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Protein

Dihydroorotase

Gene

pyrC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase catalytic chain (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi17Zinc 1; via tele nitrogen1
Metal bindingi19Zinc 1; via tele nitrogen1
Metal bindingi103Zinc 1; via carbamate group1
Metal bindingi103Zinc 2; via carbamate group1
Metal bindingi140Zinc 2; via pros nitrogen1
Metal bindingi178Zinc 2; via tele nitrogen1
Metal bindingi251Zinc 11

GO - Molecular functioni

  • dihydroorotase activity Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10806. pyrC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001472052 – 348DihydroorotaseAdd BLAST347

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei103N6-carboxylysine1 Publication1

Proteomic databases

PaxDbiP05020.
PRIDEiP05020.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4261761. 17 interactors.
DIPiDIP-10624N.
IntActiP05020. 6 interactors.
STRINGi511145.b1062.

Chemistry databases

BindingDBiP05020.

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Beta strandi15 – 18Combined sources4
Helixi23 – 34Combined sources12
Beta strandi38 – 42Combined sources5
Helixi53 – 65Combined sources13
Beta strandi74 – 80Combined sources7
Helixi87 – 95Combined sources9
Beta strandi98 – 104Combined sources7
Turni113 – 115Combined sources3
Helixi120 – 123Combined sources4
Helixi124 – 133Combined sources10
Beta strandi137 – 139Combined sources3
Helixi150 – 152Combined sources3
Helixi153 – 160Combined sources8
Helixi162 – 168Combined sources7
Turni169 – 171Combined sources3
Beta strandi174 – 176Combined sources3
Helixi182 – 189Combined sources8
Beta strandi195 – 199Combined sources5
Helixi201 – 205Combined sources5
Helixi208 – 212Combined sources5
Helixi218 – 220Combined sources3
Helixi229 – 240Combined sources12
Beta strandi246 – 248Combined sources3
Helixi257 – 260Combined sources4
Beta strandi261 – 265Combined sources5
Turni272 – 274Combined sources3
Helixi275 – 285Combined sources11
Helixi289 – 291Combined sources3
Helixi292 – 297Combined sources6
Helixi299 – 304Combined sources6
Beta strandi312 – 316Combined sources5
Beta strandi329 – 333Combined sources5
Turni336 – 339Combined sources4
Beta strandi341 – 343Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP05020.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05020.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Type 1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105EKE. Bacteria.
COG0418. LUCA.
HOGENOMiHOG000256259.
InParanoidiP05020.
KOiK01465.
OMAiYAEAFEQ.
PhylomeDBiP05020.

Family and domain databases

CDDicd01294. DHOase. 1 hit.
HAMAPiMF_00219. PyrC_type1. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
SUPFAMiSSF51556. SSF51556. 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

        10         20         30         40         50
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV
60 70 80 90 100
TTVEAAVAYR QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT
110 120 130 140 150
AAKLYPANAT TNSSHGVTSI DAIMPVLERM EKIGMPLLVH GEVTHADIDI
160 170 180 190 200
FDREARFIES VMEPLRQRLT ALKVVFEHIT TKDAADYVRD GNERLAATIT
210 220 230 240 250
PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA SGFNRVFLGT
260 270 280 290 300
DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG
310 320 330 340
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
Length:348
Mass (Da):38,827
Last modified:January 23, 2007 - v2
Checksum:i179B35324204A111
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000126534.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74146; AAC74146; b1062.
BAA35870; BAA35870; BAA35870.
GeneIDi945787.
KEGGiecj:JW1049.
eco:b1062.
PATRICi32117363. VBIEscCol129921_1104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000126534.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP05020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261761. 17 interactors.
DIPiDIP-10624N.
IntActiP05020. 6 interactors.
STRINGi511145.b1062.

Chemistry databases

BindingDBiP05020.

Protein family/group databases

MEROPSiM38.A02.

Proteomic databases

PaxDbiP05020.
PRIDEiP05020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74146; AAC74146; b1062.
BAA35870; BAA35870; BAA35870.
GeneIDi945787.
KEGGiecj:JW1049.
eco:b1062.
PATRICi32117363. VBIEscCol129921_1104.

Organism-specific databases

EchoBASEiEB0799.
EcoGeneiEG10806. pyrC.

Phylogenomic databases

eggNOGiENOG4105EKE. Bacteria.
COG0418. LUCA.
HOGENOMiHOG000256259.
InParanoidiP05020.
KOiK01465.
OMAiYAEAFEQ.
PhylomeDBiP05020.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP05020.
PROiP05020.

Family and domain databases

CDDicd01294. DHOase. 1 hit.
HAMAPiMF_00219. PyrC_type1. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.