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Q8A155 (PUR9_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:BT_3812
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length507 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192071

Sequences

Sequence LengthMass (Da)Tools
Q8A155 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: 0C09966527E570E4

FASTA50755,880
        10         20         30         40         50         60 
MSESKRIKTA LVSVYHKEGL DEIITKLYEE GVEFLSTGGT RQFIESLGYP CKAVEDLTTY 

        70         80         90        100        110        120 
PSILGGRVKT LHPKIFGGIL CRRDLEQDIQ QIEKYEIPEI DLVIVDLYPF EATVASGASE 

       130        140        150        160        170        180 
ADIIEKIDIG GISLIRAAAK NYNDVIIVAS QAQYKPLLDM LMEHGATSSL EERRWMAKEA 

       190        200        210        220        230        240 
FAVSSHYDSA IFNYFDAGEG SAFRCSVNNQ KQLRYGENPH QKGYFYGNLD AMFDQIHGKE 

       250        260        270        280        290        300 
ISYNNLLDIN AAVDLIDEYE DLTFAILKHN NACGLASRPT VLEAWTDALA GDPVSAFGGV 

       310        320        330        340        350        360 
LITNGVIDKA AAEEINKIFF EVIIAPDYDV DALEILGQKK NRIILVRKEA KLPKKQFRAL 

       370        380        390        400        410        420 
LNGVLVQDKD MNIETVADLR TVTDKAPTPE EVEDLLFANK IVKNSKSNAI VLAKGKQLLA 

       430        440        450        460        470        480 
SGVGQTSRVD ALKQAIEKAK SFGFDLNGAV MASDAFFPFP DCVEIADKEG ITAVIQPGGS 

       490        500 
VKDDLTFAYC NEHGMAMVTT GIRHFKH 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO78917.1.
RefSeqNP_812723.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_3812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO78917; AAO78917; BT_3812.
GeneID1072684.
KEGGbth:BT_3812.
PATRIC21062640. VBIBacThe70966_3876.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADEIACCA.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-3881-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.
ProtoNetSearch...

Entry information

Entry namePUR9_BACTN
AccessionPrimary (citable) accession number: Q8A155
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: May 14, 2014
This is version 76 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