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A1SZJ2 (PUR9_PSYIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:Ping_3220
OrganismPsychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]
Taxonomic identifier357804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPsychromonadaceaePsychromonas

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_1000018943

Sequences

Sequence LengthMass (Da)Tools
A1SZJ2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 3DF9EAD835128656

FASTA53057,477
        10         20         30         40         50         60 
MENSRPIKRA LLSVSDKAGI IEFAKELSAR GVEILSTGGT CKLLAENDIK VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKIHGGIL ARRGIDEVIM SENDIAPIDL VVVNLYPFAE TVARPDCSLE 

       130        140        150        160        170        180 
DAIENIDIGG PTMVRAAAKN HKDVGIVVNA GDYPRVLKEM QENNNSLAYK TRFDLAIAAY 

       190        200        210        220        230        240 
EHTAQYDGMI ANYFGTMVPS YGENSEGDLE SKFPRTINMQ FKKKQDMRYG ENSHQSAAFY 

       250        260        270        280        290        300 
VEDDIQEASV STATQLQGKA LSYNNIADTD AALECVKEFS EPACVIVKHS NPCGVAVAGN 

       310        320        330        340        350        360 
ILDAYEGAYK TDPTSAFGGI IAFNRELDAK TAEAIVSRQF VEVIIAPSVS PEAAKIVATK 

       370        380        390        400        410        420 
KNLRLLACGE WSDKTTQFDI KRVNGGLLVQ DRDQGMVGLE DLKVVTKRQP TEAELKDLLF 

       430        440        450        460        470        480 
SWKVAKFVKS NAIVYVKNNA TVGVGAGQMS RVYSAKVAGI KAADENLVVA GSVMSSDAFF 

       490        500        510        520        530 
PFRDGIDAAA EAGISCVIQP GGSMRDNEVI AAADEHGMAM VFTGMRHFRH 

« Hide

References

[1]"Complete sequence of Psychromonas ingrahamii 37."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000510 Genomic DNA. Translation: ABM04907.1.
RefSeqYP_944506.1. NC_008709.1.

3D structure databases

ProteinModelPortalA1SZJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357804.Ping_3220.

Proteomic databases

PRIDEA1SZJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM04907; ABM04907; Ping_3220.
GeneID4624653.
KEGGpin:Ping_3220.
PATRIC23071961. VBIPsyIng103130_3559.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPING357804:GJBJ-3329-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_PSYIN
AccessionPrimary (citable) accession number: A1SZJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 53 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