Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6FYG4 (PUR9_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:BQ12870
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length538 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 – 538538Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018846

Sequences

Sequence LengthMass (Da)Tools
Q6FYG4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: F0E4F51EF9F95A5B

FASTA53857,776
        10         20         30         40         50         60 
MGVVAKKFPI PDLHRVRRVL LSVSDKTGVV AFAQALHAYS VELISTGGTA KVLMDAGLPV 

        70         80         90        100        110        120 
KDVAEVTGFP EIMDGRVKTL HPLIHGALLG VRQDPSHAVA MEKHGIHGID LLVVNLYPFE 

       130        140        150        160        170        180 
KTSQSGADGQ TILENIDIGG PAMIRAAAKN HAYTGVVTAV SDYDFVLAEL KQHDGCLSFS 

       190        200        210        220        230        240 
MRRQLAMRAY AHTAAYDAAI ATWFAQDLKI ETPSWQSFSG YLENVMRYGE NPHQQAAFYR 

       250        260        270        280        290        300 
NNEKRFGVAT AKLLQGKALS YNNMNDTDAA FELVAEFDPQ KTTAVALIKH ANPCGVAEGK 

       310        320        330        340        350        360 
SLKEAYLKAL MCDNVSAFGG IVALNQPLDE ECAEEIVKIF TEVIIAPDAT IAAREIIARK 

       370        380        390        400        410        420 
KNLRLLTTGG LPDPRCGGLV AKTLAGGILV QSRDNMVVDD LNLQVVTKRA PSQDEMRDLQ 

       430        440        450        460        470        480 
FAFRVVKHVK SNAIVYAKNS ATVGIGAGQM SRIDSAKIAA RKAEESAQRA GLTESPTRGS 

       490        500        510        520        530 
VVASDAFFPF ADGLLAAVEA GATALIQPGG SMRDEEVIAA ADAHGLAMVF TGVRHFRH 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26746.1.
RefSeqYP_032811.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6FYG4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ12870.

Proteomic databases

PRIDEQ6FYG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF26746; CAF26746; BQ12870.
GeneID2867074.
KEGGbqu:BQ12870.
PATRIC31954013. VBIBarQui58630_1404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBQUI283165:GHZA-1285-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_BARQU
AccessionPrimary (citable) accession number: Q6FYG4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: February 19, 2014
This is version 61 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