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A2S597 (PUR9_BURM9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:BMA10229_A1131
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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_1000018855

Sequences

Sequence LengthMass (Da)Tools
A2S597 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: CDDA7B76B25BB0E6

FASTA52155,458
        10         20         30         40         50         60 
MIKQALISVS DKTGIVDFAK ALSALGVKLL STGGTAKLLA DAGLPVTEVA DYTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRDL PEHMQALEAH GIPTIDLLVV NLYPFVQTIA KDDCTLADAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRSAAKNHRD VTVVVDPADY AVVLDEMKAN GNTLGYKTNF RLATKVFAHT 

       190        200        210        220        230        240 
AQYDGAITNY LTSLGDDLQH GSRSAYPATL NLAFDKVQDL RYGENPHQSA AFYRDVATPA 

       250        260        270        280        290        300 
GALANYRQLQ GKELSYNNIA DSDAAWECVK TFDAPACVII KHANPCGVAV GADAGEAYAK 

       310        320        330        340        350        360 
AFQTDPTSAF GGIIAFNREV DEAAAQAVAK QFVEVLIAPS FSDAAKQVFA AKQNVRLLEI 

       370        380        390        400        410        420 
ALGEGHNAFD LKRVGGGLLV QSLDSKNVQP RELRVVTKRH PTPKEMDDLL FAWRVAKYVK 

       430        440        450        460        470        480 
SNAIVFCGNG MTLGVGAGQM SRVDSARIAS IKAQNAGLTL AGSAVASDAF FPFRDGLDVV 

       490        500        510        520 
VAAGATCVIQ PGGSVRDDEV IAAADEHNIA MVVTGVRHFR H 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000546 Genomic DNA. Translation: ABN03293.1.
RefSeqYP_001027116.1. NC_008836.1.

3D structure databases

ProteinModelPortalA2S597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412022.BMA10229_A1131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN03293; ABN03293; BMA10229_A1131.
GeneID4793976.
KEGGbml:BMA10229_A1131.
PATRIC19133214. VBIBurMal46188_3327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMACGVATGP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBMAL412022:GJI8-1131-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_BURM9
AccessionPrimary (citable) accession number: A2S597
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: May 14, 2014
This is version 52 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