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Q5E257 (PUR9_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:VF_2394
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

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

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192145

Sequences

Sequence LengthMass (Da)Tools
Q5E257 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: A5E5752E7EAFE284

FASTA53057,625
        10         20         30         40         50         60 
MNNARPIRRA LISVSDKTGI VEFAQALAER GVDILSTGGT ARLLAEKGIS VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGVL GRRGQDDDIM EQHGINPIDM VVVNLYPFAE TVAKEGCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVTIVVNA HDYDRVIAEM DANEKSLTLE TRFDLAIAAF 

       190        200        210        220        230        240 
EHTASYDGMI ANYFGTMVPS YGENKEGDEE SKFPRTFNQQ FEKKQDMRYG ENSHQAAAFY 

       250        260        270        280        290        300 
VEANPEEASV STARQIQGKA LSYNNIADTD AALECVKEFD EPACVIVKHA NPCGVALGKD 

       310        320        330        340        350        360 
ILEAYDRAFK TDPTSAFGGI IAFNRELDAA TATAITERQF VEVIIAPSVS TEAVEIVAAK 

       370        380        390        400        410        420 
KNLRLLECGE WTTKTTGFDV KRVNGGLLVQ DRDQGMVSED DLQVVSKRQP TAEELKDALF 

       430        440        450        460        470        480 
CWKVAKYVKS NAIVYSKGDM TIGVGAGQMS RVYSAKIAGI KAADEGLQVE GCVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA EAGIKCVIQP GGSMRDNEVI EAADEHGMAM IFTGMRHFRH 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW86889.1.
RefSeqYP_205777.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_2394.

Proteomic databases

PRIDEQ5E257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW86889; AAW86889; VF_2394.
GeneID3278353.
KEGGvfi:VF_2394.
PATRIC20115540. VBIVibFis127983_2429.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycAFIS312309:GIWP-2521-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_VIBF1
AccessionPrimary (citable) accession number: Q5E257
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: March 15, 2005
Last modified: May 14, 2014
This is version 64 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