ID   MDH_STEMA               Reviewed;         110 AA.
AC   P80541; Q8RJW4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
DE   Flags: Fragment;
GN   Name=mdh;
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 9181;
RX   PubMed=12021798; DOI=10.1007/s00253-002-0943-6;
RA   Neumann S., Kula M.-R.;
RT   "Gene cloning, overexpression and biochemical characterization of the
RT   peptide amidase from Stenotrophomonas maltophilia.";
RL   Appl. Microbiol. Biotechnol. 58:772-780(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-22.
RC   STRAIN=ICPB 2648-67;
RX   PubMed=9190829; DOI=10.1128/jb.179.12.4066-4070.1997;
RA   Charnock C.;
RT   "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas
RT   species are the first reported MDHs in Proteobacteria which resemble
RT   lactate dehydrogenases in primary structure.";
RL   J. Bacteriol. 179:4066-4070(1997).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ414049; CAC93613.1; -; Genomic_DNA.
DR   AlphaFoldDB; P80541; -.
DR   SMR; P80541; -.
DR   STRING; 1210005.GCA_000295735_02255; -.
DR   eggNOG; COG0039; Bacteria.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..>110
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113404"
FT   BINDING         11..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   NON_TER         110
SQ   SEQUENCE   110 AA;  11619 MW;  123924337D853F79 CRC64;
     MKAPVRVAVT GAAGQIGYAL LFRIASGEML GKDQPVILQL LELPVDKAQA ALKGVMMELE
     DCAFPLLAGM VGTDDAEVAF KDADIALLVG ARPRGPGMER KDLLLENAKI
//