ID   MDH_RHORU               Reviewed;          27 AA.
AC   P80459;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:Q25QU7};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:Q25QU7};
DE   Flags: Fragment;
GN   Name=mdh;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Naterstad K., Synstad B., Sirevag R.;
RL   Submitted (SEP-1996) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:Q25QU7}.
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:0000250|UniProtKB:Q25QU7};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000305}.
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DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IDA:CACAO.
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..>27
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113466"
FT   BINDING         9..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P80040"
FT   NON_TER         27
SQ   SEQUENCE   27 AA;  2668 MW;  3D1BBF0CAAD98FF0 CRC64;
     ADKKIALVGA GNIGGTLAHL IGLKXLL