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B5EL42 (PUR9_ACIF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Lferr_1907
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length521 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 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096036

Sequences

Sequence LengthMass (Da)Tools
B5EL42 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 1B937EF54A52D111

FASTA52155,945
        10         20         30         40         50         60 
MGEITRALIS VSDKRGVVEF ARRLQDFGVE ILSTGGTAKA LMADGVAVQE VGDYTGFPEL 

        70         80         90        100        110        120 
LEGRLKTLHP KIHGGLLAKR DDSSHTRQMA EYGIPAIDLL CVNLYPFAET IASADCTLEE 

       130        140        150        160        170        180 
AMENIDIGGP TMLRAAAKNW EGVTVLVDPD DYAAVLQEME QSYGGVGAST RFRLATKVFA 

       190        200        210        220        230        240 
HTARYDGAIA NYLSSLGPDG NRTTFPQTLS LQFKKAQDLR YGENPHQAAA FYRDGSGGGL 

       250        260        270        280        290        300 
ADAHQLQGKE LSYNNIGDGD AAVALVMEFA EPACCVVKHG NPCGVAVGPD LLGAYQRAWA 

       310        320        330        340        350        360 
GDPISAFGGI VACNRPLDAQ TAELISDQFI EMVLAPAILP DARPILAKRK NLRVLAFDDG 

       370        380        390        400        410        420 
RAWRRTGWDY KRVRGGLLVQ NFDQAMEAET DWKVVSERAP TVQEARDLAF VWRVGKYVRS 

       430        440        450        460        470        480 
NAIVYGREGQ TVGIGAGQMS RVDAARCGVA KALELGFDLH GAALASDAFF PFRDGIDAAA 

       490        500        510        520 
AAGVKAIIQP GGSIRDEEVI ASANEHGIAM VFTGVRHFRH G 

« Hide

References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53993.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001132 Genomic DNA. Translation: ACH84128.1.
RefSeqYP_002220335.1. NC_011206.1.

3D structure databases

ProteinModelPortalB5EL42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380394.Lferr_1907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH84128; ACH84128; Lferr_1907.
GeneID6877892.
KEGGafe:Lferr_1907.
PATRIC20661416. VBIAciFer6930_1903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBCLSK2408239.

Enzyme and pathway databases

BioCycAFER380394:GHE0-1943-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_ACIF5
AccessionPrimary (citable) accession number: B5EL42
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: February 19, 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