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Q87KT0 (PUR9_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:VP2896
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length530 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 – 530530Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192146

Sequences

Sequence LengthMass (Da)Tools
Q87KT0 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: BC0242CD0F020B69

FASTA53057,322
        10         20         30         40         50         60 
MNNARPIRRA LISVSDKTGI VEFAQALAER GVDILSTGGT ARLLAEQGIA VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGVL GRRGQDDDVM AKHGINPIDM VVVNLYPFAE TVAKDGCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVTIVVNA SDYDRVIAEM DANDKSLTLE TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTMVPS YGENKEGDEE SKFPRTFNQQ FEKKQDMRYG ENSHQAAAFY 

       250        260        270        280        290        300 
VEANPQEASV STARQIQGKA LSYNNIADTD AALECVKEFN EPACVIVKHA NPCGVALGKD 

       310        320        330        340        350        360 
ILEAYNRAYQ TDPTSAFGGI IAFNQELDAE TASAIVERQF VEVIIAPSVS AEAIEVVAAK 

       370        380        390        400        410        420 
KNVRLLECGE WTTKTTGFDV KRVNGGLLVQ DRDQGMVSLD DLKVVSKRQP TEEELKDALF 

       430        440        450        460        470        480 
CWKVAKYVKS NAIVYAKGDM TIGVGAGQMS RVYSAKIAGI KAADEGLEVA GSVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA EAGIKCVIQP GGSMRDDEVI AAADEHGMAM IFTGMRHFRH 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC61159.1.
RefSeqNP_799275.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87KT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2896.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC61159; BAC61159; BAC61159.
GeneID1190471.
KEGGvpa:VP2896.
PATRIC20144040. VBIVibPar50997_2787.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-3015-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_VIBPA
AccessionPrimary (citable) accession number: Q87KT0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: February 19, 2014
This is version 74 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