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B5FQM1 (PUR9_SALDC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 46. 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:SeD_A4583
OrganismSalmonella dublin (strain CT_02021853) [Complete proteome] [HAMAP]
Taxonomic identifier439851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length529 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096089

Sequences

Sequence LengthMass (Da)Tools
B5FQM1 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: DF0F123009E81F6C

FASTA52957,427
        10         20         30         40         50         60 
MQQRRPVRRA LLSVSDKAGI IEFAQALSAR GVELLSTGGT ARLLAEKGLA VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EQHHIAPIDM VVVNLYPFAE TVAREGCSLE 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIIKEM DANEGSLTLD TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAAYDSMI ANYFGSMVPA YHGESKEAAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI 

       250        260        270        280        290        300 
EENVKEASVA TAQQVQGKAL SYNNIADTDA ALECVKEFNE PACVIVKHAN PCGVAVSTTI 

       310        320        330        340        350        360 
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSATE DALKITAAKQ 

       370        380        390        400        410        420 
NVRVLTCGQW AQRVPGLDFK RVNGGLLVQD RDLGMVSEAE LRVVSKRQPT EQELRDALFC 

       430        440        450        460        470        480 
WKVAKFVKSN AIVYAKENMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SAMASDAFFP 

       490        500        510        520 
FRDGIDAAAA VGVSCVIQPG GSIRDDEVIA AADEHGIAMI FTDMRHFRH 

« Hide

References

[1]"Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT_02021853.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001144 Genomic DNA. Translation: ACH76450.1.
RefSeqYP_002218092.1. NC_011205.1.

3D structure databases

ProteinModelPortalB5FQM1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439851.SeD_A4583.

Proteomic databases

PRIDEB5FQM1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH76450; ACH76450; SeD_A4583.
PATRIC18497208. VBISalEnt111443_4482.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSENT439851:GH2Z-4526-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_SALDC
AccessionPrimary (citable) accession number: B5FQM1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 46 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