ECMDB: Dihydroorotate dehydrogenase (P0A7E1)

Identification

Name:

Dihydroorotate dehydrogenase

Synonyms:

DHOdehase
DHOD
DHODase
Dihydroorotate oxidase

Gene Name:

pyrD

Enzyme Class:

1.3.5.2

Biological Properties

General Function:

Involved in catalytic activity

Specific Function:

(S)-dihydroorotate + a quinone = orotate + a quinol

Cellular Location:

Cell membrane; Peripheral membrane protein

SMPDB Pathways:

Pyrimidine metabolism PW000942

KEGG Pathways:

Metabolic pathways eco01100
Pyrimidine metabolism ec00240

KEGG Reactions:

1.0

↔

1.0

1.04,5-Dihydroorotic acid + 1.0Fumaric acid ↔ 1.0Orotic acid + 1.0Succinic acid
ReactionCard

1.0

↔

1.0

1.04,5-Dihydroorotic acid + 1.0Quinone ↔ 1.0Orotic acid + 1.0Hydroquinone
ReactionCard

SMPDB Reactions:

1.04,5-Dihydroorotic acid

1.0

→

1.0

1.04,5-Dihydroorotic acid + 1.0Ubiquinone-1 + 1.04,5-Dihydroorotic acid → 1.0Ubiquinol-1 + 1.0Orotic acid
ReactionCard

EcoCyc Reactions:

1.0

1.0a ubiquinone

→

1.0

1.0a ubiquinol

1.04,5-Dihydroorotic acid + 1.0a ubiquinone → 1.0Orotic acid + 1.0a ubiquinol
ReactionCard

1.0

1.0a menaquinone

→

1.0

1.0a menaquinol

1.04,5-Dihydroorotic acid + 1.0a menaquinone → 1.0Orotic acid + 1.0a menaquinol
ReactionCard

Complex Reactions:

1.0

→

1.0

1.04,5-Dihydroorotic acid + 1.0Ubiquinone-8 → 1.0Orotic acid + 1.0Ubiquinol-8
ReactionCard

1.0

1.0Menaquinone 8

→

1.0

1.04,5-Dihydroorotic acid + 1.0Menaquinone 8 → 1.0Menaquinol 8 + 1.0Orotic acid
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00528	4,5-Dihydroorotic acid	MetaboCard
ECMDB00176	Fumaric acid	MetaboCard
ECMDB02434	Hydroquinone	MetaboCard
ECMDB21245	Menaquinol 8	MetaboCard
ECMDB00226	Orotic acid	MetaboCard
ECMDB23060	Quinone	MetaboCard
ECMDB00254	Succinic acid	MetaboCard
ECMDB21574	Ubiquinol-1	MetaboCard
ECMDB01060	Ubiquinol-8	MetaboCard
ECMDB21438	Ubiquinone-1	MetaboCard
ECMDB21296	Ubiquinone-8	MetaboCard

GO Classification:

Component
cell part
membrane
Function
catalytic activity
dihydroorotate dehydrogenase activity
dihydroorotate oxidase activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
oxidoreductase activity, acting on the CH-CH group of donors, quinone or related compound as acceptor
Process
'de novo' pyrimidine base biosynthetic process
cellular aromatic compound metabolic process
cellular metabolic process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
oxidation reduction
pyrimidine base biosynthetic process
pyrimidine base metabolic process
pyrimidine nucleoside monophosphate biosynthetic process
pyrimidine nucleotide biosynthetic process
pyrimidine nucleotide metabolic process
pyrimidine ribonucleoside monophosphate biosynthetic process
UMP biosynthetic process

Gene Properties

Blattner:

b0945

Gene Orientation

Clockwise

Centisome Percentage:

21.64

Left Sequence End

1003991

Right Sequence End

1005001

Gene Sequence:

>1011 bp
ATGTACTACCCCTTCGTTCGTAAAGCCCTTTTCCAGCTCGATCCAGAGCGCGCTCATGAG
TTTACTTTTCAGCAATTACGCCGTATTACAGGAACGCCGTTTGAAGCACTGGTGCGGCAG
AAAGTGCCTGCGAAACCTGTTAACTGCATGGGCCTGACGTTTAAAAATCCGCTTGGTCTG
GCAGCCGGTCTTGATAAAGACGGGGAGTGCATTGACGCGTTAGGCGCGATGGGATTTGGA
TCGATCGAGATCGGTACCGTCACGCCACGTCCACAGCCAGGTAATGACAAGCCGCGTCTC
TTTCGTCTGGTAGATGCCGAAGGTTTGATCAACCGTATGGGCTTTAATAATCTTGGCGTT
GATAACCTCGTAGAGAACGTAAAAAAGGCCCATTATGACGGCGTCCTGGGTATTAACATC
GGCAAAAATAAAGATACGCCAGTGGAGCAGGGCAAAGATGACTATCTGATTTGTATGGAA
AAAATCTATGCCTATGCGGGATATATCGCCATCAATATTTCATCGCCGAATACCCCAGGA
TTACGCACGCTGCAATATGGTGAAGCGCTGGATGATCTCTTAACCGCGATTAAAAATAAG
CAAAATGATTTGCAAGCGATGCACCATAAATATGTGCCGATCGCAGTGAAGATCGCGCCG
GATCTTTCTGAAGAAGAATTGATCCAGGTTGCCGATAGTTTAGTTCGCCATAATATTGAT
GGCGTTATTGCAACCAATACCACACTCGATCGTTCTCTTGTTCAGGGAATGAAAAATTGC
GATCAAACCGGTGGCTTAAGTGGTCGTCCGCTTCAGTTAAAAAGCACCGAAATTATTCGC
CGCTTGTCACTGGAATTAAACGGTCGCTTACCGATCATCGGTGTTGGCGGCATCGACTCG
GTTATCGCTGCGCGTGAAAAGATTGCTGCGGGTGCCTCACTGGTGCAAATTTATTCTGGT
TTTATTTTTAAAGGTCCGCCGCTGATTAAAGAAATCGTTACCCATATCTAA

Protein Properties

Pfam Domain Function:

DHO_dh (PF01180 )

Protein Residues:

336

Protein Molecular Weight:

36774

Protein Theoretical pI:

PDB File:

1F76

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Dihydroorotate dehydrogenase
MYYPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAKPVNCMGLTFKNPLGL
AAGLDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGV
DNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYLICMEKIYAYAGYIAINISSPNTPG
LRTLQYGEALDDLLTAIKNKQNDLQAMHHKYVPIAVKIAPDLSEEELIQVADSLVRHNID
GVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDS
VIAAREKIAAGASLVQIYSGFIFKGPPLIKEIVTHI

References

External Links:

Resource	Link
Uniprot ID:	P0A7E1
Uniprot Name:	PYRD_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	1651460
PDB ID:	1F76
Ecogene ID:	EG10807
Ecocyc:	EG10807
ColiBase:	b0945
Kegg Gene:	b0945
EchoBASE ID:	EB0800
CCDB:	PYRD_ECOLI
BacMap:	16128912

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Larsen, J. N., Jensen, K. F. (1985). "Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase." Eur J Biochem 151:59-65. Pubmed: 2992959
Norager, S., Jensen, K. F., Bjornberg, O., Larsen, S. (2002). "E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases." Structure 10:1211-1223. Pubmed: 12220493
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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232