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 04-NOV-2026, entry version 130. 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(+) = oxaloacetate + NADH + H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L01628; AAC37464.1; -; mRNA. DR AlphaFoldDB; P37228; -. DR SMR; P37228; -. DR STRING; 3847.P37228; -. DR PaxDb; 3847-P37228; -. DR eggNOG; KOG1494; Eukaryota. DR InParanoid; P37228; -. DR OMA; AHLNPRN; -. 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 (NAD+) activity; IBA:GO_Central. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1. DR FunFam; 3.40.50.720:FF:000013; Malate dehydrogenase; 1. DR FunFam; 3.90.110.10:FF:000001; Malate dehydrogenase; 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; 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 NCBIfam; TIGR01772; MDH_euk_gproteo; 1. DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR11540:SF71; MALATE DEHYDROGENASE 1, PEROXISOMAL; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 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 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 //