ID   MDH_ACIDE               Reviewed;          17 AA.
AC   P80540;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   13-SEP-2023, entry version 58.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
DE   Flags: Fragment;
GN   Name=mdh;
OS   Acidovorax delafieldii (Pseudomonas delafieldii).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=47920;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=CCUG 12929 / LMG 7167;
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   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..>17
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113344"
FT   BINDING         11..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   NON_TER         17
SQ   SEQUENCE   17 AA;  1663 MW;  110E8111A516909E CRC64;
     XKKPVRVAVT GAAGQIG
//