ID   MDH_KLEOX               Reviewed;         223 AA.
AC   P61894;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
DE   Flags: Fragment;
GN   Name=mdh;
OS   Klebsiella oxytoca.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13182;
RX   PubMed=15053318; DOI=10.1078/0723-2020-00261;
RA   Rosenblueth M., Martinez L., Silva J., Martinez-Romero E.;
RT   "Klebsiella variicola, a novel species with clinical and plant-associated
RT   isolates.";
RL   Syst. Appl. Microbiol. 27:27-35(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; AY367380; AAQ72406.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61894; -.
DR   SMR; P61894; -.
DR   STRING; 571.AB185_09780; -.
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; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; 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:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           <1..>223
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113309"
FT   ACT_SITE        142
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         59
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         82..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         192
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         223
SQ   SEQUENCE   223 AA;  22855 MW;  D4175B9AEE52ACFB CRC64;
     APVTPGVAVD LSHIPTDVKI KGFSGEDATP ALEGADVVLI SAGVARKPGM DRSDLFNVNA
     GIVKNLVQQI AKTCPQACVG IITNPVNTTV AIAAEVLKKA GVYDKNKLFG VTTLDIIRSN
     TFVAELKGKS SSDVEVPVIG GHSGVTILPL LSQIPGVSFS EQEVADLTKR IQNAGTEVVE
     AKAGGGSATL SMGQAAARFG LSLVRAMQGE KGVVECAYVE GDG
//