ID   MDH_ECOLI               Reviewed;         312 AA.
AC   P61889; O30401; O30402; O30403; P06994; Q2M8X7; Q59343; Q59344; Q59345;
AC   Q59346; Q59347; Q59348; Q60133; Q60150; Q933J3; Q93R02; Q9FDQ3; Q9FDQ4;
AC   Q9FDQ5;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   02-SEP-2026, entry version 178.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000303|PubMed:7028159};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000269|PubMed:2993232, ECO:0000269|PubMed:7028159};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01516,
GN   ECO:0000303|PubMed:2993232}; OrderedLocusNames=b3236, JW3205;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3299262; DOI=10.1093/nar/15.12.4993;
RA   McAlister-Henn L., Blaber M., Bradshaw R.A., Nisco S.J.;
RT   "Complete nucleotide sequence of the Escherichia coli gene encoding malate
RT   dehydrogenase.";
RL   Nucleic Acids Res. 15:4993-4993(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3322223; DOI=10.1007/bf00423133;
RA   Vogel R.F., Entian K.-D., Mecke D.;
RT   "Cloning and sequence of the mdh structural gene of Escherichia coli coding
RT   for malate dehydrogenase.";
RL   Arch. Microbiol. 149:36-42(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=2993232; DOI=10.1128/jb.163.3.1074-1079.1985;
RA   Sutherland P., McAlister-Henn L.;
RT   "Isolation and expression of the Escherichia coli gene encoding malate
RT   dehydrogenase.";
RL   J. Bacteriol. 163:1074-1079(1985).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-36, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=7028159; DOI=10.1007/bf01121583;
RA   Fernley R.T., Lentz S.R., Bradshaw R.A.;
RT   "Malate dehydrogenase: isolation from E. coli and comparison with the
RT   eukaryotic mitochondrial and cytoplasmic forms.";
RL   Biosci. Rep. 1:497-507(1981).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-26.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   PROTEIN SEQUENCE OF 1-26.
RX   PubMed=9190829; DOI=10.1128/jb.179.12.4066-4070.1997;
RA   Charnock C.;
RT   "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas
RT   species are the first reported MDHs in Proteobacteria which resemble
RT   lactate dehydrogenases in primary structure.";
RL   J. Bacteriol. 179:4066-4070(1997).
RN   [9]
RP   PROTEIN SEQUENCE OF 1-16.
RX   PubMed=8506346; DOI=10.1073/pnas.90.11.5011;
RA   Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.;
RT   "Identifying proteins from two-dimensional gels by molecular mass searching
RT   of peptide fragments in protein sequence databases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993).
RN   [10]
RP   PROTEIN SEQUENCE OF 1-13.
RX   PubMed=8670822; DOI=10.1002/j.1460-2075.1996.tb00686.x;
RA   Nystroem T., Larsson C., Gustafsson L.;
RT   "Bacterial defense against aging: role of the Escherichia coli ArcA
RT   regulator in gene expression, readjusted energy flux and survival during
RT   stasis.";
RL   EMBO J. 15:3219-3228(1996).
RN   [11]
RP   PROTEIN SEQUENCE OF 1-11.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL   Submitted (FEB-1996) to UniProtKB.
RN   [12]
RP   PROTEIN SEQUENCE OF 1-4.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA   Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA   Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA   Hochstrasser D.F.;
RT   "Protein identification with N and C-terminal sequence tags in proteome
RT   projects.";
RL   J. Mol. Biol. 278:599-608(1998).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
RC   STRAIN=Various strains;
RX   PubMed=8108402; DOI=10.1073/pnas.91.4.1280;
RA   Boyd E.F., Nelson K., Wang F.-S., Whittam T.S., Selander R.K.;
RT   "Molecular genetic basis of allelic polymorphism in malate dehydrogenase
RT   (mdh) in natural populations of Escherichia coli and Salmonella enterica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1280-1284(1994).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
RC   STRAIN=Various strains;
RX   PubMed=9199437; DOI=10.1128/iai.65.7.2685-2692.1997;
RA   Pupo G.M., Karaolis D.K., Lan R., Reeves P.R.;
RT   "Evolutionary relationships among pathogenic and nonpathogenic Escherichia
RT   coli strains inferred from multilocus enzyme electrophoresis and mdh
RT   sequence studies.";
RL   Infect. Immun. 65:2685-2692(1997).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
RC   STRAIN=Various strains;
RX   PubMed=11214793; DOI=10.1046/j.1462-2920.2000.00142.x;
RA   Pupo G.M., Lan R., Reeves P.R., Baverstock P.R.;
RT   "Population genetics of Escherichia coli in a natural population of native
RT   Australian rats.";
RL   Environ. Microbiol. 2:594-610(2000).
RN   [16]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [17] {ECO:0007744|PDB:2CMD}
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP   AND SUBUNIT.
RX   PubMed=1507230; DOI=10.1016/0022-2836(92)90637-y;
RA   Hall M.D., Levitt D.G., Banaszak L.J.;
RT   "Crystal structure of Escherichia coli malate dehydrogenase. A complex of
RT   the apoenzyme and citrate at 1.87-A resolution.";
RL   J. Mol. Biol. 226:867-882(1992).
RN   [18] {ECO:0007744|PDB:1EMD}
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP   ANALOG, AND SUBUNIT.
RX   PubMed=8331658; DOI=10.1006/jmbi.1993.1377;
RA   Hall M.D., Banaszak L.J.;
RT   "Crystal structure of a ternary complex of Escherichia coli malate
RT   dehydrogenase citrate and NAD at 1.9 A resolution.";
RL   J. Mol. Biol. 232:213-222(1993).
RN   [19] {ECO:0007744|PDB:1IB6, ECO:0007744|PDB:1IE3}
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP   ANALOG, SUBUNIT, MUTAGENESIS OF ARG-153, AND ACTIVE SITE.
RX   PubMed=11389141; DOI=10.1074/jbc.m100902200;
RA   Bell J.K., Yennawar H.P., Wright S.K., Thompson J.R., Viola R.E.,
RA   Banaszak L.J.;
RT   "Structural analyses of a malate dehydrogenase with a variable active
RT   site.";
RL   J. Biol. Chem. 276:31156-31162(2001).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000269|PubMed:2993232,
CC       ECO:0000269|PubMed:7028159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = oxaloacetate + NADH + H(+);
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         ECO:0000269|PubMed:2993232, ECO:0000269|PubMed:7028159};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01516,
CC       ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:1507230,
CC       ECO:0000269|PubMed:7028159, ECO:0000269|PubMed:8331658}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000305}.
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DR   EMBL; Y00129; CAA68326.1; -; Genomic_DNA.
DR   EMBL; M24777; AAA16107.1; -; Unassigned_DNA.
DR   EMBL; U18997; AAA58038.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76268.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77279.1; -; Genomic_DNA.
DR   EMBL; M10417; AAA24147.1; -; Genomic_DNA.
DR   EMBL; U04742; AAC43730.1; -; Genomic_DNA.
DR   EMBL; U04743; AAC43731.1; -; Genomic_DNA.
DR   EMBL; U04744; AAC43732.1; -; Genomic_DNA.
DR   EMBL; U04745; AAC43733.1; -; Genomic_DNA.
DR   EMBL; U04746; AAC43734.1; -; Genomic_DNA.
DR   EMBL; U04747; AAC43735.1; -; Genomic_DNA.
DR   EMBL; U04748; AAC43736.1; -; Genomic_DNA.
DR   EMBL; U04749; AAC43737.1; -; Genomic_DNA.
DR   EMBL; U04750; AAC43738.1; -; Genomic_DNA.
DR   EMBL; U04751; AAC43739.1; -; Genomic_DNA.
DR   EMBL; U04752; AAC43740.1; -; Genomic_DNA.
DR   EMBL; U04753; AAC43741.1; -; Genomic_DNA.
DR   EMBL; U04754; AAC43742.1; -; Genomic_DNA.
DR   EMBL; U04755; AAC43743.1; -; Genomic_DNA.
DR   EMBL; U04756; AAC43744.1; -; Genomic_DNA.
DR   EMBL; U04757; AAC43745.1; -; Genomic_DNA.
DR   EMBL; U04758; AAC43746.1; -; Genomic_DNA.
DR   EMBL; U04759; AAC43747.1; -; Genomic_DNA.
DR   EMBL; U04760; AAC43748.1; -; Genomic_DNA.
DR   EMBL; U04770; AAC43758.1; -; Genomic_DNA.
DR   EMBL; AF004170; AAB87003.1; -; Genomic_DNA.
DR   EMBL; AF004171; AAB87004.1; -; Genomic_DNA.
DR   EMBL; AF004172; AAB87005.1; -; Genomic_DNA.
DR   EMBL; AF004173; AAB87006.1; -; Genomic_DNA.
DR   EMBL; AF004174; AAB87007.1; -; Genomic_DNA.
DR   EMBL; AF004175; AAB87008.1; -; Genomic_DNA.
DR   EMBL; AF004176; AAB87009.1; -; Genomic_DNA.
DR   EMBL; AF004177; AAB87010.1; -; Genomic_DNA.
DR   EMBL; AF004179; AAB87012.1; -; Genomic_DNA.
DR   EMBL; AF004180; AAB87013.1; -; Genomic_DNA.
DR   EMBL; AF004182; AAB87015.1; -; Genomic_DNA.
DR   EMBL; AF004183; AAB87016.1; -; Genomic_DNA.
DR   EMBL; AF004184; AAB87017.1; -; Genomic_DNA.
DR   EMBL; AF004186; AAB87019.1; -; Genomic_DNA.
DR   EMBL; AF004187; AAB87020.1; -; Genomic_DNA.
DR   EMBL; AF004188; AAB87021.1; -; Genomic_DNA.
DR   EMBL; AF004190; AAB87023.1; -; Genomic_DNA.
DR   EMBL; AF004191; AAB87024.1; -; Genomic_DNA.
DR   EMBL; AF004195; AAB87028.1; -; Genomic_DNA.
DR   EMBL; AF004196; AAB87029.1; -; Genomic_DNA.
DR   EMBL; AF004199; AAB87032.1; -; Genomic_DNA.
DR   EMBL; AF004200; AAB87033.1; -; Genomic_DNA.
DR   EMBL; AF004201; AAB87034.1; -; Genomic_DNA.
DR   EMBL; AF004202; AAB87035.1; -; Genomic_DNA.
DR   EMBL; AF004203; AAB87036.1; -; Genomic_DNA.
DR   EMBL; AF004204; AAB87037.1; -; Genomic_DNA.
DR   EMBL; AF004205; AAB87038.1; -; Genomic_DNA.
DR   EMBL; AF004206; AAB87039.1; -; Genomic_DNA.
DR   EMBL; AF004207; AAB87040.1; -; Genomic_DNA.
DR   EMBL; AF004208; AAB87041.1; -; Genomic_DNA.
DR   EMBL; AF004209; AAB87042.1; -; Genomic_DNA.
DR   EMBL; AF091758; AAF97988.1; -; Genomic_DNA.
DR   EMBL; AF091759; AAF97989.1; -; Genomic_DNA.
DR   EMBL; AF091760; AAF97990.1; -; Genomic_DNA.
DR   EMBL; AF091761; AAF97991.1; -; Genomic_DNA.
DR   EMBL; AF091762; AAF97992.1; -; Genomic_DNA.
DR   EMBL; AF091763; AAF97993.1; -; Genomic_DNA.
DR   EMBL; AF091764; AAF97994.1; -; Genomic_DNA.
DR   EMBL; AF091765; AAF97995.1; -; Genomic_DNA.
DR   EMBL; AF091766; AAF97996.1; -; Genomic_DNA.
DR   EMBL; AF091767; AAF97997.1; -; Genomic_DNA.
DR   EMBL; AF091768; AAF97998.1; -; Genomic_DNA.
DR   EMBL; AF091769; AAF97999.1; -; Genomic_DNA.
DR   EMBL; AF091770; AAF98000.1; -; Genomic_DNA.
DR   EMBL; AF091771; AAF98001.1; -; Genomic_DNA.
DR   EMBL; AF091772; AAF98002.1; -; Genomic_DNA.
DR   EMBL; AF091773; AAF98003.1; -; Genomic_DNA.
DR   EMBL; AF091774; AAF98004.1; -; Genomic_DNA.
DR   EMBL; AF091775; AAF98005.1; -; Genomic_DNA.
DR   EMBL; AF091776; AAF98006.1; -; Genomic_DNA.
DR   EMBL; AF091777; AAF98007.1; -; Genomic_DNA.
DR   EMBL; AF091778; AAF98008.1; -; Genomic_DNA.
DR   PIR; F65115; DEECM.
DR   RefSeq; NP_417703.1; NC_000913.3.
DR   RefSeq; WP_001295272.1; NZ_CP009789.1.
DR   PDB; 1EMD; X-ray; 1.90 A; A=1-312.
DR   PDB; 1IB6; X-ray; 2.10 A; A/B/C/D=1-312.
DR   PDB; 1IE3; X-ray; 2.50 A; A/B/C/D=1-312.
DR   PDB; 2CMD; X-ray; 1.87 A; A=1-312.
DR   PDB; 2PWZ; X-ray; 2.20 A; A/C/E/G=1-312.
DR   PDB; 3HHP; X-ray; 1.45 A; A/B/C/D=1-312.
DR   PDB; 5KKA; X-ray; 1.75 A; A/B=1-312.
DR   PDB; 5Z3W; X-ray; 2.29 A; A/B/C/D=1-311.
DR   PDB; 6KA0; X-ray; 2.22 A; A/B/C/D=1-312.
DR   PDB; 6KA1; X-ray; 1.54 A; A/B/C/D=1-311.
DR   PDB; 7CGC; X-ray; 2.55 A; A/B/C/D=1-312.
DR   PDB; 7CGD; X-ray; 2.06 A; A/B/C/D=1-312.
DR   PDB; 7XQN; X-ray; 1.98 A; A/B=1-312.
DR   PDB; 9WXS; X-ray; 1.56 A; A/B/C/D=1-312.
DR   AlphaFoldDB; P61889; -.
DR   SMR; P61889; -.
DR   BioGRID; 4260779; 31.
DR   BioGRID; 852165; 2.
DR   DIP; DIP-35924N; -.
DR   FunCoup; P61889; 824.
DR   IntAct; P61889; 10.
DR   STRING; 511145.b3236; -.
DR   jPOST; P61889; -.
DR   PaxDb; 511145-b3236; -.
DR   EnsemblBacteria; AAC76268; AAC76268; b3236.
DR   GeneID; 67174160; -.
DR   GeneID; 93778749; -.
DR   GeneID; 947854; -.
DR   KEGG; ecj:JW3205; -.
DR   KEGG; eco:b3236; -.
DR   KEGG; ecoc:C3026_17605; -.
DR   PATRIC; fig|1411691.4.peg.3492; -.
DR   EchoBASE; EB0571; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_047181_0_1_6; -.
DR   InParanoid; P61889; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 9802969at2; -.
DR   PhylomeDB; P61889; -.
DR   BioCyc; EcoCyc:MALATE-DEHASE-MONOMER; -.
DR   BioCyc; MetaCyc:MALATE-DEHASE-MONOMER; -.
DR   BRENDA; 1.1.1.37; 2026.
DR   SABIO-RK; P61889; -.
DR   EvolutionaryTrace; P61889; -.
DR   PRO; PR:P61889; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P61889; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0019898; C:extrinsic component of membrane; IDA:EcoliWiki.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030060; F:L-malate dehydrogenase (NAD+) activity; EXP:UniProtKB.
DR   GO; GO:0016615; F:malate dehydrogenase activity; IDA:EcoliWiki.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0009061; P:anaerobic respiration; IDA:EcoliWiki.
DR   GO; GO:0006096; P:glycolytic process; IDA:EcoliWiki.
DR   GO; GO:0006108; P:malate metabolic process; IDA:EcoliWiki.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IDA:EcoliWiki.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   FunFam; 3.40.50.720:FF:000017; Malate dehydrogenase; 1.
DR   FunFam; 3.90.110.10:FF:000001; Malate dehydrogenase; 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.
DR   PDBsum; 1EMD; -.
DR   PDBsum; 1IB6; -.
DR   PDBsum; 1IE3; -.
DR   PDBsum; 2CMD; -.
DR   PDBsum; 2PWZ; -.
DR   PDBsum; 3HHP; -.
DR   PDBsum; 5KKA; -.
DR   PDBsum; 5Z3W; -.
DR   PDBsum; 6KA0; -.
DR   PDBsum; 6KA1; -.
DR   PDBsum; 7CGC; -.
DR   PDBsum; 7CGD; -.
DR   PDBsum; 7XQN; -.
DR   PDBsum; 9WXS; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..312
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113301"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000305|PubMed:11389141"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:8331658"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:8331658"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000305|PubMed:1507230, ECO:0000305|PubMed:8331658"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000305|PubMed:1507230, ECO:0000305|PubMed:8331658"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:8331658"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:8331658"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000305|PubMed:1507230, ECO:0000305|PubMed:8331658"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000305|PubMed:1507230, ECO:0000305|PubMed:8331658"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01516,
FT                   ECO:0000269|PubMed:11389141, ECO:0000269|PubMed:8331658"
FT   VARIANT         71
FT                   /note="D -> N (in strain: EC47, EC49, EC50 and RT272)"
FT   VARIANT         106
FT                   /note="A -> S (in strain: ECOR 27 and RT082)"
FT   VARIANT         209
FT                   /note="A -> P (in strain: MB001D)"
FT   VARIANT         218
FT                   /note="A -> R (in strain: A8190, E2666-74, E830587,
FT                   E851819, E3406, EC10, EC14, EC32, EC35, EC38, EC40, EC44,
FT                   EC46, EC47, EC49, EC50, EC52, EC58, E64 and EC70)"
FT   VARIANT         232
FT                   /note="A -> T (in strain: ECOR37)"
FT   VARIANT         249
FT                   /note="V -> I (in strain: RT083)"
FT   VARIANT         289
FT                   /note="Q -> K (in strain: EC35, EC38, EC40, EC44, EC46,
FT                   EC47 and RT272)"
FT   VARIANT         290
FT                   /note="N -> S (in strain: E2666-74, ECOR 27, ECOR 45,
FT                   RL012A, RT104 and RT174)"
FT   VARIANT         291
FT                   /note="A -> S (in strain: EC35)"
FT   VARIANT         294
FT                   /note="G -> A (in strain: ECOR 45)"
FT   VARIANT         297
FT                   /note="D -> N (in strain: E830587)"
FT   MUTAGEN         153
FT                   /note="R->C: Loss of interaction with substrate."
FT                   /evidence="ECO:0000269|PubMed:11389141"
FT   CONFLICT        37
FT                   /note="P -> S (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="A -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="A -> R (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="I -> N (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="F -> L (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305..312
FT                   /note="LGEEFVNK -> WAKSSLISN (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="E -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   TURN            7..9
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           11..23
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           39..47
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          51..58
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:6KA1"
FT   HELIX           87..108
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          112..116
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:2CMD"
FT   HELIX           121..134
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           148..162
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           209..216
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           225..242
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          249..255
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          262..271
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:3HHP"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:2CMD"
FT   HELIX           286..311
FT                   /evidence="ECO:0007829|PDB:3HHP"
SQ   SEQUENCE   312 AA;  32337 MW;  17741A3B5AD068BA CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG
     EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQVAKTCP KACIGIITNP
     VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV
     TILPLLSQVP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
     ALQGEQGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK
     KDIALGEEFV NK
//