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Q6A6Y8 (PUR9_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:PPA1747
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length516 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 – 516516Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057904

Sequences

Sequence LengthMass (Da)Tools
Q6A6Y8 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 0A766E14EAF82C21

FASTA51654,992
        10         20         30         40         50         60 
MSERQPIRRA LVSVYDKSGL DQLAKALIDA QVEVVSTGST AKELASHGVT VTEVSEITGF 

        70         80         90        100        110        120 
PECLDGRVKT LHPKVHAGIL ADRRLTSHRE QLTALEVKPF DLVVCNLYPF AETVAQGGDF 

       130        140        150        160        170        180 
DECIEKIDIG GPSMVRAAAK NHANVAVLTN PDQYEDLARA LSEGGYTMEE RRVLAARAFA 

       190        200        210        220        230        240 
HTAAYDVAVA TWFGSRDGVA VDGVPTFVGT TGELSHPLRY GENSHQAAAV YRSSGEPGLA 

       250        260        270        280        290        300 
GARQLHGKAM SYNNYVDTNS ARRAAFDFEA PCVAVIKHSN PCGIATGSDI AEAHRKAHAC 

       310        320        330        340        350        360 
DSLSAFGGVI ATNRPVSVEM AEQVAEIFTE VVVAPGYEDG AVEILSRKKN IRLLECPAPH 

       370        380        390        400        410        420 
LAGWELRQID GGLLAMETDL FQADGDDPAN WTLAAGDPVD DVTLADLSFA WRACRSVRSN 

       430        440        450        460        470        480 
AILLAHDGAS VGVGMGQVNR VDSCRLAVER AGDRAAGSVA ASDAFFPFAD GPQVLIDAHI 

       490        500        510 
AAIVEPGGSI RDDQTIEVCR TAGVPLYFTG TRHFFH 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT83476.1.
RefSeqYP_056434.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A6Y8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA1747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT83476; AAT83476; PPA1747.
GeneID2932978.
KEGGpac:PPA1747.
PATRIC23038307. VBIProAcn64440_1803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPACN267747:GHO9-1765-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_PROAC
AccessionPrimary (citable) accession number: Q6A6Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 63 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