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Dihydrofolate reductase (EC 1.5.1.3)

 DYR_ECOLI               Reviewed;         159 AA.
P0ABQ4; P00379;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 117.
RecName: Full=Dihydrofolate reductase;
EC=1.5.1.3;
Name=folA; Synonyms=tmrA; OrderedLocusNames=b0048, JW0047;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PROTEIN SEQUENCE (ISOZYME 1).
STRAIN=B [RT500];
PubMed=320005; DOI=10.1111/j.1432-1033.1977.tb11284.x;
Stone D., Phillips A.W., Burchall J.J.;
"The amino-acid sequence of the dihydrofolate reductase of a
trimethoprim-resistant strain of Escherichia coli.";
Eur. J. Biochem. 72:613-624(1977).
[2]
PROTEIN SEQUENCE.
STRAIN=B [MB1428];
PubMed=350268; DOI=10.1021/bi00600a030;
Bennett C.D., Rodkey J.A., Sondey J.M., Hirschmann R.;
"Dihydrofolate reductase: the amino acid sequence of the enzyme from a
methotrexate-resistant mutant of Escherichia coli.";
Biochemistry 17:1328-1337(1978).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6159575; DOI=10.1093/nar/8.10.2255;
Smith D.R., Calvo J.M.;
"Nucleotide sequence of the E coli gene coding for dihydrofolate
reductase.";
Nucleic Acids Res. 8:2255-2274(1980).
[4]
PROTEIN SEQUENCE (ISOZYME 2).
STRAIN=B [RT500];
PubMed=7007370;
Baccanari D.P., Stone D., Kuyper L.;
"Effect of a single amino acid substitution on Escherichia coli
dihydrofolate reductase catalysis and ligand binding.";
J. Biol. Chem. 256:1738-1747(1981).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1810;
PubMed=3549289; DOI=10.1111/j.1432-1033.1987.tb10664.x;
Flensburg J., Skoeld O.;
"Massive overproduction of dihydrofolate reductase in bacteria as a
response to the use of trimethoprim.";
Eur. J. Biochem. 162:473-476(1987).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
PubMed=1630901; DOI=10.1093/nar/20.13.3305;
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[9]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=6815179;
Filman D.J., Bolin J.T., Matthews D.A., Kraut J.;
"Crystal structures of Escherichia coli and Lactobacillus casei
dihydrofolate reductase refined at 1.7-A resolution. II. Environment
of bound NADPH and implications for catalysis.";
J. Biol. Chem. 257:13663-13672(1982).
[11]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=2185835; DOI=10.1021/bi00465a018;
Bystroff C., Oatley S.J., Kraut J.;
"Crystal structures of Escherichia coli dihydrofolate reductase: the
NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate
binding and a model for the transition state.";
Biochemistry 29:3263-3277(1990).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=1998681; DOI=10.1021/bi00222a028;
Bystroff C., Kraut J.;
"Crystal structure of unliganded Escherichia coli dihydrofolate
reductase. Ligand-induced conformational changes and cooperativity in
binding.";
Biochemistry 30:2227-2239(1991).
[13]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH NADPH;
FOLATE; 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE.
PubMed=7873554; DOI=10.1021/bi00008a039;
Reyes V.M., Sawaya M.R., Brown K.A., Kraut J.;
"Isomorphous crystal structures of Escherichia coli dihydrofolate
reductase complexed with folate, 5-deazafolate, and 5,10-
dideazatetrahydrofolate: mechanistic implications.";
Biochemistry 34:2710-2723(1995).
[14]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH
5-FORMYLTETRAHYDROFOLATE.
PubMed=8679526; DOI=10.1021/bi960028g;
Lee H., Reyes V.M., Kraut J.;
"Crystal structures of Escherichia coli dihydrofolate reductase
complexed with 5-formyltetrahydrofolate (folinic acid) in two space
groups: evidence for enolization of pteridine O4.";
Biochemistry 35:7012-7020(1996).
[15]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH NADPH;
METHOTREXATE AND TETRAHYDROFOLATE.
PubMed=9012674; DOI=10.1021/bi962337c;
Sawaya M.R., Kraut J.;
"Loop and subdomain movements in the mechanism of Escherichia coli
dihydrofolate reductase: crystallographic evidence.";
Biochemistry 36:586-603(1997).
[16]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FOLATE,
CATALYTIC ACTIVITY, MUTAGENESIS OF MET-16; MET-20; MET-42; CYS-85;
MET-92 AND CYS-152, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16510443; DOI=10.1074/jbc.M508823200;
Iwakura M., Maki K., Takahashi H., Takenawa T., Yokota A.,
Katayanagi K., Kamiyama T., Gekko K.;
"Evolutional design of a hyperactive cysteine- and methionine-free
mutant of Escherichia coli dihydrofolate reductase.";
J. Biol. Chem. 281:13234-13246(2006).
[17]
X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
PubMed=17125251; DOI=10.1021/jm060570v;
Summerfield R.L., Daigle D.M., Mayer S., Mallik D., Hughes D.W.,
Jackson S.G., Sulek M., Organ M.G., Brown E.D., Junop M.S.;
"A 2.13 A structure of E. coli dihydrofolate reductase bound to a
novel competitive inhibitor reveals a new binding surface involving
the M20 loop region.";
J. Med. Chem. 49:6977-6986(2006).
[18]
STRUCTURE BY NEUTRON DIFFRACTION (2.20 ANGSTROMS) IN COMPLEX WITH
METHOTREXATE.
PubMed=17130456; DOI=10.1073/pnas.0604977103;
Bennett B., Langan P., Coates L., Mustyakimov M., Schoenborn B.,
Howell E.E., Dealwis C.;
"Neutron diffraction studies of Escherichia coli dihydrofolate
reductase complexed with methotrexate.";
Proc. Natl. Acad. Sci. U.S.A. 103:18493-18498(2006).
[19]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH METHOTREXATE
AND NADPH.
PubMed=19374017; DOI=10.1016/j.jsb.2009.01.001;
Bennett B.C., Wan Q., Ahmad M.F., Langan P., Dealwis C.G.;
"X-ray structure of the ternary MTX.NADPH complex of the anthrax
dihydrofolate reductase: a pharmacophore for dual-site inhibitor
design.";
J. Struct. Biol. 166:162-171(2009).
-!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
reaction for de novo glycine and purine synthesis, and for DNA
precursor synthesis.
-!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
dihydrofolate + NADPH. {ECO:0000255|PROSITE-ProRule:PRU00660,
ECO:0000269|PubMed:16510443}.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
-!- INTERACTION:
P77609:flxA; NbExp=4; IntAct=EBI-550404, EBI-553024;
-!- MISCELLANEOUS: The strain K12 sequence is shown.
-!- MISCELLANEOUS: Strain B [RT500] is resistant to 500 micrograms per
milliliter of trimethoprim.
-!- MISCELLANEOUS: Strain B [MB1428] is methotrexate-resistant.
-!- SIMILARITY: Belongs to the dihydrofolate reductase family.
{ECO:0000305}.
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EMBL; J01609; AAA87976.1; -; Genomic_DNA.
EMBL; X05108; CAA28755.1; -; Genomic_DNA.
EMBL; U00096; AAC73159.1; -; Genomic_DNA.
EMBL; AP009048; BAB96616.1; -; Genomic_DNA.
PIR; A93704; RDECD.
RefSeq; NP_414590.1; NC_000913.3.
RefSeq; WP_000624375.1; NZ_LN832404.1.
PDB; 1DDR; X-ray; 2.45 A; A/B=1-159.
PDB; 1DDS; X-ray; 2.20 A; A/B=1-159.
PDB; 1DHI; X-ray; 1.90 A; A/B=1-159.
PDB; 1DHJ; X-ray; 1.80 A; A/B=1-159.
PDB; 1DRA; X-ray; 1.90 A; A/B=1-159.
PDB; 1DRB; X-ray; 1.96 A; A/B=1-159.
PDB; 1DRE; X-ray; 2.60 A; A=1-159.
PDB; 1DRH; X-ray; 2.30 A; A=1-159.
PDB; 1DYH; X-ray; 1.90 A; A/B=1-159.
PDB; 1DYI; X-ray; 1.90 A; A/B=1-159.
PDB; 1DYJ; X-ray; 1.85 A; A/B=1-159.
PDB; 1JOL; X-ray; 1.96 A; A/B=1-159.
PDB; 1JOM; X-ray; 1.90 A; A=1-159.
PDB; 1RA1; X-ray; 1.90 A; A=1-159.
PDB; 1RA2; X-ray; 1.60 A; A=1-159.
PDB; 1RA3; X-ray; 1.80 A; A=1-159.
PDB; 1RA8; X-ray; 1.80 A; A=1-159.
PDB; 1RA9; X-ray; 1.55 A; A=1-159.
PDB; 1RB2; X-ray; 2.10 A; A/B=1-159.
PDB; 1RB3; X-ray; 2.30 A; A/B=1-159.
PDB; 1RC4; X-ray; 1.90 A; A=1-159.
PDB; 1RD7; X-ray; 2.60 A; A/B=1-159.
PDB; 1RE7; X-ray; 2.60 A; A/B=1-159.
PDB; 1RF7; X-ray; 1.80 A; A=1-159.
PDB; 1RG7; X-ray; 2.00 A; A=1-159.
PDB; 1RH3; X-ray; 2.40 A; A=1-159.
PDB; 1RX1; X-ray; 2.00 A; A=1-159.
PDB; 1RX2; X-ray; 1.80 A; A=1-159.
PDB; 1RX3; X-ray; 2.20 A; A=1-159.
PDB; 1RX4; X-ray; 2.20 A; A=1-159.
PDB; 1RX5; X-ray; 2.30 A; A=1-159.
PDB; 1RX6; X-ray; 2.00 A; A=1-159.
PDB; 1RX7; X-ray; 2.30 A; A=1-159.
PDB; 1RX8; X-ray; 2.80 A; A=1-159.
PDB; 1RX9; X-ray; 1.90 A; A=1-159.
PDB; 1TDR; X-ray; 2.50 A; A/B=1-159.
PDB; 2ANO; X-ray; 2.68 A; A=1-159.
PDB; 2ANQ; X-ray; 2.13 A; A=1-159.
PDB; 2D0K; X-ray; 1.90 A; A/B=2-159.
PDB; 2DRC; X-ray; 1.90 A; A/B=1-159.
PDB; 2INQ; Neutron; 2.20 A; A/B=1-159.
PDB; 3DAU; X-ray; 1.50 A; A=1-159.
PDB; 3DRC; X-ray; 1.90 A; A/B=1-159.
PDB; 3K74; X-ray; 1.95 A; A=1-159.
PDB; 3KFY; X-ray; 2.08 A; A=1-159.
PDB; 3OCH; X-ray; 1.79 A; A/B=1-159.
PDB; 3QL3; X-ray; 1.80 A; A=1-159.
PDB; 3QYL; X-ray; 1.79 A; A=1-159.
PDB; 3QYO; X-ray; 2.09 A; A=1-159.
PDB; 3R33; X-ray; 2.09 A; A=1-159.
PDB; 4DFR; X-ray; 1.70 A; A/B=1-159.
PDB; 4EIG; X-ray; 2.50 A; A=1-159.
PDB; 4EIZ; X-ray; 2.20 A; A/B=1-159.
PDB; 4EJ1; X-ray; 1.75 A; A/B=1-159.
PDB; 4FHB; X-ray; 2.80 A; A=1-159.
PDB; 4GH8; X-ray; 1.85 A; A/B=1-158.
PDB; 4I13; X-ray; 1.60 A; A=1-159.
PDB; 4I1N; X-ray; 1.89 A; A=1-159.
PDB; 4KJJ; X-ray; 1.15 A; A=1-159.
PDB; 4KJK; X-ray; 1.35 A; A=1-159.
PDB; 4KJL; X-ray; 1.38 A; A=1-159.
PDB; 4NX6; X-ray; 1.35 A; A=1-159.
PDB; 4NX7; X-ray; 1.15 A; A=1-159.
PDB; 4PDJ; Other; 1.60 A; A=1-159.
PDB; 4X5F; X-ray; 1.70 A; A/B=1-159.
PDB; 4X5G; X-ray; 1.90 A; A/B=1-159.
PDB; 4X5H; X-ray; 1.90 A; A=1-159.
PDB; 4X5I; X-ray; 1.80 A; A=1-159.
PDB; 4X5J; X-ray; 1.85 A; A=1-159.
PDB; 5CC9; X-ray; 1.20 A; A=1-159.
PDB; 5CCC; X-ray; 1.50 A; A=1-159.
PDB; 5DFR; X-ray; 2.30 A; A=1-159.
PDB; 5E8Q; X-ray; 1.80 A; A/B=1-159.
PDB; 5EAJ; X-ray; 1.70 A; A/B=1-159.
PDB; 6DFR; X-ray; 2.40 A; A=1-159.
PDB; 7DFR; X-ray; 2.50 A; A=1-159.
PDBsum; 1DDR; -.
PDBsum; 1DDS; -.
PDBsum; 1DHI; -.
PDBsum; 1DHJ; -.
PDBsum; 1DRA; -.
PDBsum; 1DRB; -.
PDBsum; 1DRE; -.
PDBsum; 1DRH; -.
PDBsum; 1DYH; -.
PDBsum; 1DYI; -.
PDBsum; 1DYJ; -.
PDBsum; 1JOL; -.
PDBsum; 1JOM; -.
PDBsum; 1RA1; -.
PDBsum; 1RA2; -.
PDBsum; 1RA3; -.
PDBsum; 1RA8; -.
PDBsum; 1RA9; -.
PDBsum; 1RB2; -.
PDBsum; 1RB3; -.
PDBsum; 1RC4; -.
PDBsum; 1RD7; -.
PDBsum; 1RE7; -.
PDBsum; 1RF7; -.
PDBsum; 1RG7; -.
PDBsum; 1RH3; -.
PDBsum; 1RX1; -.
PDBsum; 1RX2; -.
PDBsum; 1RX3; -.
PDBsum; 1RX4; -.
PDBsum; 1RX5; -.
PDBsum; 1RX6; -.
PDBsum; 1RX7; -.
PDBsum; 1RX8; -.
PDBsum; 1RX9; -.
PDBsum; 1TDR; -.
PDBsum; 2ANO; -.
PDBsum; 2ANQ; -.
PDBsum; 2D0K; -.
PDBsum; 2DRC; -.
PDBsum; 2INQ; -.
PDBsum; 3DAU; -.
PDBsum; 3DRC; -.
PDBsum; 3K74; -.
PDBsum; 3KFY; -.
PDBsum; 3OCH; -.
PDBsum; 3QL3; -.
PDBsum; 3QYL; -.
PDBsum; 3QYO; -.
PDBsum; 3R33; -.
PDBsum; 4DFR; -.
PDBsum; 4EIG; -.
PDBsum; 4EIZ; -.
PDBsum; 4EJ1; -.
PDBsum; 4FHB; -.
PDBsum; 4GH8; -.
PDBsum; 4I13; -.
PDBsum; 4I1N; -.
PDBsum; 4KJJ; -.
PDBsum; 4KJK; -.
PDBsum; 4KJL; -.
PDBsum; 4NX6; -.
PDBsum; 4NX7; -.
PDBsum; 4PDJ; -.
PDBsum; 4X5F; -.
PDBsum; 4X5G; -.
PDBsum; 4X5H; -.
PDBsum; 4X5I; -.
PDBsum; 4X5J; -.
PDBsum; 5CC9; -.
PDBsum; 5CCC; -.
PDBsum; 5DFR; -.
PDBsum; 5E8Q; -.
PDBsum; 5EAJ; -.
PDBsum; 6DFR; -.
PDBsum; 7DFR; -.
DisProt; DP00301; -.
ProteinModelPortal; P0ABQ4; -.
SMR; P0ABQ4; -.
BioGrid; 4262199; 282.
DIP; DIP-35824N; -.
IntAct; P0ABQ4; 16.
MINT; MINT-1239602; -.
STRING; 316385.ECDH10B_0049; -.
BindingDB; P0ABQ4; -.
ChEMBL; CHEMBL1809; -.
DrugBank; DB07262; 1-{[N-(1-IMINO-GUANIDINO-METHYL)]SULFANYLMETHYL}-3-TRIFLUOROMETHYL-BENZENE.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB02363; 2'-Monophosphoadenosine-5'-Diphosphate.
DrugBank; DB02718; 5-Formyl-6-Hydrofolic Acid.
DrugBank; DB02015; Dihydrofolic Acid.
DrugBank; DB03904; Urea.
SWISS-2DPAGE; P0ABQ4; -.
PaxDb; P0ABQ4; -.
PRIDE; P0ABQ4; -.
EnsemblBacteria; AAC73159; AAC73159; b0048.
EnsemblBacteria; BAB96616; BAB96616; BAB96616.
GeneID; 944790; -.
KEGG; ecj:JW0047; -.
KEGG; eco:b0048; -.
PATRIC; fig|511145.12.peg.49; -.
EchoBASE; EB0322; -.
EcoGene; EG10326; folA.
eggNOG; ENOG4108YYV; Bacteria.
eggNOG; COG0262; LUCA.
HOGENOM; HOG000040233; -.
InParanoid; P0ABQ4; -.
KO; K00287; -.
PhylomeDB; P0ABQ4; -.
BioCyc; EcoCyc:DIHYDROFOLATEREDUCT-MONOMER; -.
BioCyc; MetaCyc:DIHYDROFOLATEREDUCT-MONOMER; -.
BRENDA; 1.5.1.3; 2026.
SABIO-RK; P0ABQ4; -.
UniPathway; UPA00077; UER00158.
EvolutionaryTrace; P0ABQ4; -.
PRO; PR:P0ABQ4; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0004146; F:dihydrofolate reductase activity; IDA:EcoCyc.
GO; GO:0051871; F:dihydrofolic acid binding; IDA:CAFA.
GO; GO:0005542; F:folic acid binding; IDA:CAFA.
GO; GO:0051870; F:methotrexate binding; IMP:CAFA.
GO; GO:0070401; F:NADP+ binding; IDA:CAFA.
GO; GO:0070402; F:NADPH binding; IDA:CAFA.
GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IDA:EcoliWiki.
GO; GO:0031427; P:response to methotrexate; IEA:UniProtKB-KW.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00209; DHFR; 1.
Gene3D; 3.40.430.10; -; 1.
InterPro; IPR012259; DHFR.
InterPro; IPR024072; DHFR-like_dom.
InterPro; IPR017925; DHFR_CS.
InterPro; IPR001796; DHFR_dom.
Pfam; PF00186; DHFR_1; 1.
PIRSF; PIRSF000194; DHFR; 1.
PRINTS; PR00070; DHFR.
SUPFAM; SSF53597; SSF53597; 1.
PROSITE; PS00075; DHFR_1; 1.
PROSITE; PS51330; DHFR_2; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Methotrexate resistance; NADP;
One-carbon metabolism; Oxidoreductase; Reference proteome;
Trimethoprim resistance.
CHAIN 1 159 Dihydrofolate reductase.
/FTId=PRO_0000186387.
DOMAIN 1 158 DHFR. {ECO:0000255|PROSITE-
ProRule:PRU00660}.
NP_BIND 13 19 NADP. {ECO:0000269|PubMed:19374017}.
NP_BIND 45 46 NADP. {ECO:0000269|PubMed:19374017}.
NP_BIND 63 64 NADP. {ECO:0000269|PubMed:19374017}.
NP_BIND 95 102 NADP. {ECO:0000269|PubMed:19374017}.
BINDING 5 5 Substrate; via carbonyl oxygen.
{ECO:0000305|PubMed:9012674}.
BINDING 7 7 NADP; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:19374017}.
BINDING 27 27 Substrate. {ECO:0000305|PubMed:9012674}.
BINDING 52 52 Substrate. {ECO:0000305|PubMed:9012674}.
BINDING 57 57 Substrate. {ECO:0000305|PubMed:9012674}.
BINDING 76 76 NADP; via carbonyl oxygen.
{ECO:0000269|PubMed:19374017}.
BINDING 113 113 Substrate. {ECO:0000305|PubMed:9012674}.
VARIANT 28 28 L -> R (in strain: B[RT500] isozyme 2).
VARIANT 30 30 W -> G (in strain: 1810).
VARIANT 154 154 E -> K (in strain: B[MB1428]).
VARIANT 154 154 E -> Q (in strain: 1810).
MUTAGEN 16 16 M->F,S: Increases catalytic rate about 2-
fold. {ECO:0000269|PubMed:16510443}.
MUTAGEN 16 16 M->N: Increases catalytic rate about 2-
fold. Increases catalytic rate about 7-
fold; when associated with L-20; Y-42; F-
92; A-85 and S-152.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 20 20 M->I,V: Increases catalytic rate 2-fold.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 20 20 M->L: Increases catalytic rate 2.5-fold.
Increases catalytic rate about 7-fold;
when associated with N-16; Y-42; F-92; A-
85 and S-152.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 42 42 M->V: Increases catalytic rate almost 2-
fold. {ECO:0000269|PubMed:16510443}.
MUTAGEN 42 42 M->Y: Increases catalytic rate almost 2-
fold. Increases catalytic rate about 7-
fold; when associated with N-16; L-20; A-
85; F-92 and S-152.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 85 85 C->A: Decreases catalytic rate by one
third. Increases catalytic rate about 7-
fold; when associated with N-16; L-20; Y-
42; F-92 and S-152.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 92 92 M->F: No effect. Increases catalytic rate
about 7-fold; when associated with N-16;
L-20; Y-42; A-85 and S-152.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 92 92 M->L: No effect.
{ECO:0000269|PubMed:16510443}.
MUTAGEN 152 152 C->S: Increases catalytic rate 1.5-fold.
Increases catalytic rate about 7-fold;
when associated with N-16; L-20; Y-42; A-
85 and F-92.
{ECO:0000269|PubMed:16510443}.
STRAND 2 9 {ECO:0000244|PDB:4KJJ}.
HELIX 10 12 {ECO:0000244|PDB:4KJJ}.
STRAND 13 16 {ECO:0000244|PDB:4KJJ}.
HELIX 17 19 {ECO:0000244|PDB:5CC9}.
HELIX 25 35 {ECO:0000244|PDB:4KJJ}.
STRAND 40 43 {ECO:0000244|PDB:4KJJ}.
HELIX 44 50 {ECO:0000244|PDB:4KJJ}.
STRAND 55 57 {ECO:0000244|PDB:4X5J}.
STRAND 59 62 {ECO:0000244|PDB:4KJJ}.
STRAND 72 77 {ECO:0000244|PDB:4KJJ}.
HELIX 78 85 {ECO:0000244|PDB:4KJJ}.
STRAND 91 93 {ECO:0000244|PDB:4KJJ}.
HELIX 97 103 {ECO:0000244|PDB:4KJJ}.
HELIX 104 106 {ECO:0000244|PDB:4KJJ}.
STRAND 108 115 {ECO:0000244|PDB:4KJJ}.
STRAND 122 124 {ECO:0000244|PDB:4KJJ}.
HELIX 130 132 {ECO:0000244|PDB:4KJJ}.
STRAND 133 141 {ECO:0000244|PDB:4KJJ}.
STRAND 147 149 {ECO:0000244|PDB:4KJJ}.
STRAND 151 158 {ECO:0000244|PDB:4KJJ}.
SEQUENCE 159 AA; 17999 MW; 6A03CDCD7F5F8562 CRC64;
MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI
ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE
GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR


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