Name | Dihydrofolate reductase |
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Synonyms | |
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Gene Name | Not Available |
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Organism | Pneumocystis carinii |
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Amino acid sequence | >lcl|BSEQ0011101|Dihydrofolate reductase
MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFESMNVVLMGRK
TWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDHALELLYRTYGSESSVQINRI
FVIGGAQLYKAAMDHPKLDRIMATIIYKDIHCDVFFPLKFRDKEWSSVWKKEKHSDLESW
VGTKVPHGKINEDGFDYEFEMWTRDL |
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Number of residues | 206 |
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Molecular Weight | 23883.325 |
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Theoretical pI | 9.67 |
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GO Classification | Functions - NADP binding
- dihydrofolate reductase activity
Processes - one-carbon metabolic process
- tetrahydrofolate biosynthetic process
- glycine biosynthetic process
- nucleotide biosynthetic process
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General Function | Nadp binding |
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Specific Function | Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. |
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Pfam Domain Function | |
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Transmembrane Regions | Not Available |
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GenBank Protein ID | 169408 |
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UniProtKB ID | P16184 |
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UniProtKB Entry Name | DYR_PNECA |
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Cellular Location | Not Available |
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Gene sequence | >lcl|BSEQ0003086|621 bp
ATGAATCAGCAAAAGTCTTTAACATTGATTGTTGCACTTACAACTTCTTATGGAATTGGC
CGATCAAACTCTCTTCCATGGAAATTAAAGAAAGAAATAAGTTATTTTAAACGAGTAACC
TCTTTTGTACCAACTTTTGATTCATTTGAATCGATGAATGTTGTATTGATGGGTCGAAAA
ACATGGGAAAGTATTCCTTTGCAATTTCGGCCCCTTAAAGGTCGTATTAATGTTGTTATC
ACTCGAAATGAATCTCTGGATCTAGGAAATGGAATTCATTCTGCAAAATCCTTGGATCAT
GCTTTGGAATTGTTATATCGTACATATGGTTCTGAAAGTTCGGTTCAAATTAATCGAATT
TTCGTTATAGGTGGTGCACAGCTATATAAAGCAGCTATGGATCATCCTAAATTAGATAGA
ATTATGGCTACAATAATATACAAGGATATTCATTGTGATGTATTTTTTCCACTTAAATTT
AGGGATAAAGAATGGTCTTCTGTATGGAAAAAAGAAAAACATTCAGATTTAGAATCTTGG
GTTGGTACTAAAGTTCCTCATGGTAAAATAAATGAAGACGGTTTTGATTATGAATTCGAA
ATGTGGACAAGAGATTTATAA |
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GenBank Gene ID | M26495 |
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GeneCard ID | Not Available |
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GenAtlas ID | Not Available |
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HGNC ID | Not Available |
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Chromosome Location | Not Available |
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Locus | Not Available |
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References | - Edman JC, Edman U, Cao M, Lundgren B, Kovacs JA, Santi DV: Isolation and expression of the Pneumocystis carinii dihydrofolate reductase gene. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8625-9. 2682653
- Champness JN, Achari A, Ballantine SP, Bryant PK, Delves CJ, Stammers DK: The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution. Structure. 1994 Oct 15;2(10):915-24. 7866743
- Cody V, Galitsky N, Rak D, Luft JR, Pangborn W, Queener SF: Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+. Biochemistry. 1999 Apr 6;38(14):4303-12. 10194348
- Cody V, Chan D, Galitsky N, Rak D, Luft JR, Pangborn W, Queener SF, Laughton CA, Stevens MF: Structural studies on bioactive compounds. 30. Crystal structure and molecular modeling studies on the Pneumocystis carinii dihydrofolate reductase cofactor complex with TAB, a highly selective antifolate. Biochemistry. 2000 Apr 4;39(13):3556-64. 10736154
- Cody V, Galitsky N, Luft JR, Pangborn W, Rosowsky A, Queener SF: Structure-based enzyme inhibitor design: modeling studies and crystal structure analysis of Pneumocystis carinii dihydrofolate reductase ternary complex with PT653 and NADPH. Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):946-54. Epub 2002 May 29. 12037296
- Cody V, Galitsky N, Luft JR, Pangborn W, Queener SF, Gangjee A: Analysis of quinazoline and pyrido[2,3-d]pyrimidine N9-C10 reversed-bridge antifolates in complex with NADP+ and Pneumocystis carinii dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1393-9. Epub 2002 Aug 23. 12198294
- Cody V, Luft JR, Pangborn W, Gangjee A, Queener SF: Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry. Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):646-55. Epub 2004 Mar 23. 15039552
- Cody V, Pace J, Chisum K, Rosowsky A: New insights into DHFR interactions: analysis of Pneumocystis carinii and mouse DHFR complexes with NADPH and two highly potent 5-(omega-carboxy(alkyloxy) trimethoprim derivatives reveals conformational correlations with activity and novel parallel ring stacking interactions. Proteins. 2006 Dec 1;65(4):959-69. 17019704
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