MDH_ECOLI
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 03-AUG-2022, entry version 161.
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, ECO:0000303|PubMed:2993232};
GN OrderedLocusNames=b3236, JW3205;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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(+) = 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 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_STEB01000012.1.
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 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 AlphaFoldDB; P61889; -.
DR SMR; P61889; -.
DR BioGRID; 4260779; 27.
DR BioGRID; 852165; 2.
DR DIP; DIP-35924N; -.
DR IntAct; P61889; 10.
DR STRING; 511145.b3236; -.
DR SWISS-2DPAGE; P61889; -.
DR jPOST; P61889; -.
DR PaxDb; P61889; -.
DR PRIDE; P61889; -.
DR EnsemblBacteria; AAC76268; AAC76268; b3236.
DR EnsemblBacteria; BAE77279; BAE77279; BAE77279.
DR GeneID; 67415932; -.
DR GeneID; 947854; -.
DR KEGG; ecj:JW3205; -.
DR KEGG; eco:b3236; -.
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; MGWTSQA; -.
DR PhylomeDB; P61889; -.
DR BioCyc; EcoCyc:MALATE-DEHASE-MON; -.
DR BioCyc; MetaCyc:MALATE-DEHASE-MON; -.
DR BRENDA; 1.1.1.37; 2026.
DR SABIO-RK; P61889; -.
DR EvolutionaryTrace; P61889; -.
DR PRO; PR:P61889; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 activity; IBA:GO_Central.
DR GO; GO:0016615; F:malate dehydrogenase activity; IDA:EcoliWiki.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0009061; P:anaerobic respiration; IDA:EcoliWiki.
DR GO; GO:0006113; P:fermentation; 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 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 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: ECO R37)"
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 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 286..310
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
