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P05020 (PYRC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotase

Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:b1062, JW1049
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00219

Cofactor

Binds 2 zinc ions per subunit.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP-Rule MF_00219

Subunit structure

Homodimer.

Sequence similarities

Belongs to the DHOase family. Type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 348347Dihydroorotase HAMAP-Rule MF_00219
PRO_0000147205

Sites

Metal binding171Zinc 1
Metal binding191Zinc 1
Metal binding1031Zinc 1; via carbamate group
Metal binding1031Zinc 2; via carbamate group
Metal binding1401Zinc 2
Metal binding1781Zinc 2
Metal binding2511Zinc 1

Amino acid modifications

Modified residue1031N6-carboxylysine HAMAP-Rule MF_00219

Secondary structure

................................................................. 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05020 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 179B35324204A111

FASTA34838,827
        10         20         30         40         50         60 
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 

        70         80         90        100        110        120 
QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSI 

       130        140        150        160        170        180 
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT 

       190        200        210        220        230        240 
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA 

       250        260        270        280        290        300 
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 

       310        320        330        340 
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the structural gene for dihydroorotase of Escherichia coli K12."
Baeckstroem D., Sjoeberg R.-M., Lundberg L.G.
Eur. J. Biochem. 160:77-82(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Nucleotide sequence and expression of the pyrC gene of Escherichia coli K-12."
Wilson H.R., Chan P.T., Turnbough C.L. Jr.
J. Bacteriol. 169:3051-3058(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"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."
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. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]Ohmori H.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-348.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[8]"Dihydroorotase from Escherichia coli. Substitution of Co(II) for the active site Zn(II)."
Brown D.C., Collins K.D.
J. Biol. Chem. 266:1597-1604(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-BINDING.
[9]"Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center."
Thoden J.B., Phillips G.N. Jr., Neal T.M., Raushel F.M., Holden H.M.
Biochemistry 40:6989-6997(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), CARBAMYLATION AT LYS-103.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04469 Genomic DNA. Translation: CAA28157.1.
M16752 Genomic DNA. Translation: AAA24482.1.
U00096 Genomic DNA. Translation: AAC74146.1.
AP009048 Genomic DNA. Translation: BAA35870.1.
D31709 Genomic DNA. Translation: BAA06514.1.
PIRDEECOO. A25008.
RefSeqNP_415580.1. NC_000913.3.
YP_489330.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J79X-ray1.70A/B2-348[»]
1XGEX-ray1.90A/B2-348[»]
2E25X-ray2.70A2-348[»]
2EG6X-ray1.70A/B2-348[»]
2EG7X-ray2.00A/B2-348[»]
2EG8X-ray2.20A/B2-348[»]
2Z24X-ray1.90A/B2-348[»]
2Z25X-ray1.87A/B2-348[»]
2Z26X-ray1.29A/B2-348[»]
2Z27X-ray1.87A/B2-348[»]
2Z28X-ray1.87A/B2-348[»]
2Z29X-ray1.90A/B2-348[»]
2Z2AX-ray1.87A/B2-348[»]
2Z2BX-ray1.85A2-348[»]
ProteinModelPortalP05020.
SMRP05020. Positions 4-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10624N.
IntActP05020. 6 interactions.
STRING511145.b1062.

Chemistry

BindingDBP05020.

Protein family/group databases

MEROPSM38.A02.

Proteomic databases

PaxDbP05020.
PRIDEP05020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74146; AAC74146; b1062.
BAA35870; BAA35870; BAA35870.
GeneID12932767.
945787.
KEGGecj:Y75_p1032.
eco:b1062.
PATRIC32117363. VBIEscCol129921_1104.

Organism-specific databases

EchoBASEEB0799.
EcoGeneEG10806. pyrC.

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHOG000256259.
KOK01465.
OMAYAEAFEQ.
OrthoDBEOG6TFCMH.
PhylomeDBP05020.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycEcoCyc:DIHYDROOROT-MONOMER.
ECOL316407:JW1049-MONOMER.
MetaCyc:DIHYDROOROT-MONOMER.
BRENDA3.5.2.3. 2026.
SABIO-RKP05020.
UniPathwayUPA00070; UER00117.

Gene expression databases

GenevestigatorP05020.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. pyrC_dimer. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05020.
PROP05020.

Entry information

Entry namePYRC_ECOLI
AccessionPrimary (citable) accession number: P05020
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene