ID   MDH_SYNFM               Reviewed;         329 AA.
AC   A0LFF8; P80648;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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};
GN   OrderedLocusNames=Sfum_0460;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=8900056; DOI=10.1111/j.1574-6968.1996.tb08520.x;
RA   van Kuijk B.L.M., Stams A.J.M.;
RT   "Purification and characterization of malate dehydrogenase from the
RT   syntrophic propionate-oxidizing bacterium strain MPOB.";
RL   FEMS Microbiol. Lett. 144:141-144(1996).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       Catalyzes the reduction of oxaloacetate more efficiently than the
CC       oxidation of malate. {ECO:0000269|PubMed:8900056}.
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         ECO:0000269|PubMed:8900056};
CC   -!- ACTIVITY REGULATION: Substrate inhibition is observed at high
CC       concentrations of oxaloacetate. {ECO:0000269|PubMed:8900056}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=50 uM for oxaloacetate (at 37 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:8900056};
CC         KM=30 uM for NADH (at 37 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:8900056};
CC         KM=4 mM for L-malate (at 37 degrees Celsius and pH 9.0)
CC         {ECO:0000269|PubMed:8900056};
CC         KM=1.1 mM for NAD (at 37 degrees Celsius and pH 9.0)
CC         {ECO:0000269|PubMed:8900056};
CC       pH dependence:
CC         Optimum pH is 8.5 with oxaloacetate as substrate.
CC         {ECO:0000269|PubMed:8900056};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius with oxaloacetate as
CC         substrate. {ECO:0000269|PubMed:8900056};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8900056}.
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; CP000478; ABK16160.1; -; Genomic_DNA.
DR   RefSeq; WP_011697333.1; NC_008554.1.
DR   AlphaFoldDB; A0LFF8; -.
DR   SMR; A0LFF8; -.
DR   STRING; 335543.Sfum_0460; -.
DR   KEGG; sfu:Sfum_0460; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_7; -.
DR   InParanoid; A0LFF8; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000001784; 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   CDD; cd01338; MDH_choloroplast_like; 1.
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   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   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8900056"
FT   CHAIN           2..329
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000292376"
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   329 AA;  35690 MW;  1BE66E683446BE07 CRC64;
     MAKKPVRVTV TGAAGQIGYA LLFRVASGQM LGPDQPIILQ MLELPIDKVQ AALKGVMMEL
     EDCAFPLLAD MIGTGDPKVA FKDSDYALLV GARPRGPGME RKDLLLENAK IFIEQGKAMN
     AVASRDIRVI VVGNPANTNA WIAMKSAPDL PKGNFTAMLR LDHNRAKSQL ATRTGKPVAS
     VEKMIVWGNH SPTMYPDIRF CTVDGQPAVK LVNDEAWYRN EYIPKVGKRG AAIIEARGLS
     SAASAANAAI DHMHDWALGT NGKWVTMGLP SDGSYGIPEG TMYGVPVTCT PGKYERVKGL
     EIDAFSREKM DFTLKELTEE QAGVKEMVK
//