Dihydroorotate dehydrogenase (quinone)
Details
- Name
- Dihydroorotate dehydrogenase (quinone)
- Synonyms
- 1.3.5.2
- DHOD
- DHODase
- DHOdehase
- Dihydroorotate oxidase
- Gene Name
- pyrD
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016461|Dihydroorotate dehydrogenase (quinone) MYYPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAKPVNCMGLTFKNPLGL AAGLDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGV DNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYLICMEKIYAYAGYIAINISSPNTPG LRTLQYGEALDDLLTAIKNKQNDLQAMHHKYVPIAVKIAPDLSEEELIQVADSLVRHNID GVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDS VIAAREKIAAGASLVQIYSGFIFKGPPLIKEIVTHI
- Number of residues
- 336
- Molecular Weight
- 36774.185
- Theoretical pI
- 7.97
- GO Classification
- Functionsdihydroorotate dehydrogenase activity / FMN bindingProcesses'de novo' pyrimidine nucleobase biosynthetic process / 'de novo' UMP biosynthetic processComponentscytoplasm / cytosol / membrane / plasma membrane
- General Function
- Fmn binding
- Specific Function
- Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
- Pfam Domain Function
- DHO_dh (PF01180)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell membrane
- Gene sequence
>lcl|BSEQ0016462|Dihydroorotate dehydrogenase (quinone) (pyrD) ATGTACTACCCCTTCGTTCGTAAAGCCCTTTTCCAGCTCGATCCAGAGCGCGCTCATGAG TTTACTTTTCAGCAATTACGCCGTATTACAGGAACGCCGTTTGAAGCACTGGTGCGGCAG AAAGTGCCTGCGAAACCTGTTAACTGCATGGGCCTGACGTTTAAAAATCCGCTTGGTCTG GCAGCCGGTCTTGATAAAGACGGGGAGTGCATTGACGCGTTAGGCGCGATGGGATTTGGA TCGATCGAGATCGGTACCGTCACGCCACGTCCACAGCCAGGTAATGACAAGCCGCGTCTC TTTCGTCTGGTAGATGCCGAAGGTTTGATCAACCGTATGGGCTTTAATAATCTTGGCGTT GATAACCTCGTAGAGAACGTAAAAAAGGCCCATTATGACGGCGTCCTGGGTATTAACATC GGCAAAAATAAAGATACGCCAGTGGAGCAGGGCAAAGATGACTATCTGATTTGTATGGAA AAAATCTATGCCTATGCGGGATATATCGCCATCAATATTTCATCGCCGAATACCCCAGGA TTACGCACGCTGCAATATGGTGAAGCGCTGGATGATCTCTTAACCGCGATTAAAAATAAG CAAAATGATTTGCAAGCGATGCACCATAAATATGTGCCGATCGCAGTGAAGATCGCGCCG GATCTTTCTGAAGAAGAATTGATCCAGGTTGCCGATAGTTTAGTTCGCCATAATATTGAT GGCGTTATTGCAACCAATACCACACTCGATCGTTCTCTTGTTCAGGGAATGAAAAATTGC GATCAAACCGGTGGCTTAAGTGGTCGTCCGCTTCAGTTAAAAAGCACCGAAATTATTCGC CGCTTGTCACTGGAATTAAACGGTCGCTTACCGATCATCGGTGTTGGCGGCATCGACTCG GTTATCGCTGCGCGTGAAAAGATTGCTGCGGGTGCCTCACTGGTGCAAATTTATTCTGGT TTTATTTTTAAAGGTCCGCCGCTGATTAAAGAAATCGTTACCCATATCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A7E1 UniProtKB Entry Name PYRD_ECOLI GenBank Protein ID 42609 GenBank Gene ID X02826 - General References
- Larsen JN, Jensen KF: Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase. Eur J Biochem. 1985 Aug 15;151(1):59-65. [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]
- Bjornberg O, Gruner AC, Roepstorff P, Jensen KF: The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis. Biochemistry. 1999 Mar 9;38(10):2899-908. [Article]
- Norager S, Jensen KF, Bjornberg O, Larsen S: E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure. 2002 Sep;10(9):1211-23. [Article]