Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UZ35 (PYRF_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orotidine 5'-phosphate decarboxylase

EC=4.1.1.23
Alternative name(s):
OMP decarboxylase
Short name=OMPDCase
Short name=OMPdecase
Gene names
Name:pyrF
Ordered Locus Names:PYRAB13190
ORF Names:PAB1505
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) By similarity. HAMAP-Rule MF_01200

Catalytic activity

Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01200

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. HAMAP-Rule MF_01200

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01200

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionorotidine-5'-phosphate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134614

Regions

Region57 – 6610Substrate binding By similarity
Region162 – 17211Substrate binding By similarity

Sites

Active site591Proton donor By similarity
Binding site71Substrate By similarity
Binding site291Substrate By similarity
Binding site1091Substrate By similarity
Binding site1851Substrate; via amide nitrogen By similarity
Binding site1861Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UZ35 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B993BF06CD61A9BC

FASTA20822,991
        10         20         30         40         50         60 
MIVLALDVYD EDRALKIAEE TKDYVAMIKV NWPLIIGSGL DIIRKLKDRT GLKIIADLKL 

        70         80         90        100        110        120 
ADIPNTNKLI ARKVYEAGAD YIIVHPFVGR DSVEAVNELG EIILVVEMSH PGALEFINPL 

       130        140        150        160        170        180 
TDKFIELAND VEPFGVIAPG TRPERVKYIR ERLKEGVKIL TPGIGAQGGK AKEAIEAGAD 

       190        200 
YVIVGRSIYN APNPREAARE IYDEIRGE 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248287 Genomic DNA. Translation: CAB50224.1.
HE613800 Genomic DNA. Translation: CCE70760.1.
PIRC75041.
RefSeqNP_126994.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UZ35.
SMRQ9UZ35. Positions 1-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50224; CAB50224; PAB1505.
GeneID1496706.
KEGGpab:PAB1505.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226069.
KOK01591.
OMATEMSHPG.

Enzyme and pathway databases

UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_A. OMPdecase_type1_A.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRF_PYRAB
AccessionPrimary (citable) accession number: Q9UZ35
Secondary accession number(s): G8ZHC3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways