MDH_PSEPG
ID MDH_PSEPG Reviewed; 309 AA.
AC B0KMD1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=PputGB1_0697;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABY96607.1; -; Genomic_DNA.
DR RefSeq; WP_012270412.1; NC_010322.1.
DR AlphaFoldDB; B0KMD1; -.
DR SMR; B0KMD1; -.
DR STRING; 76869.PputGB1_0697; -.
DR EnsemblBacteria; ABY96607; ABY96607; PputGB1_0697.
DR KEGG; ppg:PputGB1_0697; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_6; -.
DR OMA; ASCAEYI; -.
DR Proteomes; UP000002157; 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.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..309
FT /note="Malate dehydrogenase"
FT /id="PRO_1000191653"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ SEQUENCE 309 AA; 32718 MW; DB218AAD31586E46 CRC64;
MNKLTIVGAG LVGEAAAQII ARDELCRELV LMDVQGELAQ GKALDVWQAA VESGSDTRVY
GGAKAEMLDG SDLVVITAGV PRKPGQSRQD VLSINLPILD GIMTDIKHHA PAATVLVVSN
PVDVLTYRAW SVSGLGRDKV FGQAGVLDTA RMKCFIAEQT GFSAKDITAL VLGGHGDSMV
PLMRYCQIGS VPLSHFLSSE QIEQIVERTR KGGGEILGLK KMGSACDAPG VAIAQMVDAI
ANGRNRILPA VAILQGEYGR KDIAMGVPCV LADEGLARVI ELPLDAQEQA MFDQSADQVA
RDIDEMKAL
