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P05020

- PYRC_ECOLI

UniProt

P05020 - PYRC_ECOLI

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Protein
Dihydroorotase
Gene
pyrC, b1062, JW1049
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.UniRule annotation

Cofactori

Binds 2 zinc ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Zinc 1; via tele nitrogen
Metal bindingi19 – 191Zinc 1; via tele nitrogen
Metal bindingi103 – 1031Zinc 1; via carbamate group
Metal bindingi103 – 1031Zinc 2; via carbamate group
Metal bindingi140 – 1401Zinc 2; via pros nitrogen
Metal bindingi178 – 1781Zinc 2; via tele nitrogen
Metal bindingi251 – 2511Zinc 1

GO - Molecular functioni

  1. dihydroorotase activity Source: EcoCyc
  2. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  2. 'de novo' pyrimidine nucleobase biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:DIHYDROOROT-MONOMER.
ECOL316407:JW1049-MONOMER.
MetaCyc:DIHYDROOROT-MONOMER.
BRENDAi3.5.2.3. 2026.
SABIO-RKP05020.
UniPathwayiUPA00070; UER00117.

Protein family/group databases

MEROPSiM38.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotase (EC:3.5.2.3)
Short name:
DHOase
Gene namesi
Name:pyrC
Ordered Locus Names:b1062, JW1049
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10806. pyrC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 348347DihydroorotaseUniRule annotation
PRO_0000147205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031N6-carboxylysineUniRule annotation

Proteomic databases

PaxDbiP05020.
PRIDEiP05020.

Expressioni

Gene expression databases

GenevestigatoriP05020.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-10624N.
IntActiP05020. 6 interactions.
STRINGi511145.b1062.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Beta strandi15 – 184
Helixi23 – 3412
Beta strandi38 – 425
Helixi53 – 6513
Beta strandi74 – 807
Helixi87 – 959
Beta strandi98 – 1047
Turni113 – 1153
Helixi120 – 1234
Helixi124 – 13310
Beta strandi137 – 1393
Helixi150 – 1523
Helixi153 – 1608
Helixi162 – 1687
Turni169 – 1713
Beta strandi174 – 1763
Helixi182 – 1898
Beta strandi195 – 1995
Helixi201 – 2055
Helixi208 – 2125
Helixi218 – 2203
Helixi229 – 24012
Beta strandi246 – 2483
Helixi257 – 2604
Beta strandi261 – 2655
Turni272 – 2743
Helixi275 – 28511
Helixi289 – 2913
Helixi292 – 2976
Helixi299 – 3046
Beta strandi312 – 3165
Beta strandi329 – 3335
Turni336 – 3394
Beta strandi341 – 3433

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP05020.

Miscellaneous databases

EvolutionaryTraceiP05020.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0418.
HOGENOMiHOG000256259.
KOiK01465.
OMAiLKRNVHQ.
OrthoDBiEOG6TFCMH.
PhylomeDBiP05020.

Family and domain databases

HAMAPiMF_00219. PyrC_type1.
InterProiIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05020-1 [UniParc]FASTAAdd to Basket

« Hide

MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV    50
TTVEAAVAYR QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT 100
AAKLYPANAT TNSSHGVTSI DAIMPVLERM EKIGMPLLVH GEVTHADIDI 150
FDREARFIES VMEPLRQRLT ALKVVFEHIT TKDAADYVRD GNERLAATIT 200
PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA SGFNRVFLGT 250
DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 300
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ 348
Length:348
Mass (Da):38,827
Last modified:January 23, 2007 - v2
Checksum:i179B35324204A111
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA25008. DEECOO.
RefSeqiNP_415580.1. NC_000913.3.
YP_489330.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74146; AAC74146; b1062.
BAA35870; BAA35870; BAA35870.
GeneIDi12932767.
945787.
KEGGiecj:Y75_p1032.
eco:b1062.
PATRICi32117363. VBIEscCol129921_1104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A25008. DEECOO.
RefSeqi NP_415580.1. NC_000913.3.
YP_489330.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J79 X-ray 1.70 A/B 2-348 [» ]
1XGE X-ray 1.90 A/B 2-348 [» ]
2E25 X-ray 2.70 A 2-348 [» ]
2EG6 X-ray 1.70 A/B 2-348 [» ]
2EG7 X-ray 2.00 A/B 2-348 [» ]
2EG8 X-ray 2.20 A/B 2-348 [» ]
2Z24 X-ray 1.90 A/B 2-348 [» ]
2Z25 X-ray 1.87 A/B 2-348 [» ]
2Z26 X-ray 1.29 A/B 2-348 [» ]
2Z27 X-ray 1.87 A/B 2-348 [» ]
2Z28 X-ray 1.87 A/B 2-348 [» ]
2Z29 X-ray 1.90 A/B 2-348 [» ]
2Z2A X-ray 1.87 A/B 2-348 [» ]
2Z2B X-ray 1.85 A 2-348 [» ]
ProteinModelPortali P05020.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10624N.
IntActi P05020. 6 interactions.
STRINGi 511145.b1062.

Chemistry

BindingDBi P05020.

Protein family/group databases

MEROPSi M38.A02.

Proteomic databases

PaxDbi P05020.
PRIDEi P05020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74146 ; AAC74146 ; b1062 .
BAA35870 ; BAA35870 ; BAA35870 .
GeneIDi 12932767.
945787.
KEGGi ecj:Y75_p1032.
eco:b1062.
PATRICi 32117363. VBIEscCol129921_1104.

Organism-specific databases

EchoBASEi EB0799.
EcoGenei EG10806. pyrC.

Phylogenomic databases

eggNOGi COG0418.
HOGENOMi HOG000256259.
KOi K01465.
OMAi LKRNVHQ.
OrthoDBi EOG6TFCMH.
PhylomeDBi P05020.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00117 .
BioCyci EcoCyc:DIHYDROOROT-MONOMER.
ECOL316407:JW1049-MONOMER.
MetaCyc:DIHYDROOROT-MONOMER.
BRENDAi 3.5.2.3. 2026.
SABIO-RK P05020.

Miscellaneous databases

EvolutionaryTracei P05020.
PROi P05020.

Gene expression databases

Genevestigatori P05020.

Family and domain databases

HAMAPi MF_00219. PyrC_type1.
InterProi IPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view ]
Pfami PF01979. Amidohydro_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001237. DHOdimr. 1 hit.
TIGRFAMsi TIGR00856. pyrC_dimer. 1 hit.
PROSITEi PS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiPYRC_ECOLI
AccessioniPrimary (citable) accession number: P05020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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