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A4VPK9 (PUR9_PSEU5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:PST_3279
OrganismPseudomonas stutzeri (strain A1501) [Complete proteome] [HAMAP]
Taxonomic identifier379731 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length534 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 – 534534Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018942

Sequences

Sequence LengthMass (Da)Tools
A4VPK9 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 3ACEFAC66D086BD1

FASTA53457,627
        10         20         30         40         50         60 
MTDQTTRLPV RRALISVSDK TGVVDFAREL EALGVEILST GGTFKLLREN GIAAIEVADY 

        70         80         90        100        110        120 
TGFPEMMDGR VKTLHPKIHG GILGRRDLDG AVMAEHGIAP IDLVAVNLYP FAATVAKPGC 

       130        140        150        160        170        180 
TLPDAIENID IGGPTMVRSA AKNHKDVAIV VNAEDYAAVV DNLKNGGLTY AQRFDLALKA 

       190        200        210        220        230        240 
FEHTAGYDGM IANYLGGIDQ STEQLSTDNR SLFPRTYNMQ FIKAQDMRYG ENPHQQAAFY 

       250        260        270        280        290        300 
VEKPDEACVA TARQLQGKEL SFNNVADTDA ALECVKSFTK PACVIVKHAN PCGVAVVPEN 

       310        320        330        340        350        360 
EGGIRKAYDL AYATDSESAF GGIIAFNREL DGETAQAIVE RQFVEVIIAP KVSQAARDVV 

       370        380        390        400        410        420 
ASKANVRLLE CGEWPAERSP GWDYKRVNGG LLIQSRDIGM ITEADLKIVT QRAPTEQEIH 

       430        440        450        460        470        480 
DLIFAWKVAK FVKSNAIVYA KNRQTVGVGA GQMSRVNSAR IAAIKAEHAG LQVQGAVMAS 

       490        500        510        520        530 
DAFFPFRDGI DNAAKAGITA VIQPGGSMRD NEVIAAADEA GIAMVFTGMR HFRH 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y. expand/collapse author list , Elmerich C., Lin M., Jin Q.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000304 Genomic DNA. Translation: ABP80910.1.
RefSeqYP_001173752.1. NC_009434.1.

3D structure databases

ProteinModelPortalA4VPK9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379731.PST_3279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP80910; ABP80910; PST_3279.
GeneID5096240.
KEGGpsa:PST_3279.
PATRIC19967114. VBIPseStu31643_3294.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPSTU379731:GJER-3274-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_PSEU5
AccessionPrimary (citable) accession number: A4VPK9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 47 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