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A4VSB5 (PUR9_STRSY) 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:SSU05_0032
OrganismStreptococcus suis (strain 05ZYH33) [Complete proteome] [HAMAP]
Taxonomic identifier391295 [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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018974

Sequences

Sequence LengthMass (Da)Tools
A4VSB5 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: C35ED161C570C6DF

FASTA51556,504
        10         20         30         40         50         60 
MTKRALISVS DKNGIVEFAQ ELTKLGWEII STGGTKVALD NAGVATIAID DVTGFPEMMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLARRDV DSHLQAAKDH EIGLIDLVVV NLYPFKETIL RPDVTYDLAV 

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

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

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

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

       370        380        390        400        410        420 
ASEVEKEFTG VVGGLLVQDQ DVVVESPADW 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]"A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y. expand/collapse author list , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 05ZYH33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000407 Genomic DNA. Translation: ABP89004.1.
RefSeqYP_001197404.1. NC_009442.1.

3D structure databases

ProteinModelPortalA4VSB5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391295.SSU05_0032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP89004; ABP89004; SSU05_0032.
GeneID5099769.
KEGGssu:SSU05_0032.
PATRIC19771771. VBIStrSui128929_0031.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSSUI391295:GHI8-98-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_STRSY
AccessionPrimary (citable) accession number: A4VSB5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 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