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Reviewed, UniProtKB/Swiss-Prot Q5E1R3 (PURK_VIBF1)

Last modified February 9, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoribosylaminoimidazole carboxylase ATPase subunit
    EC=4.1.1.21
Alternative name(s):
    AIR carboxylase
      Short name=AIRC
Gene names
Name: purK
Ordered Locus Names: VF_2538
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Complete proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Possesses an ATPase activity that is dependent on the presence of AIR (aminoimidazole ribonucleotide). The association of purK and purE produces an enzyme complex capable of converting AIR to CAIR efficiently under physiological condition By similarity.

Catalytic activity

5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the purK/purT family.

Contains 1 ATP-grasp domain.

Ontologies

Keywords
   Biological processPurine biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylaminoimidazole carboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Phosphoribosylaminoimidazole carboxylase ATPase subunit
PRO_0000075016

Regions

Domain97 – 288192ATP-grasp
Nucleotide binding175 – 1784ATP By similarity
Nucleotide binding258 – 2592ATP By similarity

Sites

Binding site931ATP By similarity
Binding site1331ATP By similarity
Binding site1441ATP By similarity
Binding site1831ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E1R3-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 797F90E7489AD36F

FASTA37040,933
        10         20         30         40         50         60 
MNVLILGSGQ LARMMSLASA PLNIDVIAYD VNSQQIVHPL TQQPIDLSLE QAIKQVDVIT 

        70         80         90        100        110        120 
AEFEHIPHHI LDICSVSGKF QPTPDAIKAG GDRRLEKKLL DNAHVANAKY HNINTKQDFL 

       130        140        150        160        170        180 
NAIDTVGIPM VLKSALGGYD GKGQWRLKDV SQVDSIWEEM DELIKSSPNQ AIVAEQFIPF 

       190        200        210        220        230        240 
NREVSLIGAR NKNGQMVTYP LTENVHVDGV LALSTALEGT SNLQQQADEM FTAIADELNY 

       250        260        270        280        290        300 
IGVLAIEFFD VDGTLLVNEI APRVHNSGHW TQQGTDICQF EMHIRAVCNL PLTGNQLLRS 

       310        320        330        340        350        360 
TAMINILGED SLPDEILTMP NCHIHWYGKE KRAGRKMGHI NVCADSPEML QKELSKLANI 

       370 
LDKQAFKALS 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed: 15703294] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW87033.1.
RefSeqYP_205921.1.

3D structure databases

SMRQ5E1R3. Positions 1-362.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5E1R3.

Genome annotation databases

GeneID3279691.
GenomeReviewsGene locus VF_2538 in contig CP000020_GR.
KEGGvfi:VF_2538.
NMPDRfig|312309.3.peg.2538.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0026.
HOGENOMHBG516369.
OMAYDGKGQA.
PhylomeDBQ5E1R3.

Enzyme and pathway databases

BioCycVFIS312309:VF2538-MONOMER.

Family and domain databases

InterProIPR005875. AIR_COase_ATPase-su.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013816. ATP_grasp_subdomain_2.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
PANTHERPTHR23047:SF1. PurK_ATP. 1 hit.
PfamPF02222. ATP-grasp. 1 hit.
[Graphical view]
TIGRFAMsTIGR01161. purK. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURK_VIBF1
AccessionPrimary (citable) accession number: Q5E1R3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 15, 2005
Last modified: February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents