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A1B5K8 (PUR9_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Pden_2718
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057901

Sequences

Sequence LengthMass (Da)Tools
A1B5K8 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 5A8224550D6D4B2B

FASTA52956,268
        10         20         30         40         50         60 
MTDRIPLKRA LISVSDKTGL VDFARALSAR GVEILSTGGT AKTLREAGLS VVDVADVTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPVVHGGLL ALRDNDEHMA AAKSHRIGMI DLLVVNLYPF EATVAKGAAY 

       130        140        150        160        170        180 
DDCIENIDIG GPAMIRAAAK NHAFVTVVVD VQDYAAVLAE LDANDDRTGL AFRQRQAQIA 

       190        200        210        220        230        240 
YARTAAYDAA VSTWMAGAIG EETPRRRSFS GQLAQSLRYG ENPHQSAAFY RDGSDRPGVA 

       250        260        270        280        290        300 
TARQWQGKEL SYNNINDTDA AFELVAEFDP AEGPAVAIIK HANPCGVARG DSAVDAYLRA 

       310        320        330        340        350        360 
FDCDRTSAFG GIIALNTTLD GETAQAITEI FTEVVIAPDA TDEAKEIFAA KKNLRLLTTG 

       370        380        390        400        410        420 
GLPDPAAPGL AFRQVAGGFL VQGRDNGRIL RADLKVVTKR QPTDQELADL LFAWTVAKHV 

       430        440        450        460        470        480 
KSNAIVYARD LATVGIGAGQ MSRVDSTRIG KRKSEDMAEA LGLAQALTIG SSVASDAFFP 

       490        500        510        520 
FADGVEALAA AGARAVIQPG GSMRDAEVIE AADRLGLAMV FTGQRHFRH 

« Hide

References

[1]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000489 Genomic DNA. Translation: ABL70802.1.
RefSeqYP_916498.1. NC_008686.1.

3D structure databases

ProteinModelPortalA1B5K8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_2718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL70802; ABL70802; Pden_2718.
GeneID4580353.
KEGGpde:Pden_2718.
PATRIC22856577. VBIParDen97112_2654.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-2759-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_PARDP
AccessionPrimary (citable) accession number: A1B5K8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 52 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