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A7GYY6 (PUR9_CAMC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Ccur92_11240
ORF Names:CCV52592_1838
OrganismCampylobacter curvus (strain 525.92) [Complete proteome] [HAMAP]
Taxonomic identifier360105 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length510 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 – 510510Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018868

Sequences

Sequence LengthMass (Da)Tools
A7GYY6 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 0E25DBA5862106AF

FASTA51056,584
        10         20         30         40         50         60 
MRALISVSDK EGVVEFAKGL EQLGWQIVST GGTYKILNEN GVKAVEVAQI TQSPEMFEGR 

        70         80         90        100        110        120 
VKTLHPKIHG GILYKRDDAS HVAQAKEFGI EGIDLVCVNL YPFKETTIRT DDFDEIIENI 

       130        140        150        160        170        180 
DIGGPAMVRS AAKNFKDVLI VTSVLDYDEI LQRLKEGTDD LEFRRNLMIK AYEHTASYDA 

       190        200        210        220        230        240 
TIANYMNERF KGGFGDARFI FGNKVFDTRY GENPHQKGAL YEFEYFFTNN FRALKGEASF 

       250        260        270        280        290        300 
NNMTDINGAV MLATSFENAP VVAIVKHSNP CGLAVKDSLL ESYVEALKCD PISAYGGVVA 

       310        320        330        340        350        360 
INGTLDRALA RKINEIYVEV IIAANVDDDA LAVFENKKRI KIFTQDNKFL VRAGDKFDFK 

       370        380        390        400        410        420 
HIDGGFVFQE RDVVSDDELK NMKQMSKKHA NENQLKDAQI AWKVAALTKS NCVVYVKDGA 

       430        440        450        460        470        480 
MVAIGMGMTS RVDAARAAVA KAKELDLDLH GCVLASEAFF PFRDSIDIAS KVGVKCVIEP 

       490        500        510 
GGSIRDDEVI EAANEHGMSL YFTGVRHFLH 

« Hide

References

[1]"Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 525.92.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000767 Genomic DNA. Translation: EAU00271.1.
RefSeqYP_001408428.1. NC_009715.1.

3D structure databases

ProteinModelPortalA7GYY6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360105.CCV52592_1838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAU00271; EAU00271; CCV52592_1838.
GeneID5406548.
KEGGccv:CCV52592_1838.
PATRIC20032752. VBICamCur47627_1183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycCCUR360105:GJ9P-1223-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_CAMC5
AccessionPrimary (citable) accession number: A7GYY6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 45 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