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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: -Protein inferred from homologyi

Functioni

Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotation
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)DescriptionActionsGraphical viewLength
Metal bindingi14Zinc 1; via tele nitrogenUniRule annotation1
Metal bindingi16Zinc 1; via tele nitrogenUniRule annotation1
Binding sitei42SubstrateUniRule annotation1
Metal bindingi100Zinc 1; via carbamate groupUniRule annotation1
Metal bindingi100Zinc 2; via carbamate groupUniRule annotation1
Metal bindingi137Zinc 2; via pros nitrogenUniRule annotation1
Binding sitei137SubstrateUniRule annotation1
Metal bindingi175Zinc 2; via tele nitrogenUniRule annotation1
Binding sitei220Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1
Active sitei248UniRule annotation1
Metal bindingi248Zinc 1UniRule annotation1
Binding sitei252SubstrateUniRule annotation1
Binding sitei264Substrate; via carbonyl oxygenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyrimidine biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-3595-MONOMER
BRENDAi3.5.2.3 5087
UniPathwayiUPA00070; UER00117

Names & Taxonomyi

Protein namesi
Recommended name:
DihydroorotaseUniRule annotation (EC:3.5.2.3UniRule annotation)
Short name:
DHOaseUniRule annotation
Gene namesi
Name:pyrCUniRule annotation
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

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001472121 – 348DihydroorotaseAdd BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei100N6-carboxylysineUniRule annotation1

Proteomic databases

PaxDbiP72170

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA3527

Structurei

3D structure databases

ProteinModelPortaliP72170
SMRiP72170
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni16 – 18Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EKE Bacteria
COG0418 LUCA
HOGENOMiHOG000256259
InParanoidiP72170
KOiK01465
OMAiHLRDGAM
PhylomeDBiP72170

Family and domain databases

CDDicd01294 DHOase, 1 hit
HAMAPiMF_00219 PyrC_classII, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR004721 DHOdimr
IPR002195 Dihydroorotase_CS
IPR032466 Metal_Hydrolase
PANTHERiPTHR43137 PTHR43137, 1 hit
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
PIRSFiPIRSF001237 DHOdimr, 1 hit
SUPFAMiSSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR00856 pyrC_dimer, 1 hit
PROSITEiView protein in PROSITE
PS00482 DIHYDROOROTASE_1, 1 hit
PS00483 DIHYDROOROTASE_2, 1 hit

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, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG06915; AAG06915; PA3527
GeneIDi879809
KEGGipae:PA3527
PATRICifig|208964.12.peg.3691

Similar proteinsi

Entry informationi

Entry nameiPYRC_PSEAE
AccessioniPrimary (citable) accession number: P72170
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: February 28, 2018
This is version 120 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome