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A7MJ89 (PUR9_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:ESA_03670
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

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_1000018890

Sequences

Sequence LengthMass (Da)Tools
A7MJ89 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 182CEDC641DC3B73

FASTA52957,244
        10         20         30         40         50         60 
MQQPRPVRRA LLSVSDKAGI VDFARALSTR GVELLSTGGT ARLLAEAGLP VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGQDDDIM AQHAISPIDM VVVNLYPFAQ TVAREGCTLE 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYTAIIDEL DANNGSLTFD TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAAYDSMI ANYFGSLVPA YHGETTAPAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI 

       250        260        270        280        290        300 
EEEIKEASVA TARQVQGKAL SYNNIADTDA ALECVKEFSE PACVIVKHAN PCGVAVSSSI 

       310        320        330        340        350        360 
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIVSRQFV EVIIAPSASD DALKITAAKQ 

       370        380        390        400        410        420 
NVRVLVCGEW QSRVPGLDFK RVNGGLLVQD RDLGMVTEAD LRVVTKRQPT EQELRDALFC 

       430        440        450        460        470        480 
WKVAKFVKSN AIVYARDNMT IGIGAGQMSR VYSAKIAGIK AGDEGLEVKG SAMASDAFFP 

       490        500        510        520 
FRDGIDAAAA VGITCVIQPG GSIRDDEVIA AADEHGIAMI FTDMRHFRH 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU78874.1.
RefSeqYP_001439710.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MJ89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290339.ESA_03670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU78874; ABU78874; ESA_03670.
GeneID5550524.
KEGGesa:ESA_03670.
PATRIC20399029. VBICroSak107175_3267.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCSAK290339:GJ80-3659-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_CROS8
AccessionPrimary (citable) accession number: A7MJ89
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: May 14, 2014
This is version 44 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