MDH_SHESA
ID MDH_SHESA Reviewed; 311 AA.
AC A0L113;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01516};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01516};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01516};
GN OrderedLocusNames=Shewana3_3509;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_01516}.
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_01516};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01516}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01516}.
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DR EMBL; CP000469; ABK49732.1; -; Genomic_DNA.
DR RefSeq; WP_011718296.1; NC_008577.1.
DR AlphaFoldDB; A0L113; -.
DR SMR; A0L113; -.
DR STRING; 94122.Shewana3_3509; -.
DR EnsemblBacteria; ABK49732; ABK49732; Shewana3_3509.
DR KEGG; shn:Shewana3_3509; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_047181_0_1_6; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 870724at2; -.
DR Proteomes; UP000002589; 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; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR023958; Malate_DH_type1_bac.
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 SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..311
FT /note="Malate dehydrogenase"
FT /id="PRO_0000294304"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516"
SQ SEQUENCE 311 AA; 32149 MW; 7EAF5B6FC2A7E738 CRC64;
MKVAVLGAAG GIGQALALLL KTQLPAGSKL SLYDIAPVTP GVAVDLSHIP TAVEIKGFAG
EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNINAGIVRN LIEKVAVTCP KALVGIITNP
VNTTVAIAAE VLKKAGVYDK NRLFGVTTLD VIRSETFIAE LKGLNVADVK VNVIGGHSGV
TILPLLSQVE GVTFSDEEVA SLTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGMSLVR
GLQGEANIVE CAYVDGGSEH AEFFAQPVLL GKNGIEKVLP YGEVSAFEAN ARDSMLDTLK
GDIKLGVDFV K