Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroorotase

Gene

pyrC

Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 small chain (carA), Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (carB)
  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 bindingi17 – 171Zinc 1; via tele nitrogenUniRule annotation
Metal bindingi19 – 191Zinc 1; via tele nitrogenUniRule annotation
Metal bindingi103 – 1031Zinc 1; via carbamate groupUniRule annotation
Metal bindingi103 – 1031Zinc 2; via carbamate groupUniRule annotation
Metal bindingi140 – 1401Zinc 2; via pros nitrogenUniRule annotation
Metal bindingi178 – 1781Zinc 2; via tele nitrogenUniRule annotation
Metal bindingi251 – 2511Zinc 1UniRule annotation

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

BioCyciYPSE273123:GI1M-2569-MONOMER.
UniPathwayiUPA00070; UER00117.

Protein family/group databases

MEROPSiM38.A02.

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:YPTB2482
OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
Taxonomic identifieri273123 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
Proteomesi
  • UP000001011 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348DihydroorotasePRO_1000024077Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ669K2.
SMRiQ669K2. Positions 6-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000256259.
KOiK01465.
OMAiYAEAFEQ.

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.
PROSITEiPS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q669K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAQPQTLKI RRPDDWHIHL RDDEMLSTVL PYTSEVFARA IVMPNLAQPI
60 70 80 90 100
TTVASAIAYR ERILAAVPAG HKFTPLMTCY LTNSLDVKEL TTGFEQGVFT
110 120 130 140 150
AAKLYPANAT TNSTHGVSDI PAIYPLFEQM QKIGMPLLIH GEVTDAAVDI
160 170 180 190 200
FDREARFIDQ ILEPIRQKFP ELKIVFEHIT TKDAADYVLA GNRFLGATVT
210 220 230 240 250
PQHLMFNRNH MLVGGIRPHL FCLPILKRST HQQALRAAVA SGSDRFFLGT
260 270 280 290 300
DSAPHAKHRK ESSCGCAGVF NAPAALPAYA SVFEELNALQ HLEAFCALNG
310 320 330 340
PRFYGLPVND DVVELVRTPF LQPEEIPLGN ESVIPFLAGQ TLNWSVKR
Length:348
Mass (Da):38,570
Last modified:October 11, 2004 - v1
Checksum:iB92B613E026ED571
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH21720.1.
RefSeqiWP_011192610.1. NZ_CP009712.1.

Genome annotation databases

EnsemblBacteriaiCAH21720; CAH21720; YPTB2482.
KEGGiypo:BZ17_4155.
yps:YPTB2482.
PATRICi18643929. VBIYerPse22266_3022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH21720.1.
RefSeqiWP_011192610.1. NZ_CP009712.1.

3D structure databases

ProteinModelPortaliQ669K2.
SMRiQ669K2. Positions 6-347.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM38.A02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH21720; CAH21720; YPTB2482.
KEGGiypo:BZ17_4155.
yps:YPTB2482.
PATRICi18643929. VBIYerPse22266_3022.

Phylogenomic databases

HOGENOMiHOG000256259.
KOiK01465.
OMAiYAEAFEQ.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
BioCyciYPSE273123:GI1M-2569-MONOMER.

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.
PROSITEiPS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRC_YERPS
AccessioniPrimary (citable) accession number: Q669K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2004
Last modified: September 7, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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.