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A4WWQ0 (PUR9_RHOS5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Rsph17025_2928
OrganismRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]
Taxonomic identifier349102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

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_1000057911

Sequences

Sequence LengthMass (Da)Tools
A4WWQ0 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 5D4B15ACC9A0BB00

FASTA52955,856
        10         20         30         40         50         60 
MTNLVPVGRA LLSVSDKSGL LDLARALAEL EVELISTGGT AATLRAAGLK VRDVAEVTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPMVHGGLL ALRDDDEHLV AMAAHGIEPI DLLVVNLYPF EAAVARGASY 

       130        140        150        160        170        180 
DDCIENIDIG GPAMIRAAAK NHRFVNVVTD TADYKALLDE LRAHDGATTL AFRQKLALTA 

       190        200        210        220        230        240 
YSRTAAYDAA VSAWMAGALK SEAPRRRTFA GTLAQTMRYG ENPHQKAAFY TDGSHRPGVA 

       250        260        270        280        290        300 
TAKQWQGKEL SYNNINDTDA AFELVAEFDP SEGPACVIVK HANPCGVARG ATLAEAYGRA 

       310        320        330        340        350        360 
FDCDRVSAFG GIIALNQPLD AATAEKITEI FTEVVIAPGA DEEARAIFAA KKNLRLLTTE 

       370        380        390        400        410        420 
ALPDPLAPGL AFKQVAGGFL VQDRDAGHVD ALDLKVVTKR APSDAELADL LFAWTVAKHV 

       430        440        450        460        470        480 
KSNAIVYVKD GATVGVGAGQ MSRVDSTRIA ARKSQDMAQA LGLAQPLTQG SVVASDAFFP 

       490        500        510        520 
FADGLLAAAE AGATAIIQPG GSMRDDEVIA AADEAGLAMV FTGQRHFRH 

« Hide

References

[1]"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."
US DOE Joint Genome Institute
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000661 Genomic DNA. Translation: ABP71814.1.
RefSeqYP_001169119.1. NC_009428.1.

3D structure databases

ProteinModelPortalA4WWQ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349102.Rsph17025_2928.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP71814; ABP71814; Rsph17025_2928.
GeneID5084528.
KEGGrsq:Rsph17025_2928.
PATRIC23164247. VBIRhoSph94549_3027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRSPH349102:GHE1-4255-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_RHOS5
AccessionPrimary (citable) accession number: A4WWQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 50 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