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A0PWC5 (PUR9_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:MUL_4712
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length523 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 – 523523Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018915

Sequences

Sequence LengthMass (Da)Tools
A0PWC5 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: BF522ECAEFA94C60

FASTA52355,581
        10         20         30         40         50         60 
MSTDHIRRPI RRALISVYDK TGLVDLAQGL TAAGVEIVST GSTAKTIASK GIPVTRVEEL 

        70         80         90        100        110        120 
TGFPEVLDGR VKTLHPRVHA GLLADLRNPE HEAALAELGV EAFELVVVNL YPFSQTVESG 

       130        140        150        160        170        180 
ASVDECVEQI DIGGPSMVRA AAKNHPSVAV VTDPQGYDGV LAAVRSGGFT FAERKKLASL 

       190        200        210        220        230        240 
AFQHTAEYDI AVASWMQSTV APEQPETDFP RWFGRNWRRQ AMLRYGENPH QQAALYADPG 

       250        260        270        280        290        300 
AWPGLAQAEQ LHGKEMSYNN FTDADAAWRA AFDHEQKCVA IIKHANPCGI AISEVSVADA 

       310        320        330        340        350        360 
HRKAHACDPL SAYGGVIACN TEVSPEMAEY VSTIFTEVIV APAYAPAALD QLTKKKNIRV 

       370        380        390        400        410        420 
LVASEPQDGG AELRPISGGL LMQQRDQLDA AGDNPANWIL ATGSPADPAT LTDLVFAWRS 

       430        440        450        460        470        480 
CRAVKSNAIV IVADGATIGV GMGQVNRVDA ARLAVERGGE RVNGAVAASD AFFPFPDGLE 

       490        500        510        520 
TLTAAGVKAI VHPGGSVRDE EVTAAAAKAG ITLYLTGSRH FVH 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL06644.1.
RefSeqYP_908115.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PWC5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_4712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL06644; ABL06644; MUL_4712.
GeneID4554310.
KEGGmul:MUL_4712.
PATRIC18177287. VBIMycUlc37413_5440.

Organism-specific databases

GenoListMUL_4712.
CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

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_MYCUA
AccessionPrimary (citable) accession number: A0PWC5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 53 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