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A4SR98 (PUR9_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:ASA_3451
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

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_1000018833

Sequences

Sequence LengthMass (Da)Tools
A4SR98 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 04EF8740975F314C

FASTA53056,834
        10         20         30         40         50         60 
MEQARPIRRA LLSVSDKTGI LEFAKALNER GVALLSTGGT AKLLGDAGLP VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRDQDDAIM AQHNIYPIDM VVVNLYPFAA TVAKAGCSLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVKA ADYARVIAEM DANGNSLKLA TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTMVPS YGDNKEGDAE SRFPRTFNSQ FIKKQDMRYG ENSHQAAAFY 

       250        260        270        280        290        300 
AEEHATPGSV SSAIQLQGKA LSYNNIADTD AALECVKEFS EPACVIVKHA NPCGVAIGDD 

       310        320        330        340        350        360 
LLTAYDRAYQ TDPTSAFGGI IAFNRELDGA TAAAIVARQF VEVIIAPSVS QEARDVVAAK 

       370        380        390        400        410        420 
QNVRLLECGQ WTAPAQGFDL KRVNGGLLIQ ERDFGMVTQG DLKVVSKRQP TEAELKDLLF 

       430        440        450        460        470        480 
CWKVAKFVKS NAIVYAKEGQ TIGVGAGQMS RVYSAKIAGI KAEDEGLTVA GSVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA AAGISCVIQP GGSMRDQEVI DAADEHGMTM VFTNMRHFRH 

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO91420.1.
RefSeqYP_001143168.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SR98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382245.ASA_3451.

Proteomic databases

PRIDEA4SR98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO91420; ABO91420; ASA_3451.
GeneID4996877.
KEGGasa:ASA_3451.
PATRIC20793360. VBIAerSal2987_3441.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycASAL382245:GJJN-3438-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_AERS4
AccessionPrimary (citable) accession number: A4SR98
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 49 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