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Q4FRN8 (PUR9_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:Psyc_1472
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length526 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 – 526526Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057906

Sequences

Sequence LengthMass (Da)Tools
Q4FRN8 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 95388A5911545799

FASTA52656,508
        10         20         30         40         50         60 
MSKAPLALLS VSDKSNIVEF AQGLIQAGFG LLSTGGTFRL LTEHNVAVTE VSDYTGFPEM 

        70         80         90        100        110        120 
MDGRVKTLHP KIHGGILGRR GTDDMVMSEH AIERIDLVVV NLYPFAETIA RSDVTMNDAI 

       130        140        150        160        170        180 
ENIDIGGPTM VRSAAKNHAH VGIVTDPADY TRVLEALGDS TALTATLRYD LAVKAFEHTA 

       190        200        210        220        230        240 
QYDGMIANFL GSRVNESQEP ESFSRTFNVQ LEKVQDLRYG ENPHQKAAFY VENNSSKSKQ 

       250        260        270        280        290        300 
ASIATAKQLQ GKALSYNNIA DTDAALECVK AFSTPACVIV KHANPCGVAV DIDQVAAYRT 

       310        320        330        340        350        360 
AFSTDPESSF GGIIAFNRPL TLAAATAIID NQFVEVIIAP SVEDGVLEAT ASKKNVRVLV 

       370        380        390        400        410        420 
CGDLPAPELR DRQLDYKRVN GGLLVQEQDL GLITAHDLKI VTDVQPTEAQ IADLLFSWNV 

       430        440        450        460        470        480 
AKYVKSNAIV YAKGQRTIGV GAGQMSRVNS ARIAAIKAEH AGLATEGAVM ASDAFFPFRD 

       490        500        510        520 
GIDNAAEVGI AAIIQPGGSM RDDETIAAAN EHGIAMVFTG MRHFRH 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ19320.1.
RefSeqYP_264754.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FRN8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_1472.

Proteomic databases

PRIDEQ4FRN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ19320; AAZ19320; Psyc_1472.
GeneID3515433.
KEGGpar:Psyc_1472.
PATRIC23057637. VBIPsyArc98534_1732.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPARC259536:GI3A-1508-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_PSYA2
AccessionPrimary (citable) accession number: Q4FRN8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 30, 2005
Last modified: May 14, 2014
This is version 61 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