Dihydrofolate reductase
Details
- Name
- Dihydrofolate reductase
- Kind
- protein
- Synonyms
- 1.5.1.3
- dfrD
- Gene Name
- dfrA
- UniProtKB Entry
- Q81R22TrEMBL
- Organism
- Bacillus anthracis
- NCBI Taxonomy ID
- 1392
- Amino acid sequence
>lcl|BSEQ0012961|Dihydrofolate reductase MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEAIGRPLPGRRN IIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQIYDLFLPYVDKLYITKIHHA FEGDTFFPEMDMTNWKEVFVEKGLTDEKNPYTYYYHVYEKQQ
- Number of residues
- 162
- Molecular Weight
- 19124.795
- Theoretical pI
- 5.3
- GO Classification
- Functionsdihydrofolate reductase activity / metal ion binding / NADP bindingProcessesglycine biosynthetic process / nucleotide biosynthetic process / one-carbon metabolic process / tetrahydrofolate biosynthetic process
- General Function
- Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
- Specific Function
- dihydrofolate reductase activity
- Pfam Domain Function
- DHFR_1 (PF00186)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0012962|Dihydrofolate reductase (dfrA) ATGATAGTTTCATTTATGGTCGCAATGGACGAAAATAGAGTAATTGGTAAAGATAATAAT TTACCTTGGCGTTTACCGAGTGAATTGCAGTATGTAAAGAAAACAACGATGGGTCACCCG CTTATTATGGGAAGAAAAAACTATGAAGCGATTGGTAGACCACTGCCTGGAAGACGTAAT ATTATTGTAACTCGCAATGAAGGATATCATGTTGAAGGCTGTGAAGTAGCACATTCTGTA GAAGAAGTGTTTGAGCTATGCAAAAATGAAGAAGAGATCTTTATTTTTGGCGGAGCACAA ATTTATGATCTCTTTTTACCTTACGTAGACAAGTTATATATAACAAAAATCCATCATGCA TTTGAAGGAGATACATTTTTCCCAGAAATGGATATGACAAATTGGAAAGAAGTTTTTGTT GAAAAAGGTTTAACGGATGAAAAAAATCCGTATACGTATTATTACCATGTATATGAGAAA CAACAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q81R22 UniProtKB Entry Name Q81R22_BACAN GenBank Protein ID 30253517 GenBank Gene ID AE016879 PDB ID(s) 2KGK, 2QK8, 3DAT, 3E0B, 3FL8, 3FL9, 3JVX, 3JW3, 3JW5, 3JWC, 3JWF, 3JWK, 3JWM, 3S9U, 3SA1, 3SA2, 3SAI, 4ELB, 4ELE, 4ELF, 4ELG, 4ELH KEGG ID banh:HYU01_11160 - General References
- Bennett BC, Xu H, Simmerman RF, Lee RE, Dealwis CG: Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase. J Med Chem. 2007 Sep 6;50(18):4374-81. Epub 2007 Aug 14. [Article]
- Beierlein JM, Frey KM, Bolstad DB, Pelphrey PM, Joska TM, Smith AE, Priestley ND, Wright DL, Anderson AC: Synthetic and crystallographic studies of a new inhibitor series targeting Bacillus anthracis dihydrofolate reductase. J Med Chem. 2008 Dec 11;51(23):7532-40. doi: 10.1021/jm800776a. [Article]
- Bourne CR, Bunce RA, Bourne PC, Berlin KD, Barrow EW, Barrow WW: Crystal structure of Bacillus anthracis dihydrofolate reductase with the dihydrophthalazine-based trimethoprim derivative RAB1 provides a structural explanation of potency and selectivity. Antimicrob Agents Chemother. 2009 Jul;53(7):3065-73. doi: 10.1128/AAC.01666-08. Epub 2009 Apr 13. [Article]
- Beierlein JM, Deshmukh L, Frey KM, Vinogradova O, Anderson AC: The solution structure of Bacillus anthracis dihydrofolate reductase yields insight into the analysis of structure-activity relationships for novel inhibitors. Biochemistry. 2009 May 19;48(19):4100-8. doi: 10.1021/bi802319w. [Article]
- Ravel J, Jiang L, Stanley ST, Wilson MR, Decker RS, Read TD, Worsham P, Keim PS, Salzberg SL, Fraser-Liggett CM, Rasko DA: The complete genome sequence of Bacillus anthracis Ames "Ancestor". J Bacteriol. 2009 Jan;191(1):445-6. doi: 10.1128/JB.01347-08. Epub 2008 Oct 24. [Article]
- Bennett BC, Wan Q, Ahmad MF, Langan P, Dealwis CG: X-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor design. J Struct Biol. 2009 May;166(2):162-71. [Article]
- Bourne CR, Wakeham N, Nammalwar B, Tseitin V, Bourne PC, Barrow EW, Mylvaganam S, Ramnarayan K, Bunce RA, Berlin KD, Barrow WW: Structure-activity relationship for enantiomers of potent inhibitors of B. anthracis dihydrofolate reductase. Biochim Biophys Acta. 2013 Jan;1834(1):46-52. doi: 10.1016/j.bbapap.2012.09.001. Epub 2012 Sep 20. [Article]
- Johnson SL, Daligault HE, Davenport KW, Jaissle J, Frey KG, Ladner JT, Broomall SM, Bishop-Lilly KA, Bruce DC, Gibbons HS, Coyne SR, Lo CC, Meincke L, Munk AC, Koroleva GI, Rosenzweig CN, Palacios GF, Redden CL, Minogue TD, Chain PS: Complete genome sequences for 35 biothreat assay-relevant bacillus species. Genome Announc. 2015 Apr 30;3(2). pii: e00151-15. doi: 10.1128/genomeA.00151-15. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 5-[3-(2,5-dimethoxyphenyl)prop-1-yn-1-yl]-6-ethylpyrimidine-2,4-diamine experimental unknown target Details