ID   MDH_METPP               Reviewed;         328 AA.
AC   A2SHT9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=Mpe_A2172;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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|HAMAP-Rule:MF_01517};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP000555; ABM95128.1; -; Genomic_DNA.
DR   RefSeq; WP_011829765.1; NC_008825.1.
DR   AlphaFoldDB; A2SHT9; -.
DR   SMR; A2SHT9; -.
DR   STRING; 420662.Mpe_A2172; -.
DR   EnsemblBacteria; ABM95128; ABM95128; Mpe_A2172.
DR   KEGG; mpt:Mpe_A2172; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_4; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 870724at2; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..328
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000294391"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         12..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         115
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         132..134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
SQ   SEQUENCE   328 AA;  34943 MW;  66D86E09AA1F2E4B CRC64;
     MSKKPVRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ KALKGVMMEL
     EDCAFPLLAG MEAHGDPMTA FKDADYALLV GSRPRGPGME RAELLSINGA IFTAQGKALN
     AVASRNVKVL VVGNPANTNA YIAMKAAPDL PRKNFTAMLR LDHNRAASQI AAKTGKPVSS
     IKQLAVWGNH SPTMYADYRF ATIDGASVKD MINDQVWNKD VFLPTVGKRG AAIIEARGLS
     SAASAANAAI DHMRDWALGT NGAWVTMGVP SNGEYGIPKD VMFGFPVTCA NGEYKIVDGL
     AIDAFSQECI NKTLAELQGE QDGVKHLI