ID   MDH_KLEPR               Reviewed;         114 AA.
AC   P0C1G5; P80535;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-MAY-2023, entry version 59.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
DE   Flags: Fragment;
GN   Name=mdh;
OS   Klebsiella pneumoniae subsp. rhinoscleromatis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=39831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13884 / JCM 1664 / LMG 3184 / NCTC 5046 / R-70;
RX   PubMed=15215087; DOI=10.1128/aac.48.7.2400-2408.2004;
RA   Haeggman S., Loefdahl S., Paauw A., Verhoef J., Brisse S.;
RT   "Diversity and evolution of the class A chromosomal beta-lactamase gene in
RT   Klebsiella pneumoniae.";
RL   Antimicrob. Agents Chemother. 48:2400-2408(2004).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ635391; CAG25802.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1G5; -.
DR   SMR; P0C1G5; -.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           <1..>114
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000240201"
FT   BINDING         4
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         87..89
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   NON_TER         1
FT   NON_TER         114
SQ   SEQUENCE   114 AA;  11913 MW;  D63AEB7FD35062AE CRC64;
     SLYDIAPVTP GVAVDLSHIP TDVKIKGFSG EDATPALEGA DVVLISAGVA RKPGMDRSDL
     FNVNAGIVKN LVQQIAKTRP QACIGIITNP VNTTVAIAAE VLKKAGVYDK NKLF
//