MDH_SYNFM
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 03-AUG-2022, entry version 90.
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=Sfum_0460;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; 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 PRIDE; A0LFF8; -.
DR EnsemblBacteria; ABK16160; ABK16160; Sfum_0460.
DR KEGG; sfu:Sfum_0460; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_7; -.
DR OMA; TKGMERG; -.
DR OrthoDB; 870724at2; -.
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 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 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
