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Q16CE0 (PUR9_ROSDO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:RD1_0655
OrganismRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) [Complete proteome] [HAMAP]
Taxonomic identifier375451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter

Protein attributes

Sequence length528 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 – 528528Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057912

Sequences

Sequence LengthMass (Da)Tools
Q16CE0 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: BC1267D670542EF2

FASTA52855,891
        10         20         30         40         50         60 
MTDLAPLRRA LLSVSDKTGL VALGKALAAR GVELLSTGGT ARALRDAGLE VKDVAEVTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPAVHGGLL ALRDNDDHLA AMQEHGIAGI DLVVVNLYPF EQTVAKGAQY 

       130        140        150        160        170        180 
DEVIENIDIG GPAMIRSAAK NHGFVSVVVD VEDYDVLIAQ LEAYDGHTTY ALRQRLAQTA 

       190        200        210        220        230        240 
YARTAAYDTA VSTWMAAQVG EPPRRRSFGG TLAQTLRYGE NPHQDAAFYL DGSNSPGVAT 

       250        260        270        280        290        300 
ARQLQGKELS YNNINDTDAA FELVSEFDQG DGPACAIIKH ANPCGVARAE TLTEAYRRAF 

       310        320        330        340        350        360 
DCDRTSAFGG IIALNQPLDG ATAEEISSIF TEVVIAPGAD AEAQEVFAKK KNLRLLTTDG 

       370        380        390        400        410        420 
LADPTAPGLA IRQVSGGYLV QDRDTGRLSA DALQIVTKRA PSDQEMADLM FAWTVAKHVK 

       430        440        450        460        470        480 
SNAIIYVKDG ATVGVGAGQM SRVDSTRIAA RKAQDMAEAM GLPAPLTQGS VVASDAFFPF 

       490        500        510        520 
ADGLITAAEA GATALIQPGG SMRDDEVIAA ADEAGLAMVF TGMRHFRH 

« Hide

References

[1]"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism."
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.
J. Bacteriol. 189:683-690(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33942 / OCh 114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000362 Genomic DNA. Translation: ABG30353.1.
RefSeqYP_681039.1. NC_008209.1.

3D structure databases

ProteinModelPortalQ16CE0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375451.RD1_0655.

Proteomic databases

PRIDEQ16CE0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG30353; ABG30353; RD1_0655.
GeneID4198089.
KEGGrde:RD1_0655.
PATRIC23359477. VBIRosDen86677_0642.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycRDEN375451:GJIZ-614-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_ROSDO
AccessionPrimary (citable) accession number: Q16CE0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 25, 2006
Last modified: February 19, 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