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B1J5T3 (PUR9_PSEPW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:PputW619_4612
OrganismPseudomonas putida (strain W619) [Complete proteome] [HAMAP]
Taxonomic identifier390235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length535 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 – 535535Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096084

Sequences

Sequence LengthMass (Da)Tools
B1J5T3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: ED9EC9D22E1063EE

FASTA53557,737
        10         20         30         40         50         60 
MTDQTTRLPV RRALISVSDK TGILEFAREL QQLGVEILST GGTYKLLKDN GVNAVEVADY 

        70         80         90        100        110        120 
TGFAEMMDGR VKTLHPKIHG GILGRRGVDD AIMNEHGIKP IDLVAVNLYP FEATIAKPGC 

       130        140        150        160        170        180 
DLPTAIENID IGGPTMVRSA AKNHKDVAIV VNASDYASVL EGLKAGGLTY AQRFDLMLKA 

       190        200        210        220        230        240 
FEHTAAYDGM IANYMGTIDQ AKDTLSTEAR SEFPRTFNSQ FVKAQEMRYG ENPHQSAAFY 

       250        260        270        280        290        300 
VEAKKGEASV STAIQLQGKE LSFNNVADTD AALECVKSFV KPACVIVKHA NPCGVAVVPE 

       310        320        330        340        350        360 
DEGGIRKAYD LAYATDTESA FGGIIAFNRE LDGETAKAIV ERQFVEVIIA PKISQAARDV 

       370        380        390        400        410        420 
VAAKQNVRLL ECGEWPAERA AGWDFKRVNG GLLVQSRDNG MITAEDLKIV TKRAPTEQEI 

       430        440        450        460        470        480 
HDLVFAWKVA KFVKSNAIVY AKQRQTIGVG AGQMSRVNSA RIAAIKAEHA GLQVQGAVMA 

       490        500        510        520        530 
SDAFFPFRDG IDNAAKVGIS AVIQPGGSMR DAEVIAAADE AGIAMVFTGM RHFRH 

« Hide

References

[1]"Complete sequence of Pseudomonas putida W619."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Taghavi S., Vangronsveld D., van der Lelie D., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W619.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000949 Genomic DNA. Translation: ACA75092.1.
RefSeqYP_001751461.1. NC_010501.1.

3D structure databases

ProteinModelPortalB1J5T3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390235.PputW619_4612.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA75092; ACA75092; PputW619_4612.
GeneID6113593.
KEGGppw:PputW619_4612.
PATRIC19959145. VBIPsePut93764_4638.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPPUT390235:GHHJ-4686-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_PSEPW
AccessionPrimary (citable) accession number: B1J5T3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 43 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