ID   MDHG_CUCSA              Reviewed;         356 AA.
AC   P46488;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Malate dehydrogenase, glyoxysomal;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=MDHG;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Masterpiece; TISSUE=Cotyledon;
RX   PubMed=7858221; DOI=10.1007/bf00019496;
RA   Kim D.J., Smith S.M.;
RT   "Expression of a single gene encoding microbody NAD-malate dehydrogenase
RT   during glyoxysome and peroxisome development in cucumber.";
RL   Plant Mol. Biol. 26:1833-1841(1994).
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. {ECO:0000250}.
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; L31900; AAC41647.1; -; mRNA.
DR   PIR; S52039; S52039.
DR   RefSeq; NP_001292692.1; NM_001305763.1.
DR   AlphaFoldDB; P46488; -.
DR   SMR; P46488; -.
DR   STRING; 3659.XP_004143423.1; -.
DR   PRIDE; P46488; -.
DR   GeneID; 101219252; -.
DR   KEGG; csv:101219252; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..36
FT                   /note="Glyoxysome"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..356
FT                   /note="Malate dehydrogenase, glyoxysomal"
FT                   /id="PRO_0000018639"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         51..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  37739 MW;  78695445C8D9E7B1 CRC64;
     MQPIPDVNQR IARISAHLHP PKYQMEESSV LRRANCRAKG GAPGFKVAIL GAAGGIGQPL
     AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF LGQQQLERAL TGMDLVVIPA
     GVPRKPGMTR DDLFKINAGI VKTLCEGIAK CCPTAIVNLI SNPVNSTVPI AAEVFKKAGT
     YDPKRLLGVT MLDVVRANTF VAEVLGLDPR DVNVPVVGGH AGVTILPLLS QVKPPSSFTQ
     EEINYLTDRI QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVVECAFVSS
     QVTELPFFAT KVRLGRNGID EVYSLGPLNE YERIGLEKAK KELAGSIEKG VSFIRG