Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A8AUA2 (PUR9_STRGC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:SGO_0040
OrganismStreptococcus gordonii (strain Challis / ATCC 35105 / CH1 / DL1 / V288) [Complete proteome] [HAMAP]
Taxonomic identifier29390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length515 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 – 515515Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076499

Sequences

Sequence LengthMass (Da)Tools
A8AUA2 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: C626F11A8972428B

FASTA51556,348
        10         20         30         40         50         60 
MTKRALISVS DKAGIVEFAQ ELKKLGWEII STGGTKVALD SAGVETIAID DVTGFPEMMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLARRDL DSHLEAAKDN NIELIDLVVV NLYPFKETIL KPDVTYADAV 

       130        140        150        160        170        180 
ENIDIGGPSM LRSAAKNHAS VTVVVDPADY AVVLDELSAN GETTYETRQR LAAKVFRHTA 

       190        200        210        220        230        240 
AYDALIAEYF TAQVGESKPE KLTLTYDLKQ AMRYGENPQQ DADFYQKALP TDYSIASAKQ 

       250        260        270        280        290        300 
LNGKELSFNN IRDADAAIRI IRDFKYRPTV VALKHMNPCG IGQADDIKTA WDYAYESDPV 

       310        320        330        340        350        360 
SIFGGIVVLN REVDAATAEK MHGVFLEIII APSYTDEALA ILTNKKKNLR ILALPFDAQE 

       370        380        390        400        410        420 
ASEVEAEYTG VVGGLLVQNQ DVVKESPADW QVVTKRQPTE TEATALEFAW KAIKYVKSNG 

       430        440        450        460        470        480 
IIVTNDHMTL GVGPGQTNRV ASVRIAIDQA KDRLDGAVLA SDAFFPFADN VEEIAKAGIK 

       490        500        510 
AIIQPGGSVR DQESIEAADK YGLTMVFTGV RHFRH 

« Hide

References

[1]"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
J. Bacteriol. 189:7799-7807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Challis / ATCC 35105 / CH1 / DL1 / V288.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000725 Genomic DNA. Translation: ABV10508.1.
RefSeqYP_001449362.1. NC_009785.1.

3D structure databases

ProteinModelPortalA8AUA2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING467705.SGO_0040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV10508; ABV10508; SGO_0040.
GeneID5599066.
KEGGsgo:SGO_0040.
PATRIC19658035. VBIStrGor124371_0039.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSGOR467705:GH3R-40-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_STRGC
AccessionPrimary (citable) accession number: A8AUA2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 50 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