UniProtKB - P05020 (PYRC_ECOLI)
Protein
Dihydroorotase
Gene
pyrC
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.UniRule annotation2 Publications
Catalytic activityi
- EC:3.5.2.3UniRule annotation2 Publications
Cofactori
Zn2+UniRule annotation5 PublicationsNote: Binds 2 Zn2+ ions per subunit (PubMed:6142052, PubMed:11401542, PubMed:15826651). In vitro, can also use Co2+ or Cd2+ (PubMed:1671037, PubMed:15610022).5 Publications
Kineticsi
kcat is 127 sec(-1) with dihydroorotate as substrate and 195 sec(-1) with N-carbamoyl-DL-aspartate as substrate (PubMed:6142052). kcat is 100 sec(-1) with dihydroorotate as substrate and 160 sec(-1) with carbamoyl aspartate as substrate in the presence of Zn2+. kcat is 15 sec(-1) with dihydroorotate as substrate and 25 sec(-1) with carbamoyl aspartate as substrate in the presence of Co2+. kcat is 1.9 sec(-1) with dihydroorotate as substrate and 8.2 sec(-1) with carbamoyl aspartate as substrate in the presence of Cd2+ (PubMed:15610022).2 Publications
- KM=0.0756 mM for dihydroorotate1 Publication
- KM=0.080 mM for dihydroorotate (in the presence of Zn2+)1 Publication
- KM=0.70 mM for dihydroorotate (in the presence of Co2+)1 Publication
- KM=0.23 mM for dihydroorotate (in the presence of Cd2+)1 Publication
- KM=1.07 mM for N-carbamoyl-DL-aspartate1 Publication
- KM=1.70 mM for carbamoyl aspartate (in the presence of Zn2+)1 Publication
- KM=15 mM for carbamoyl aspartate (in the presence of Co2+)1 Publication
- KM=4.0 mM for carbamoyl aspartate (in the presence of Cd2+)1 Publication
: UMP biosynthesis via de novo pathway Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotationCuratedProteins known to be involved in the 3 steps of the subpathway in this organism are:
- Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
- Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase catalytic subunit (pyrB)
- Dihydroorotase (pyrC), Dihydroorotase (pyrC)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 17 | Zinc 1; via tele nitrogenUniRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 19 | Zinc 1; via tele nitrogenUniRule annotationCombined sources2 Publications | 1 | |
Binding sitei | 45 | SubstrateUniRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 103 | Zinc 1; via carbamate groupUniRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 103 | Zinc 2; via carbamate groupUniRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 140 | Zinc 2; via pros nitrogenUniRule annotationCombined sources2 Publications | 1 | |
Binding sitei | 140 | SubstrateUniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 178 | Zinc 2; via tele nitrogenUniRule annotationCombined sources2 Publications | 1 | |
Binding sitei | 223 | Substrate; via amide nitrogen and carbonyl oxygenUniRule annotationCombined sources2 Publications | 1 | |
Active sitei | 251 | UniRule annotation1 Publication | 1 | |
Metal bindingi | 251 | Zinc 1UniRule annotationCombined sources2 Publications | 1 | |
Binding sitei | 255 | SubstrateUniRule annotationCombined sources2 Publications | 1 | |
Binding sitei | 267 | Substrate; via carbonyl oxygenUniRule annotationCombined sources2 Publications | 1 |
GO - Molecular functioni
- dihydroorotase activity Source: EcoCyc
- zinc ion binding Source: EcoCyc
GO - Biological processi
- 'de novo' pyrimidine nucleobase biosynthetic process Source: EcoCyc
- 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
- pyrimidine nucleotide biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Hydrolase |
Biological process | Pyrimidine biosynthesis |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:DIHYDROOROT-MONOMER MetaCyc:DIHYDROOROT-MONOMER |
BRENDAi | 3.5.2.3, 2026 |
SABIO-RKi | P05020 |
UniPathwayi | UPA00070;UER00117 |
Protein family/group databases
MEROPSi | M38.A02 |
Names & Taxonomyi
Protein namesi | Recommended name: DihydroorotaseUniRule annotation (EC:3.5.2.3UniRule annotation2 Publications)Short name: DHOaseUniRule annotation |
Gene namesi | Name:pyrC1 PublicationUniRule annotation Ordered Locus Names:b1062, JW1049 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 21 | R → K: 9-fold decrease in catalytic efficiency with carbamoyl aspartate as substrate. 1 Publication | 1 | |
Mutagenesisi | 21 | R → M or Q: Lack of activity. 1 Publication | 1 | |
Mutagenesisi | 45 | N → A: Lack of activity. 1 Publication | 1 | |
Mutagenesisi | 251 | D → A, H or N: Lack of activity. 1 Publication | 1 | |
Mutagenesisi | 251 | D → E: 24-fold decrease in catalytic efficiency with carbamoyl aspartate as substrate. 1 Publication | 1 | |
Mutagenesisi | 251 | D → S: 3500-fold decrease in catalytic efficiency with carbamoyl aspartate as substrate. 1 Publication | 1 | |
Mutagenesisi | 255 | H → N: Lack of activity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB02129, Dihydroorotic Acid DB03801, Lysine Nz-Carboxylic Acid DB04252, N-Carbamoylaspartic acid DB02262, Orotic acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000147205 | 2 – 348 | DihydroorotaseAdd BLAST | 347 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 103 | N6-carboxylysineUniRule annotationCombined sources2 Publications | 1 |
Proteomic databases
jPOSTi | P05020 |
PaxDbi | P05020 |
PRIDEi | P05020 |
Expressioni
Inductioni
Induced by pyrimidine limitation.1 Publication
Interactioni
Subunit structurei
Homodimer.
UniRule annotation3 PublicationsProtein-protein interaction databases
BioGRIDi | 4261761, 32 interactors 850154, 4 interactors |
DIPi | DIP-10624N |
IntActi | P05020, 6 interactors |
STRINGi | 511145.b1062 |
Chemistry databases
BindingDBi | P05020 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P05020 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05020 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 19 – 21 | Substrate bindingUniRule annotationCombined sources2 Publications | 3 |
Domaini
There is an asymmetry between active sites in the dimer, with dihydroorotate bound to the active site of subunit A and N-carbamoyl-L-aspartate bound to the active site of subunit B.1 Publication
Sequence similaritiesi
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.UniRule annotationCurated
Phylogenomic databases
eggNOGi | COG0418, Bacteria |
HOGENOMi | CLU_041558_1_0_6 |
InParanoidi | P05020 |
PhylomeDBi | P05020 |
Family and domain databases
CDDi | cd01294, DHOase, 1 hit |
HAMAPi | MF_00219, PyrC_classII, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR004721, DHOdimr IPR002195, Dihydroorotase_CS IPR032466, Metal_Hydrolase |
PANTHERi | PTHR43137, PTHR43137, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
PIRSFi | PIRSF001237, DHOdimr, 1 hit |
SUPFAMi | SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR00856, pyrC_dimer, 1 hit |
PROSITEi | View protein in PROSITE PS00482, DIHYDROOROTASE_1, 1 hit PS00483, DIHYDROOROTASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P05020-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | A25008, DEECOO |
RefSeqi | NP_415580.1, NC_000913.3 WP_000126534.1, NZ_SSZK01000053.1 |
Genome annotation databases
EnsemblBacteriai | AAC74146; AAC74146; b1062 BAA35870; BAA35870; BAA35870 |
GeneIDi | 57731849 945787 |
KEGGi | ecj:JW1049 eco:b1062 |
PATRICi | fig|1411691.4.peg.1206 |
Similar proteinsi
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 |
PIRi | A25008, DEECOO |
RefSeqi | NP_415580.1, NC_000913.3 WP_000126534.1, NZ_SSZK01000053.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
6HG1 | X-ray | 2.12 | A | 107-119 | [»] | |
SMRi | P05020 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261761, 32 interactors 850154, 4 interactors |
DIPi | DIP-10624N |
IntActi | P05020, 6 interactors |
STRINGi | 511145.b1062 |
Chemistry databases
BindingDBi | P05020 |
DrugBanki | DB02129, Dihydroorotic Acid DB03801, Lysine Nz-Carboxylic Acid DB04252, N-Carbamoylaspartic acid DB02262, Orotic acid |
Protein family/group databases
MEROPSi | M38.A02 |
Proteomic databases
jPOSTi | P05020 |
PaxDbi | P05020 |
PRIDEi | P05020 |
Genome annotation databases
EnsemblBacteriai | AAC74146; AAC74146; b1062 BAA35870; BAA35870; BAA35870 |
GeneIDi | 57731849 945787 |
KEGGi | ecj:JW1049 eco:b1062 |
PATRICi | fig|1411691.4.peg.1206 |
Organism-specific databases
EchoBASEi | EB0799 |
Phylogenomic databases
eggNOGi | COG0418, Bacteria |
HOGENOMi | CLU_041558_1_0_6 |
InParanoidi | P05020 |
PhylomeDBi | P05020 |
Enzyme and pathway databases
UniPathwayi | UPA00070;UER00117 |
BioCyci | EcoCyc:DIHYDROOROT-MONOMER MetaCyc:DIHYDROOROT-MONOMER |
BRENDAi | 3.5.2.3, 2026 |
SABIO-RKi | P05020 |
Miscellaneous databases
EvolutionaryTracei | P05020 |
PROi | PR:P05020 |
Family and domain databases
CDDi | cd01294, DHOase, 1 hit |
HAMAPi | MF_00219, PyrC_classII, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR004721, DHOdimr IPR002195, Dihydroorotase_CS IPR032466, Metal_Hydrolase |
PANTHERi | PTHR43137, PTHR43137, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
PIRSFi | PIRSF001237, DHOdimr, 1 hit |
SUPFAMi | SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR00856, pyrC_dimer, 1 hit |
PROSITEi | View protein in PROSITE PS00482, DIHYDROOROTASE_1, 1 hit PS00483, DIHYDROOROTASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PYRC_ECOLI | |
Accessioni | P05020Primary (citable) accession number: P05020 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 13, 1987 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 184 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families