ID   MDHG_SOYBN              Reviewed;         353 AA.
AC   P37228;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Malate dehydrogenase, glyoxysomal;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-353.
RC   STRAIN=cv. Maple Arrow; TISSUE=Cotyledon;
RX   PubMed=8547819; DOI=10.1007/bf00202659;
RA   Guex N., Henry H., Flach J., Richter H., Widmer F.;
RT   "Glyoxysomal malate dehydrogenase and malate synthase from soybean
RT   cotyledons (Glycine max L.): enzyme association, antibody production and
RT   cDNA cloning.";
RL   Planta 197:369-375(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-3.
RC   STRAIN=cv. Maple Arrow; TISSUE=Cotyledon;
RA   Richter H., Guex N.;
RL   Submitted (JAN-1996) to UniProtKB.
RN   [3]
RP   3D-STRUCTURE MODELING.
RA   Guex N., Widmer F., Gaillard P., Carrupt P.-A.;
RT   "3D modeling of soybean glyoxysomal malate dehydrogenase (gMDH).";
RL   (In) Wermuth C.G. (eds.);
RL   Trends in QSAR and molecular modelling 92, pp.485-486, Escom Science
RL   Publishers, Leiden (1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; L01628; AAC37464.1; -; mRNA.
DR   AlphaFoldDB; P37228; -.
DR   SMR; P37228; -.
DR   STRING; 3847.GLYMA11G04720.1; -.
DR   PRIDE; P37228; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
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; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   2: Evidence at transcript level;
KW   Glyoxylate bypass; Glyoxysome; NAD; Oxidoreductase; Peroxisome;
KW   Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..33
FT                   /note="Glyoxysome"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..353
FT                   /note="Malate dehydrogenase, glyoxysomal"
FT                   /id="PRO_0000018641"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..54
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         268
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  37395 MW;  D2B0BF1AE6CC8925 CRC64;
     MEANSGASDR ISRIAGHLRP QREDDVCLKR SDCRAKGGVS GFKVAILGAA GGIGQPLAML
     MKMNPLVSLL HLYDVVNTPG VTSDISHMDT GAVVRGFLGQ QQLEDALIGM DLVIIPAGVP
     RKPGMTRDDL FNINAGIVKT LCEAIAKCCP KAIVNVISNP VNSTVPIAAE VFKRAGTYDP
     KRLLGVTMLD VVRANTFVAE VLGVDPRDVD VPVVGGHAGI TILPLLSQIK PPCSFTPKEI
     EYLTGRIQNG GPEVVEAKAG AGSATLSMAY AAVKFADACL HALRGDAGII ECAYVASQVT
     ELPFFASKVR LGRVGVEEIL PLGPLNDYER ESLEKAKKEL AASIEKGISF IRK