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B0KJZ6 (PUR9_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:PputGB1_4875
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [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_1000076490

Sequences

Sequence LengthMass (Da)Tools
B0KJZ6 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: F5F851EF38A37F3B

FASTA53557,738
        10         20         30         40         50         60 
MTDQTTRLPV RRALISVSDK TGILEFAREL QQLGVEILST GGTYKLLKDN GVNAVEVADY 

        70         80         90        100        110        120 
TGFAEMMDGR VKTLHPKIHG GILGRRGTDD AIMNEHGIKP IDLVAVNLYP FEATISKPGC 

       130        140        150        160        170        180 
DLPTAIENID IGGPTMVRSA AKNHKDVAIV VNASDYAGIV EGLKVGGLTY AQRFDLMLKA 

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

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

       310        320        330        340        350        360 
EEGGIRKAYD LAYATDTESA FGGIIAFNRE LDGETAKAIV DRQFVEVIIA PKISQAARDV 

       370        380        390        400        410        420 
VAAKQNVRLL ECGEWPAERA AGWDFKRVNG GLLVQSRDIG MITADDLKIV 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 GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABZ00760.1.
RefSeqYP_001671095.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KJZ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_4875.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ00760; ABZ00760; PputGB1_4875.
GeneID5872688.
KEGGppg:PputGB1_4875.
PATRIC19936821. VBIPsePut76638_4872.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-4958-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_PSEPG
AccessionPrimary (citable) accession number: B0KJZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: May 14, 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