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Q892X3 (PUR9_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:CTC_01962
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length499 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 – 499499Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192086

Sequences

Sequence LengthMass (Da)Tools
Q892X3 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: 17F1CB10527AF3BB

FASTA49956,183
        10         20         30         40         50         60 
MIKRALISVY NKEGILEFAK FLEKNHVEII STGGTYKHLK DNCVRVKEVS QITNFDEILD 

        70         80         90        100        110        120 
GRVKTLHPAV HGGILAIRDN KEHMDTIKDK NIEPIDMVIV NLYPFFEKIG KGLSLEEQIE 

       130        140        150        160        170        180 
FIDIGGPTMI RAAAKNFKDV VVITDPKDYK RIEEKLEKED EIDFNNRKTL AGKVFNLMSA 

       190        200        210        220        230        240 
YDGAISKFLL EEEYPEYLSL SYKKGKDLRY GENPHQTAAF YTSLTEDGAF KDFEKLNGKE 

       250        260        270        280        290        300 
LSYNNIKDMD VAWKIVGEFE EIACCALKHN SPCGVAIGDT LLESYKKAYE CDPISIFGGI 

       310        320        330        340        350        360 
VAFNRKVNKE TAKELVKIFL EVIIAPDYDE DALRILKGKK NLRVIKCNTK PLDKMEICKV 

       370        380        390        400        410        420 
DVGILVQSTD NALIKDMDVV TAKKPTEEEM ENMIFAMKVV KYVKSNAIVV VKDKKAVGIA 

       430        440        450        460        470        480 
GGQVNRIWAA CQALERGNNS VVLASDAFFP FDDVVKKASE YGIKAIIQPG GSIRDKDSIE 

       490 
ECDEKGISMV FTGIRHFKH 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO36469.1.
RefSeqNP_782532.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ892X3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC01962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO36469; AAO36469; CTC_01962.
GeneID1059924.
KEGGctc:CTC01962.
PATRIC19511975. VBICloTet101274_2035.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCTET212717:GJAM-1799-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_CLOTE
AccessionPrimary (citable) accession number: Q892X3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: May 14, 2014
This is version 75 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