Dihydroorotase
Details
- Name
- Dihydroorotase
- Synonyms
- 3.5.2.3
- DHOase
- Gene Name
- pyrC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016428|Dihydroorotase MTAPSQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVEAAVAYR QRILDAVPAGHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKLYPANATTNSSHGVTSI DAIMPVLERMEKIGMPLLVHGEVTHADIDIFDREARFIESVMEPLRQRLTALKVVFEHIT TKDAADYVRDGNERLAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVA SGFNRVFLGTDSAPHARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNG PQFYGLPVNDTFIELVREEQQVAESIALTDDTLVPFLAGETVRWSVKQ
- Number of residues
- 348
- Molecular Weight
- 38827.045
- Theoretical pI
- 6.14
- GO Classification
- Functionsdihydroorotase activity / zinc ion bindingProcesses'de novo' pyrimidine nucleobase biosynthetic process / 'de novo' UMP biosynthetic processComponentscytosol
- General Function
- Zinc ion binding
- Specific Function
- Not Available
- Pfam Domain Function
- Amidohydro_1 (PF01979)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0016429|Dihydroorotase (pyrC) ATGACTGCACCATCCCAGGTATTAAAGATCCGCCGCCCAGACGACTGGCACCTTCACCTC CGCGATGGCGACATGTTAAAAACTGTCGTGCCATATACCAGCGAAATTTATGGACGGGCT ATCGTAATGCCCAATCTGGCTCCGCCCGTGACCACCGTTGAGGCTGCCGTGGCGTATCGC CAGCGTATTCTTGACGCCGTACCTGCCGGGCACGATTTCACCCCATTGATGACCTGTTAT TTAACAGATTCGCTGGATCCTAATGAGCTGGAGCGCGGATTTAACGAAGGCGTGTTCACC GCTGCAAAACTTTACCCGGCAAACGCAACCACTAACTCCAGCCACGGCGTGACGTCAATT GACGCAATCATGCCGGTACTTGAGCGCATGGAAAAAATCGGTATGCCGCTACTGGTGCAT GGTGAAGTGACACATGCAGATATCGACATTTTTGATCGTGAAGCGCGCTTTATAGAAAGC GTGATGGAACCTCTGCGCCAGCGCCTGACTGCGCTGAAAGTCGTTTTTGAGCACATCACC ACCAAAGATGCTGCCGACTATGTCCGTGACGGAAATGAACGGCTGGCTGCCACCATCACT CCGCAGCATCTGATGTTTAACCGCAACCATATGCTGGTTGGAGGCGTGCGTCCGCACCTG TATTGTCTACCCATCCTCAAACGTAATATTCACCAACAGGCATTGCGTGAACTGGTCGCC AGCGGTTTTAATCGAGTATTCCTCGGTACGGATTCTGCGCCACATGCACGTCATCGCAAA GAGAGCAGTTGCGGCTGCGCGGGCTGCTTCAACGCCCCAACCGCGCTGGGCAGTTACGCT ACCGTCTTTGAAGAAATGAATGCTTTGCAGCACTTTGAAGCATTCTGTTCTGTAAACGGC CCGCAGTTCTATGGGTTGCCGGTCAACGACACATTCATCGAACTGGTACGTGAAGAGCAA CAGGTTGCTGAAAGCATCGCACTGACTGATGACACGCTGGTGCCATTCCTCGCCGGGGAA ACGGTACGCTGGTCCGTTAAACAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P05020 UniProtKB Entry Name PYRC_ECOLI GenBank Protein ID 42607 GenBank Gene ID X04469 - General References
- Backstrom D, Sjoberg RM, Lundberg LG: Nucleotide sequence of the structural gene for dihydroorotase of Escherichia coli K12. Eur J Biochem. 1986 Oct 1;160(1):77-82. [Article]
- Wilson HR, Chan PT, Turnbough CL Jr: Nucleotide sequence and expression of the pyrC gene of Escherichia coli K-12. J Bacteriol. 1987 Jul;169(7):3051-8. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Brown DC, Collins KD: Dihydroorotase from Escherichia coli. Substitution of Co(II) for the active site Zn(II). J Biol Chem. 1991 Jan 25;266(3):1597-604. [Article]
- Thoden JB, Phillips GN Jr, Neal TM, Raushel FM, Holden HM: Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry. 2001 Jun 19;40(24):6989-97. [Article]