ID A0A067L9D8_JATCU Unreviewed; 437 AA.
AC A0A067L9D8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic {ECO:0000256|ARBA:ARBA00016572};
DE EC=1.1.1.82 {ECO:0000256|ARBA:ARBA00013132};
DE AltName: Full=NADP-MDH {ECO:0000256|ARBA:ARBA00033185};
GN ORFNames=JCGZ_01576 {ECO:0000313|EMBL:KDP45076.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP45076.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP45076.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP45076.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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 Evidence={ECO:0000256|ARBA:ARBA00001500};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
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DR EMBL; KK914240; KDP45076.1; -; Genomic_DNA.
DR RefSeq; XP_012090528.1; XM_012235138.1.
DR AlphaFoldDB; A0A067L9D8; -.
DR STRING; 180498.A0A067L9D8; -.
DR GeneID; 105648670; -.
DR KEGG; jcu:105648670; -.
DR OrthoDB; 312003at2759; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 96..243
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 246..416
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
SQ SEQUENCE 437 AA; 47939 MW; 6E9F115504B0EE0E CRC64;
MAVAELTSPT VAYTHTPTRL HSSSQLSLSS THLSFRLRRS FRPQNTRITC SVDQVQAPVA
VETKKSTDKS DCFGVFCQTY DLRAEEETKS WKKLINIAVS GAAGMISNHL LFKLASGEVF
GPNQPIALKL LGSERSFQAL EGVAMELEDS LYPLLREVSI GINPYEVFED AEWALLIGAK
PRGPGMERAD LLDINGQIFA EQGKALNAVA SRNVKVIVVG NPCNTNALIC LKNAPNIPAK
NFHALTRLDE NRAKCQLALK AGVFYDKVSN VTIWGNHSTT QVPDFLNARI NGLPVKEVIK
DHKWLEEEFT EMVQKRGGLL IQKWGRSSAA STAVSIADAI KSLITPTPEG DWFSSGVYTN
GNPYGIAEGL VFSMPCRSKG DGDYELVKDV IFDDYLLKKI TKTEAELLAE KRCVAHLTGE
GIAFCDLPED TMLPGEM
//
