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B7J5P7 (PUR9_ACIF2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:AFE_2260
OrganismAcidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) [Complete proteome] [HAMAP]
Taxonomic identifier243159 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length524 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 – 524524Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000203244

Sequences

Sequence LengthMass (Da)Tools
B7J5P7 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 1B8B35D12D6C8811

FASTA52456,281
        10         20         30         40         50         60 
MGFMGEITRA LISVSDKRGV VEFARRLQDF GVEILSTGGT AKALMADGVA VQEVGDYTGF 

        70         80         90        100        110        120 
PELLEGRLKT LHPKIHGGLL AKRDDSSHTR QMAEYGIPAI DLLCVNLYPF AETIASADCT 

       130        140        150        160        170        180 
LEEAMENIDI GGPTMLRAAA KNWEGVTVLV DPDDYAAVLQ EMEQSYGGVG ASTRFRLATK 

       190        200        210        220        230        240 
VFAHTARYDG AIANYLSSLG PDGNRTTFPQ TLSLQFKKAQ DLRYGENPHQ AAAFYRDGSG 

       250        260        270        280        290        300 
GGLADAHQLQ GKELSYNNIG DGDAAVALVM EFAEPACCVV KHGNPCGVAV GPDLLGAYQR 

       310        320        330        340        350        360 
AWAGDPISAF GGIVACNRPL DAQTAELISD QFIEMVLAPA ILPDARPILA KRKNLRVLAF 

       370        380        390        400        410        420 
DDGRAWRRTG WDYKRVRGGL LVQNFDQAME AETDWKVVSE RAPTVQEARD LAFVWRVGKY 

       430        440        450        460        470        480 
VRSNAIVYGR EGQTVGIGAG QMSRVDAARC GVAKALELGF DLHGAALASD AFFPFRDGID 

       490        500        510        520 
AAAAAGVKAI IQPGGSIRDE EVIASANEHG IAMVFTGVRH FRHG 

« Hide

References

[1]"Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications."
Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S.
BMC Genomics 9:597-597(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23270 / DSM 14882 / NCIB 8455.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001219 Genomic DNA. Translation: ACK79370.1.
RefSeqYP_002426658.1. NC_011761.1.

3D structure databases

ProteinModelPortalB7J5P7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243159.AFE_2260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK79370; ACK79370; AFE_2260.
GeneID7135650.
KEGGafr:AFE_2260.
PATRIC20655591. VBIAciFer29821_2058.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycAFER243159:GH3S-2255-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_ACIF2
AccessionPrimary (citable) accession number: B7J5P7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 41 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