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

A1UR09 (PUR9_BARBK) 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:BARBAKC583_0074
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [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_1000018844

Sequences

Sequence LengthMass (Da)Tools
A1UR09 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: C481387E41485124

FASTA53858,021
        10         20         30         40         50         60 
MVVVSQNYPT PDLHRVRRAL LSVFDKTGLV EFAQELHAYG IELISTGGTS ESLIAAGLPV 

        70         80         90        100        110        120 
KDVSEVTGFP QIMDGRVKTL HPLIHGGLLG VRDDPSHKAA MEKHGICGID LVVVNLYPFE 

       130        140        150        160        170        180 
KTWQSGADSQ TIIENIDIGG PAMIRAAAKN HAYTGVVTAV SDYDVVLAEL KQHNGCLSFS 

       190        200        210        220        230        240 
LRRQLAARAY EHTAAYDAAI AAWFAQDLEV EMPSWQNFSG HFESMMRYGE NPHQRAAFYR 

       250        260        270        280        290        300 
TRDTRFGVAT AKVLQGKELS YNNMNDADAA FELVAEFDPQ RTAAVALIKH ANPCGVAEGQ 

       310        320        330        340        350        360 
SLKEAYLKAL MCDSVSAFGG IVALNQPLDE ECAAEIVKLF TEVIIAPDAT EAACNIIAQK 

       370        380        390        400        410        420 
KNLRLLITGG VPDPRCGGLT VKTLAGGVLV QSRDNAVVDD FDLQIVTKRA PSQDEMRDLQ 

       430        440        450        460        470        480 
FAFRVVKHVK SNAIVYAKNS ATVGIGAGQM SRLDSARIAV HKAEDNAKRM GLTESLTRGS 

       490        500        510        520        530 
VVASDAFFPF ADGLISAAEA GVTAVIQPGG SIRDQEVIEA ADARGLAMVF TGVRHFRH 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35685 / KC583.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000524 Genomic DNA. Translation: ABM45521.1.
RefSeqYP_988412.1. NC_008783.1.

3D structure databases

ProteinModelPortalA1UR09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360095.BARBAKC583_0074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM45521; ABM45521; BARBAKC583_0074.
GeneID4684296.
KEGGbbk:BARBAKC583_0074.
PATRIC20536425. VBIBarBac6912_0074.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBBAC360095:GHRY-74-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_BARBK
AccessionPrimary (citable) accession number: A1UR09
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 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