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A4QCK4 (PUR9_CORGB) 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:cgR_0976
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length520 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 – 520520Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096058

Sequences

Sequence LengthMass (Da)Tools
A4QCK4 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 3C7387E84AA1A688

FASTA52055,772
        10         20         30         40         50         60 
MSDDRKAIKR ALISVYDKTG LEDLAQALHR ENVEIVSTGS TAAKIAELGI PVTPVEELTG 

        70         80         90        100        110        120 
FPECLEGRVK TLHPKVHAGI LADTRKEDHL RQLKELEVAP FQLVVVNLYP FAETVASGAD 

       130        140        150        160        170        180 
FDACVEQIDI GGPSMVRAAA KNHPSVAVVV SPNRYEDVQE ALKTGGFSRA ERTKLAAEAF 

       190        200        210        220        230        240 
RHTATYDVTV ATWMSEQLAA EDSETEFPGW IGTTNTLSRS LRYGENPHQS AALYVGNIRG 

       250        260        270        280        290        300 
LAQAKQFHGK EMSYNNYTDS DAAWRAAWDH ERPCVAIIKH ANPCGIAVSD ESIAAAHREA 

       310        320        330        340        350        360 
HACDSVSAFG GVIASNREVS VEMANQVAEI FTEVIIAPSY EEGAVEILSQ KKNIRILQAE 

       370        380        390        400        410        420 
APVRKGFESR EISGGLLVQE RDLIHAEGDN SANWTLAAGS AVSPEVLKDL EFAWTAVRSV 

       430        440        450        460        470        480 
KSNAILLAKN GATVGVGMGQ VNRVDSARLA VDRAGAERAT GSVAASDAFF PFADGFEVLA 

       490        500        510        520 
EAGITAVVQP GGSIRDNEVI EAANKAGVTM YLTGARHFAH 

« Hide

References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009044 Genomic DNA. Translation: BAF53951.1.
RefSeqYP_001137853.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QCK4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340322.cgR_0976.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF53951; BAF53951; cgR_0976.
GeneID4991704.
KEGGcgt:cgR_0976.
PATRIC21506489. VBICorGlu58097_1011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCGLU340322:GJBE-1018-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_CORGB
AccessionPrimary (citable) accession number: A4QCK4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 15, 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