229; 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 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 Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 41..432
FT /note="Malate dehydrogenase [NADP] 2, chloroplastic"
FT /id="PRO_0000018648"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 96..102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 67
FT /note="Activation of NADP-MDH"
FT SITE 72
FT /note="Activation of NADP-MDH"
FT DISULFID 67..72
FT /note="In oxidized inactive NAD-MDH"
FT DISULFID 408..420
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 46640 MW; 94CAB78C824DB5AA CRC64;
MGLSTAYSPA GSGLVPAPLA RAARRRSVQV RRPRLATVRC SVVDAAKQVQ DGVATAVGGG
AASGNECFGV FCNIYDLKAE DKTKSWKKLV TIAVSGAAGM ISNHLLFKLA SGEVFGQDQP
IALKLLGSER SFQALEGVRM ELEDSLYPLL REVSIGIGPY EVFQDVDWAL LIGAKPRGPG
MERAALLDIN GQIFADQGKA LNAVASRNVK VLVVGNPCNT NALICLKNTP NIPAKNFHAL
TRLDENRAKC QIALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEIIQDTKWL
EEEFTMTVQK RGGVLIQKWG RSSAASTAVS IVDAIKSLVT PTPEGEWFST GVYTTGNPYG
IAEDIVFSMP CRSKGDGDYE LATDVSMDDF LWERIKKSEA ELLAEKKCVA HLTGEGDAFC
DLPEDTMLPG EN
