Dihydroorotate dehydrogenase (quinone)

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	None
Molecular Weight	36774.185
Theoretical pI	7.97
GO Classification	Functions FMN binding dihydroorotate dehydrogenase activity Processes 'de novo' pyrimidine nucleobase biosynthetic process 'de novo' UMP biosynthetic process Components cytoplasm membrane plasma membrane cytosol
General Function	Fmn binding
Specific Function	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P0A7E1
UniProtKB Entry Name
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
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. [2992959 ] 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. [8905232 ] 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. [9278503 ] 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. [16738553 ] 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. [10074342 ] 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. [12220493 ]

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