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Protein

Dihydroorotase

Gene

pyrC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

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 (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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Zinc 1; via tele nitrogenBy similarity
Metal bindingi16 – 161Zinc 1; via tele nitrogenBy similarity
Metal bindingi100 – 1001Zinc 1; via carbamate groupBy similarity
Metal bindingi100 – 1001Zinc 2; via carbamate groupBy similarity
Metal bindingi137 – 1371Zinc 2; via pros nitrogenBy similarity
Metal bindingi175 – 1751Zinc 2; via tele nitrogenBy similarity
Metal bindingi248 – 2481Zinc 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.3. 5087.
UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotase (EC:3.5.2.3)
Short name:
DHOase
Gene namesi
Name:pyrC
Ordered Locus Names:PA3527
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348DihydroorotasePRO_0000147212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-carboxylysineBy similarity

Proteomic databases

PaxDbiP72170.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi208964.PA3527.

Structurei

3D structure databases

ProteinModelPortaliP72170.
SMRiP72170. Positions 5-343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Type 1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105EKE. Bacteria.
COG0418. LUCA.
HOGENOMiHOG000256259.
InParanoidiP72170.
KOiK01465.
OMAiYAEAFEQ.
PhylomeDBiP72170.

Family and domain databases

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.

P72170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDRLTLLRP DDWHIHLRDG AALANTVGDA ARTFGRAIVM PNLVPPVRNA
60 70 80 90 100
AEADAYRQRI LAARPAASRF EPLMVLYLTD RTSTEEIRTA KASGFVHAAK
110 120 130 140 150
LYPAGATTNS DSGVTRIDNI FEALEAMAEV GMPLLVHGEV TRAEVDVFDR
160 170 180 190 200
EKQFIDEHLR RVVERFPTLK VVFEHITTGD AAQFVREAPA NVGATITAHH
210 220 230 240 250
LLYNRNHMLV GGIRPHFYCL PILKRNTHQE ALLDAAVSGN PKFFLGTDSA
260 270 280 290 300
PHARHAKEAA CGCAGCYSAY AAIELYAEAF EQRNALDKLE GFASLHGPDF
310 320 330 340
YGLPRNTDRI TLVREEWQAP ASLPFGDFDV VPLRAGETLR WKLLEAGA
Length:348
Mass (Da):38,407
Last modified:May 30, 2000 - v2
Checksum:i6E3EF751A5B4DDB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73505 Genomic DNA. Translation: AAC73109.1.
AE004091 Genomic DNA. Translation: AAG06915.1.
PIRiT10453.
RefSeqiNP_252217.1. NC_002516.2.
WP_003112889.1. NZ_ASJY01000572.1.

Genome annotation databases

EnsemblBacteriaiAAG06915; AAG06915; PA3527.
GeneIDi879809.
KEGGipae:PA3527.
PATRICi19841667. VBIPseAer58763_3691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73505 Genomic DNA. Translation: AAC73109.1.
AE004091 Genomic DNA. Translation: AAG06915.1.
PIRiT10453.
RefSeqiNP_252217.1. NC_002516.2.
WP_003112889.1. NZ_ASJY01000572.1.

3D structure databases

ProteinModelPortaliP72170.
SMRiP72170. Positions 5-343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3527.

Proteomic databases

PaxDbiP72170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06915; AAG06915; PA3527.
GeneIDi879809.
KEGGipae:PA3527.
PATRICi19841667. VBIPseAer58763_3691.

Organism-specific databases

PseudoCAPiPA3527.

Phylogenomic databases

eggNOGiENOG4105EKE. Bacteria.
COG0418. LUCA.
HOGENOMiHOG000256259.
InParanoidiP72170.
KOiK01465.
OMAiYAEAFEQ.
PhylomeDBiP72170.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
BRENDAi3.5.2.3. 5087.

Family and domain databases

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_PSEAE
AccessioniPrimary (citable) accession number: P72170
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: September 7, 2016
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.