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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.
13-FEB-2019, entry version 127.
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:
Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3;
Evidence={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; 5UIH; X-ray; 1.65 A; A=1-159.
PDB; 5UII; X-ray; 1.35 A; A=2-159.
PDB; 5UIO; X-ray; 1.93 A; A/B/C/D/E=1-159.
PDB; 5UIP; X-ray; 1.90 A; A/B=2-159.
PDB; 5UJX; X-ray; 1.80 A; A/B=1-159.
PDB; 5W3Q; X-ray; 1.40 A; A=1-159.
PDB; 5Z6F; X-ray; 1.80 A; A=1-159.
PDB; 5Z6J; X-ray; 1.80 A; A=1-159.
PDB; 5Z6K; X-ray; 1.80 A; A=1-159.
PDB; 5Z6L; X-ray; 1.90 A; A=1-159.
PDB; 5Z6M; X-ray; 2.20 A; A=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; 5UIH; -.
PDBsum; 5UII; -.
PDBsum; 5UIO; -.
PDBsum; 5UIP; -.
PDBsum; 5UJX; -.
PDBsum; 5W3Q; -.
PDBsum; 5Z6F; -.
PDBsum; 5Z6J; -.
PDBsum; 5Z6K; -.
PDBsum; 5Z6L; -.
PDBsum; 5Z6M; -.
PDBsum; 6DFR; -.
PDBsum; 7DFR; -.
DisProt; DP00301; -.
ProteinModelPortal; P0ABQ4; -.
SMR; P0ABQ4; -.
BioGrid; 4262199; 297.
DIP; DIP-35824N; -.
IntAct; P0ABQ4; 16.
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; -.
EPD; P0ABQ4; -.
jPOST; 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; ECOL316407:JW0047-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:0050661; F:NADP binding; IBA:GO_Central.
GO; GO:0070401; F:NADP+ binding; IDA:CAFA.
GO; GO:0070402; F:NADPH binding; IDA:CAFA.
GO; GO:0046452; P:dihydrofolate metabolic process; IBA:GO_Central.
GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
GO; GO:0006545; P:glycine 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; IBA:GO_Central.
CDD; cd00209; DHFR; 1.
Gene3D; 3.40.430.10; -; 2.
InterPro; IPR012259; DHFR.
InterPro; IPR024072; DHFR-like_dom_sf.
InterPro; IPR017925; DHFR_CS.
InterPro; IPR001796; DHFR_dom.
PANTHER; PTHR22778:SF16; PTHR22778:SF16; 1.
Pfam; PF00186; DHFR_1; 1.
PIRSF; PIRSF000194; DHFR; 1.
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}.
TURN 20 23 {ECO:0000244|PDB:5UIH}.
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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1006: metapathway biotransformation
WP1124: metapathway biotransformation
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1403: AMPK signaling
WP1461: Photosynthetic Carbon Reduction
WP1566: Citrate cycle (TCA cycle)
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1680: Oxidative phosphorylation
WP1681: Pantothenate and CoA biosynthesis
WP2230: Chlorophyll b degradation
WP2248: anthocyanin biosynthesis
WP2368: HMG-CoA reductase pathway
WP237: Glucocorticoid & Mineralcorticoid Metabolism
WP2409: New Pathway
WP305: Glucocorticoid Metabolism
WP495: Glucocorticoid & Mineralcorticoid Metabolism
WP668: Octadecanoid Pathway
WP702: metapathway biotransformation
WP889: metapathway biotransformation

Related Genes :
[THY-1 At2g16370 F16F14.13] Bifunctional dihydrofolate reductase-thymidylate synthase 1 (DHFR-TS 1) [Includes: Dihydrofolate reductase (EC 1.5.1.3); Thymidylate synthase (EC 2.1.1.45)]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[DHFR] Dihydrofolate reductase (EC 1.5.1.3)
[THY-2 At4g34570 T4L20.150] Bifunctional dihydrofolate reductase-thymidylate synthase 2 (DHFR-TS 2) [Includes: Dihydrofolate reductase (EC 1.5.1.3); Thymidylate synthase (EC 2.1.1.45)]
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[arfC MJ0671] 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase (DAROPP reductase) (DARP reductase) (EC 1.1.1.302) (2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase) (2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase) (DARIPP synthase) (MjaRED)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[hchA ECH74115_2746] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[folM ydgB b1606 JW1598] Dihydromonapterin reductase (H(2)-MPt reductase) (EC 1.5.1.-) (Dihydrofolate reductase) (DHFR) (EC 1.5.1.3)
[AKR1C3 DDH1 HSD17B5 KIAA0119 PGFS] Aldo-keto reductase family 1 member C3 (EC 1.-.-.-) (17-beta-hydroxysteroid dehydrogenase type 5) (17-beta-HSD 5) (3-alpha-HSD type II, brain) (3-alpha-hydroxysteroid dehydrogenase type 2) (3-alpha-HSD type 2) (EC 1.1.1.357) (Chlordecone reductase homolog HAKRb) (Dihydrodiol dehydrogenase 3) (DD-3) (DD3) (Dihydrodiol dehydrogenase type I) (HA1753) (Indanol dehydrogenase) (EC 1.1.1.112) (Prostaglandin F synthase) (PGFS) (EC 1.1.1.188) (Testosterone 17-beta-dehydrogenase 5) (EC 1.1.1.239) (EC 1.1.1.64) (Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase) (EC 1.3.1.20)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3K24_08940 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3I61_16000 DD762_13665 DIV22_29760 DIV25_29790 DL545_05995 DL800_20505 DNQ41_18960 DNR41_08670 DQE83_04685 DS732_20695 DS966_06010 DTL43_09355 DTL84_00105 DTL90_02675 DTM10_03745 DTM25_22630 DTM27_13675 DTM45_13530 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9010_01168 NCTC9036_01135 NCTC9037_01243 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753106_03183 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753391_02580 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[hmpA hmp A8C65_03855 A9R57_17040 ACN002_2592 ACN77_09545 ACN81_26320 ACU57_10360 ACU90_01485 AM270_07210 AM464_04560 AML07_10430 APZ14_05505 AUQ13_13215 AUS26_21665 AW106_11070 BB545_05760 BHS81_15570 BHS87_14445 BJJ90_06510 BK292_20760 BMT53_22940 BMT91_09730 BN17_18391 BUE81_08005 BVL39_14050 BW690_11150 BZL31_13550 C2U48_21325 C4J69_10505 C5N07_10115 C5P01_05560 C5P43_25010 C6986_16510 C7235_06805 C9E25_16695 CG691_06165 CG705_05290 CG706_03875 COD30_01045 COD46_11500 CRM83_27495 CWS33_10010 CXB56_09850 D3I61_14815 DIV22_11300 DIV25_09890 DL545_07245 DL800_19195 DNQ41_17925 DTL43_01910 DTL84_06405 EC1094V2_1116 EC3234A_44c01590 EC95NR1_01777 ERS085365_01518 ERS085374_00038 ERS085416_03760 ERS139211_00868 ERS150873_01392 ERS150876_00857 FORC28_1400 HW43_17160 NCTC11022_02631 NCTC11181_03552 NCTC13148_02382 NCTC8500_01411 NCTC8960_04037 NCTC8985_06124 NCTC9010_01386 NCTC9036_01390 NCTC9037_01459 NCTC9058_00631 NCTC9062_01812 NCTC9073_04581 NCTC9706_04593 NCTC9962_00729 PU06_05410 RG28_09110 RK56_022045 SAMEA3472044_03009 SAMEA3472067_01827 SAMEA3472070_00042 SAMEA3472080_01630 SAMEA3484427_00463 SAMEA3484429_00572 SAMEA3484433_03169 SAMEA3752557_00946 SAMEA3753097_02775 SAMEA3753106_01160 SAMEA3753391_02738 SAMEA3753397_00885 SK85_02808 WQ89_05840] Flavohemoprotein (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)
[cypB cyp102A3 yrhJ BSU27160] Bifunctional cytochrome P450/NADPH--P450 reductase 2 (CYP102A3) (Fatty acid hydroxylase CypB) (Flavocytochrome P450 102A3) [Includes: Cytochrome P450 102A3 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[his-3 5C2.120 NCU03139] Histidine biosynthesis trifunctional protein [Includes: Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19); Phosphoribosyl-ATP pyrophosphohydrolase (EC 3.6.1.31); Histidinol dehydrogenase (HDH) (EC 1.1.1.23)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BHF46_18455 BMT91_24760 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 EC3234A_36c00010 NCTC8500_02249 NCTC9010_02117 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[SRD5A3 SRD5A2L] Polyprenol reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 2-like) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3)
[folC dedC b2315 JW2312] Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase) (Folylpolyglutamate synthetase) (Tetrahydrofolylpolyglutamate synthase)
[Akr1c21] Aldo-keto reductase family 1 member C21 (EC 1.1.1.-) (17-alpha-hydroxysteroid dehydrogenase) (17-alpha-HSD) (3(or 17)-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.209) (3-alpha-hydroxysteroid dehydrogenase) (Dihydrodiol dehydrogenase type 1) (DD1) (Dihydrodiol dehydrogenase type 3) (DD3)
[hchA ECH7EC869_3386] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[kduD ygeC yqeD b2842 JW2810] 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase (EC 1.1.1.127) (2-deoxy-D-gluconate 3-dehydrogenase) (2-keto-3-deoxygluconate 5-dehydrogenase) (2-keto-3-deoxygluconate oxidoreductase) (KDG oxidoreductase) (20-ketosteroid reductase) (EC 1.1.1.-)
[Hsd3b1 Hsd3b] 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[folC Rv2447c LH57_13380] Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (Tetrahydrofolylpolyglutamate synthase)
[Srd5a3 Srd5a2l] Polyprenol reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 2-like) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3)

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