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Q9F1T4 (PUR9_STRSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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
OrganismStreptococcus suis
Taxonomic identifier1307 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length515 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

Keywords
   Biological processPurine biosynthesis
   Molecular functionHydrolase
Transferase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionIMP cyclohydrolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphoribosylaminoimidazolecarboxamide formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192139

Sequences

Sequence LengthMass (Da)Tools
Q9F1T4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 92D3B3B63F39288A

FASTA51556,511
        10         20         30         40         50         60 
MTKRALISVS DKNGIVEFAQ ELTKFGWEII STGGTKVALD QAGVTTIAID DVTGFPEMMD 

        70         80         90        100        110        120 
GRVKTLHPKI HGGLLARRDL DSHLQAANDH EIGLIDLVVV NLYPFKETIL RPDVTYDLAV 

       130        140        150        160        170        180 
ENIDIGGPSM LRSAAKNHAS VTVVVDPADY PTVLGEIAEQ GETSYATRQR LAAKVFRHTA 

       190        200        210        220        230        240 
AYDALIADYF TKQVGEDKPE KLTITYDLNQ PMRYGENPQQ NADFYQNALP TAYSIAAAKQ 

       250        260        270        280        290        300 
LNGKELSFNN IRDADAAIRI IRDFKDRPTV VALKHMNPCG IGQAETIEQA WDYAYEADPV 

       310        320        330        340        350        360 
SIFGGIVVLN REVDAATAEK MHPIFLEIII APGYSAEALA ILTNKKKNLR ILELAFDAQD 

       370        380        390        400        410        420 
ASEVEKEFTG VVGGLLVQDQ DVVVESPVDW QVVTERQPSE QEWAAMEFAW KSSKYVKSNG 

       430        440        450        460        470        480 
IIITNDKMTL GVGPGQTNRV ASVRIAIEQA KDRLEGAVLA SDAFFPFADN VEEIAAAGIK 

       490        500        510 
AIIQPGGSVR DQDSIDMANK YGLTMVFTGV RHFRH 

« Hide

References

[1]"Evidence for horizontal transfer of the SsuDAT1I restriction-modification genes to the Streptococcus suis genome."
Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.
J. Bacteriol. 183:500-511(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DAT1 / Serotype 2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB045609 Genomic DNA. Translation: BAB20827.1.

3D structure databases

ProteinModelPortalQ9F1T4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_STRSU
AccessionPrimary (citable) accession number: Q9F1T4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 58 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