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Database: UniProt
Entry: E0SKW1_DICD3
LinkDB: E0SKW1_DICD3
Original site: E0SKW1_DICD3 
ID   E0SKW1_DICD3            Unreviewed;       313 AA.
AC   E0SKW1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01516};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01516};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01516,
GN   ECO:0000313|EMBL:ADM96824.1};
GN   OrderedLocusNames=Dda3937_03529 {ECO:0000313|EMBL:ADM96824.1};
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM96824.1, ECO:0000313|Proteomes:UP000006859};
RN   [1] {ECO:0000313|EMBL:ADM96824.1, ECO:0000313|Proteomes:UP000006859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937 {ECO:0000313|EMBL:ADM96824.1,
RC   ECO:0000313|Proteomes:UP000006859};
RX   PubMed=21217001; DOI=10.1128/JB.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|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:0000256|ARBA:ARBA00000774, ECO:0000256|HAMAP-
CC         Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01516}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824, ECO:0000256|HAMAP-Rule:MF_01516}.
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DR   EMBL; CP002038; ADM96824.1; -; Genomic_DNA.
DR   RefSeq; WP_013316303.1; NC_014500.1.
DR   AlphaFoldDB; E0SKW1; -.
DR   STRING; 198628.Dda3937_03529; -.
DR   GeneID; 9732017; -.
DR   KEGG; ddd:Dda3937_03529; -.
DR   PATRIC; fig|198628.6.peg.628; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_047181_1_0_6; -.
DR   OMA; MGWTSQA; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000006859; 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; 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_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   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01516}; Reference proteome {ECO:0000313|Proteomes:UP000006859};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_01516}.
FT   DOMAIN          1..145
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          147..310
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   313 AA;  32473 MW;  8B90BC32EE25968B CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TDVKIKGFSG
     EDATPALEGA DIVLMSAGVA RKPGMDRSDL FNVNAGIVRN LVSQIARTCP NACIGIITNP
     VNTTVAIAAE VLKQAGVYNK DKLFGVTTLD IIRSSTFVAE LKGKQPQAID VPVIGGHSGV
     TILPLLSQIP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
     ALQGESGVVE CAYVEGDGKH ARFFAQPLLL GKNGVAERKD IGTLSAFEQQ SLVSMLDTLK
     QDIALGEEFV NKK
//
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