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Database: UniProt
Entry: A0A1S3V8Q6_VIGRR
LinkDB: A0A1S3V8Q6_VIGRR
Original site: A0A1S3V8Q6_VIGRR 
ID   A0A1S3V8Q6_VIGRR        Unreviewed;       436 AA.
AC   A0A1S3V8Q6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   Name=LOC106772560 {ECO:0000313|RefSeq:XP_014514534.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014514534.1};
RN   [1] {ECO:0000313|RefSeq:XP_014514534.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014514534.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_014514534.1; XM_014659048.2.
DR   AlphaFoldDB; A0A1S3V8Q6; -.
DR   STRING; 3916.A0A1S3V8Q6; -.
DR   GeneID; 106772560; -.
DR   KEGG; vra:106772560; -.
DR   OrthoDB; 312003at2759; -.
DR   Proteomes; UP000087766; Chromosome 8.
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:UP000087766};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          95..242
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          245..415
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
SQ   SEQUENCE   436 AA;  47770 MW;  4FBFB2C9DC3F32E6 CRC64;
     MAVTHFNPTC SKPRLHSSQL SFLSRTLPRH RHCSFAPLHR TQHARISCSV APNEVQVPAV
     TTLDPKSKAD CYGVFCLTYD LRAEEETRSW KKLINIAVSG AAGMIANHLL FKLASGEVFG
     PDQPIALKLL GSERSIQALE GVAMELEDSL FPLLREVSIG IDPYEVFQDA EWALLIGAKP
     RGPGMERADL LDINGQIYAA QGRALNAVAS RNVKVIVVGN PCNTNALICL KNAPNIPAKN
     FHALTRLDEN RAKCQLALKA GVFYDKVSNV TIWGNHSTTQ VPDFLNAKID GLPVKEVVKD
     IRWLEEEFTE KVQKRGGALI QKWGRSSAAS TSVSIVDAIR SLVTPTPEGD WFSSGVYSNG
     NPYGIAEGIV FSMPCRSKGD GDYELVKDVI FDDYLRQRIK KTEAELLAEK RCVAHLTGEG
     IAVCDLPGDT MLPGEM
//
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