MDH_DESRM
ID MDH_DESRM Reviewed; 308 AA.
AC A4J5N8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487}; OrderedLocusNames=Dred_1867;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
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., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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_00487};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR EMBL; CP000612; ABO50391.1; -; Genomic_DNA.
DR RefSeq; WP_011878203.1; NC_009253.1.
DR AlphaFoldDB; A4J5N8; -.
DR SMR; A4J5N8; -.
DR STRING; 349161.Dred_1867; -.
DR EnsemblBacteria; ABO50391; ABO50391; Dred_1867.
DR KEGG; drm:Dred_1867; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_9; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 870724at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd01339; LDH-like_MDH; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..308
FT /note="Malate dehydrogenase"
FT /id="PRO_1000072418"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 119..121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ SEQUENCE 308 AA; 33015 MW; 34F412B8F2B8A7F1 CRC64;
MKRKKITIVG AGNVGATCAH WAAAKELGDI VLIDVAEGIP QGKALDLMEA APVEGYDSVI
IGTNDYADTA DSDVVVITAG VARKPGMSRD DLLNINAGIV RKVTEEIVKY SPNAYLLIVT
NPVDVSAYIA YKASGFSANR VFGLSGVLDS ARFRTFIARE LNVSFEDVIS FVLGGHGDDM
VPMVRYTYVG GIPVEKLIPT DRLEAMVERA RKGGAEIVNY LKTGSAYYAP SASVMQMAEC
ILKDKKRILP VSAFLQGEYG ESDVFSGVPA IIGGDGVEKI IELDLDDEEM AALRKSINSV
RNNISKLG
