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PEC Original Annotations
|
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Essentiality
|
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Class
|
essential
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References (PMID)
|
Can J Microbiol. 1999;45(3):191-200.
Growth properties of a folA null mutant of Escherichia coli K12.
Herrington MB, Chirwa NT.
(
10408091
)
|
|
|
Deletion
|
OCR28,29-1
(D)
|
|
Related gene (W3110 PEC)
|
|
Gene Search
|
Search MG1655 PEC by gene name:
folA
|
|
Related strains
|
|
Strains Search
|
Search strains by gene name:
folA
Search strains by all related name:
folA b0048 ECK0049 JW0047 tmrA
|
General information (Go to Linear View: )
|
|
Gene Name
|
folA
|
|
Alternative name
|
b0048,ECK0049,JW0047,tmrA
|
|
Location, Length
|
49,823 - 50,302
(
+
)
;
1.07
min
;
480
(bp) ,
159
(aa)
|
|
Product
|
dihydrofolate reductase
|
|
Operon Name
|
folA
|
|
Note
|
dihydrofolate reductase type I; trimethoprim resistance; GO_process: GO:0046656 - folic acid biosynthetic process
|
|
Function
|
enzyme; Biosynthesis of cofactors, carriers: Folic acid
|
|
Gene Ontology
|
GO:0004146
;
dihydrofolate reductase activity ( folA )
GO:0006545
;
glycine biosynthetic process ( folA )
GO:0006730
;
one-carbon compound metabolic process ( folA )
GO:0009165
;
nucleotide biosynthetic process ( folA )
GO:0016491
;
oxidoreductase activity ( folA )
GO:0031427
;
response to methotrexate ( folA )
GO:0046677
;
response to antibiotic ( folA )
GO:0050661
;
NADP binding ( folA )
|
|
PID
|
1786233
|
EC number
(KEGG Pathway)
|
1.5.1.3
|
|
Verified Protein Starts
(data
compiled from literature and appropriate citations are available from EcoGene)
|
|
EcoGene
|
folA
(
EG10326
)
|
|
Number of removed
|
0 aa cleaved
|
|
SWISS-PROT
(
Show details
)
|
Entry name(Acc.no)
|
DYR_ECOLI
(
P00379
)
|
|
- Protein name
|
Dihydrofolate reductase
|
|
- Synonyms
|
EC 1.5.1.3
|
|
- Gene name
|
OrderedLocusNames=b0048, c0058, SF0045, S0047;
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Homology Analysis
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BLAST
|
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Bacteria
|
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GTOP
|
folA
(
homologous genes of other bacterias
)
|
|
PDB
(database updated :
2007.02.20
)
|
|
PSI-BLAST
|
Chain A, Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate
|
|
SWISS-PROT
(database updated :
2007.02.20
)
|
|
BLAST
|
Dihydrofolate reductase
|
|
PSI-BLAST
|
Dihydrofolate reductase
|
|
nr
(database updated :
2007.02.20
)
|
|
BLAST
|
Dihydrofolate reductase [Escherichia coli CFT073]
|
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Pfam 28.0
(database updated :
2015-05
)
|
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Pfam
|
|
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PROSITE
|
|
PROSITE
|
CAMP_PHOSPHO_SITE
CK2_PHOSPHO_SITE
MYRISTYL
AMIDATION
DHFR
AA_TRNA_LIGASE_II_2
|
|
MMBR References
|
Mol Gen Genet. 1980;179(1):201-9.
Isolation and characterization of lambda transducing phages for the E. coli genes ksgA and pdxA.
Andresson OS, Davies JE.
(
6450312
)
|
J. Biochem. (Tokyo) 1982;91:1205-1212
Cloning of dihydrofolate reductase gene of Escherichia coli K12.
Iwakura, M., Y. Shimura, and K. Tsuda.
|
J Gen Microbiol. 1983;128:85-92.
Genetic analysis of chromosomal resistance to trimethoprim derived from clinical isolates of Escherichia coli.
Pinn, P. A., K. J. Towner, and F. W. O'Grady.
|
Gene. 1980;8(3):255-65.
Cloning of the Escherichia coli K-12 dihydrofolate reductase gene following mu-mediated transposition.
Rood JI, Laird AJ, Williams JW.
(
6444603
)
|
Mol Gen Genet. 1986;205(3):515-22.
The gene for Escherichia coli diadenosine tetraphosphatase is located immediately clockwise to folA and forms an operon with ksgA.
Blanchin-Roland S, Blanquet S, Schmitter JM, Fayat G.
(
3031429
)
|
Mol Gen Genet. 1976;147(1):91-7.
Regulatory mutants of dihydrofolate reductase in Escherichia coli K12.
Sheldon R, Brenner S.
(
785230
)
|
Mol Gen Genet. 1979;175(1):31-8.
Regulation of dihydrofolate reductase synthesis in Escherichia coli.
Smith DR, Calvo JM.
(
390304
)
|
Mol Gen Genet. 1982;187(1):72-8.
Nucleotide sequence of dihydrofolate reductase genes from trimethoprim-resistant mutants of Escherichia coli. Evidence that dihydrofolate reductase interacts with another essential gene product.
Smith DR, Calvo JM.
(
6761546
)
|
Nucleic Acids Res. 1982;8:2255-2274
Nucleotide sequence of the E. coli gene coding for dihydrofolate reductase.
Smith, D. R., and J. M. Calvo.
|
| Sequences |
Amino acid
FASTA format
|
0001 MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI ILSSQPGTDD
0071 RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE GDTHFPDYEP DDWESVFSEF
0141 HDADAQNSHS YCFEILERR
|
Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 AGCAGAATAT AAAATTTTCC TCAACATCAT
-070 CCTCGCACCA GTCGACGACG GTTTACGCTT TACGTATAGT GGCGACAATT TTTTTTATCG GGAAATCTCA
0001 atgatcagtc tgattgcggc gttagcggta gatcgcgtta tcggcatgga aaacgccatg ccgtggaacc
0071 tgcctgccga tctcgcctgg tttaaacgca acaccttaaa taaacccgtg attatgggcc gccatacctg
0141 ggaatcaatc ggtcgtccgt tgccaggacg caaaaatatt atcctcagca gtcaaccggg tacggacgat
0211 cgcgtaacgt gggtgaagtc ggtggatgaa gccatcgcgg cgtgtggtga cgtaccagaa atcatggtga
0281 ttggcggcgg tcgcgtttat gaacagttct tgccaaaagc gcaaaaactg tatctgacgc atatcgacgc
0351 agaagtggaa ggcgacaccc atttcccgga ttacgagccg gatgactggg aatcggtatt cagcgaattc
0421 cacgatgctg atgcgcagaa ctctcacagc tattgctttg agattctgga gcggcggtaa TTTTGTATAG
0491 AATTTACGGC TAGCGCCGGA TGCGACGCCG GTCGCGTCTT ATCCGGCCTT CCTATATCAG GCTGTGTTTA
0561 AGACGCCGCC GCTTCGCCCA
|
