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Protein

Dihydroorotase

Gene

pyrC

Organism
Burkholderia pseudomallei (strain 1106a)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.UniRule annotationSAAS 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 annotationSAAS annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (pyrC), 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 bindingi18Zinc 1; via tele nitrogenUniRule annotation1
Metal bindingi20Zinc 1; via tele nitrogenUniRule annotation1
Metal bindingi104Zinc 1; via carbamate groupUniRule annotation1
Metal bindingi104Zinc 2; via carbamate groupUniRule annotation1
Metal bindingi142Zinc 2; via pros nitrogenUniRule annotation1
Metal bindingi180Zinc 2; via tele nitrogenUniRule annotation1
Metal bindingi256Zinc 1UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Pyrimidine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

Metal-bindingUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
DihydroorotaseUniRule annotationSAAS annotation (EC:3.5.2.3UniRule annotationSAAS annotation)
Short name:
DHOaseUniRule annotation
Gene namesi
Name:pyrCUniRule annotationImported
Ordered Locus Names:BURPS1106A_3417Imported
OrganismiBurkholderia pseudomallei (strain 1106a)Imported
Taxonomic identifieri357348 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000006738 Componenti: Chromosome I

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei104N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliA3NZ83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 318Amidohydro-relInterPro annotationAdd BLAST303

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000256259.
KOiK01465.
OMAiYAEAFEQ.

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.

A3NZ83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNASVPASLT LARPDDWHLH VRDGAMLAAV LPHTARQFGR AIIMPNLKPP
60 70 80 90 100
VTTTAQAQAY RERILAAVPA GMTFEPLMTL YLTDNTPADE IRRARESGCV
110 120 130 140 150
HGVKLYPAGA TTNSDAGVTD LLGKCAKTLE AMQEVGMPLL VHGEVTDPSI
160 170 180 190 200
DLFDREKVFI DRVMEPLRRA LPGLKVVFEH ITTKDAADYV RDADAASGRI
210 220 230 240 250
GATITAHHLL YNRNAMFFGG IRPHYYCLPV LKRETHRIAL VEAATSGNPR
260 270 280 290 300
FFLGTDSAPH AKGAKEAACG CAGCYTALHA LELYAEAFDQ AGALDKLEGF
310 320 330 340 350
ASFFGADFYG LPRSAETVTL RRETWELPRE IDAGAGPVVP LRGGEAIGWR

LV
Length:352
Mass (Da):38,178
Last modified:April 3, 2007 - v1
Checksum:i88B2B9B04EB1F241
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000572 Genomic DNA. Translation: ABN92544.1.
RefSeqiWP_004194429.1. NC_009076.1.

Genome annotation databases

EnsemblBacteriaiABN92544; ABN92544; BURPS1106A_3417.
KEGGibpl:BURPS1106A_3417.
PATRICi19225163. VBIBurPse14980_3225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000572 Genomic DNA. Translation: ABN92544.1.
RefSeqiWP_004194429.1. NC_009076.1.

3D structure databases

ProteinModelPortaliA3NZ83.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN92544; ABN92544; BURPS1106A_3417.
KEGGibpl:BURPS1106A_3417.
PATRICi19225163. VBIBurPse14980_3225.

Phylogenomic databases

HOGENOMiHOG000256259.
KOiK01465.
OMAiYAEAFEQ.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.

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 nameiA3NZ83_BURP0
AccessioniPrimary (citable) accession number: A3NZ83
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.