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Q475R4 (PUR9_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:Reut_A0487
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length523 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 – 523523Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018945

Sequences

Sequence LengthMass (Da)Tools
Q475R4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 40A69D9A2105A33D

FASTA52355,980
        10         20         30         40         50         60 
MIKQALLSVS DKTGIVEFAR ELNALGVTLL STGGTAKLLA DSGLPVTEVA DYTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRDL PEHMAALAEH DIPTIDLLVV NLYPFQQTVA KDDCTLPDAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRSAAKNHRD VTVIVDPVDY AVVLDEMRAN GNKVGYDTNF RLATKVFAHT 

       190        200        210        220        230        240 
AQYDGAITNY LTSLGADKSH QARSAYPQTL NLAFEKVQEM RYGENPHQSA AFYRDLKAVD 

       250        260        270        280        290        300 
GALANYVQLQ GKELSYNNIA DADAAWECVK SFAVTTPACV IIKHANPCGV AVGANALEAY 

       310        320        330        340        350        360 
DKAFKTDSTS AFGGIIAFNV ELDETAAQAV AKQFVEVLIA PSFSAAARAV FASKQNVRLL 

       370        380        390        400        410        420 
EIPLGKGINQ YDLKRVGGGL LVQSPDAKNV QPTELRVVTR RHPTPKEMDD LMFAWRVAKF 

       430        440        450        460        470        480 
VKSNAIVFCG GGMTLGVGAG QMSRVDSARI ASIKAQNAGL TLAGSAVASD AFFPFRDGLD 

       490        500        510        520 
VVVDAGATCV IQPGGSMRDD EVIAAADDRG IAMVLTGTRH FRH 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ59869.1.
RefSeqYP_294713.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ475R4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A0487.

Proteomic databases

PRIDEQ475R4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59869; AAZ59869; Reut_A0487.
GeneID3611791.
KEGGreu:Reut_A0487.
PATRIC20226427. VBIRalEut24049_1090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-490-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_CUPPJ
AccessionPrimary (citable) accession number: Q475R4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 60 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