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A9IZD0 (PUR9_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:BT_2562
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length539 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 – 539539Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076474

Sequences

Sequence LengthMass (Da)Tools
A9IZD0 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 081EFFB0133DDDA5

FASTA53957,832
        10         20         30         40         50         60 
MGVVAKNFPI PDLHRVRRIL LSVSDKTGVV AFAQALHATY SVELISTGGT AKTLIAAGLP 

        70         80         90        100        110        120 
VKDVSEVTGF PEIMDGRVKT LHPLIHGALL GIREDPSHRE AMEKNSIHGI DLLVVNLYPF 

       130        140        150        160        170        180 
EETIQSGADG KTILENIDIG GPAMIRAAAK NYAYTGVVTA INDYDSILAE LKQHNGCLSL 

       190        200        210        220        230        240 
SMRHQLAMRA YAHTAAYDTA IAAWFARDLK IETPSWQSFS GHLESVMRYG ENPHQQAAFY 

       250        260        270        280        290        300 
RNNEKRFGVA TAKLLQGKAL SYNNLNDTDA AFELVAEFDP QKTAAVALIK HANPCGVAEG 

       310        320        330        340        350        360 
ENLKDAYLKA LMCDNVSAFG GIVALNQTLD EECAEEIVKI FTEVIIAPDA TMAAREIIAK 

       370        380        390        400        410        420 
KKNLRLLITG GIPNPRCGGL LAKTLAGGIL VQSRDNVVID DLKLQVVTKR TPTQDEMRDL 

       430        440        450        460        470        480 
QFAFRVAKHV KSNAIVYAKN SATVGIGAGQ MSRIDSAKIA ASKAAESARR AGLTETLTKG 

       490        500        510        520        530 
SVVASDAFFP FADGLLAAAA AGATAVIQPG GSMRDEEVIT AADEQGLAMV FTGIRHFRH 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK02522.1.
RefSeqYP_001610517.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IZD0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382640.Btr_2562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5830493.
KEGGbtr:Btr_2562.
PATRIC20552974. VBIBarTri113218_2604.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000094758.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBTRI382640:GJEK-2029-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_BART1
AccessionPrimary (citable) accession number: A9IZD0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 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