Dihydrofolate reductase
Details
- Name
- Dihydrofolate reductase
- Synonyms
- 1.5.1.3
- dfrD
- Gene Name
- dfrA
- Organism
- Bacillus anthracis
- 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
- Nadp binding
- Specific Function
- Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
- Pfam Domain Function
- DHFR_1 (PF00186)
- 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 - 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]