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Q1LU51 (PUR9_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:BCI_0035
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length526 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 – 526526Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018847

Sequences

Sequence LengthMass (Da)Tools
Q1LU51 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 4A77AA22AA874B48

FASTA52658,384
        10         20         30         40         50         60 
MQRPIIIRRA LLSVSDKTNI CELAKSLLKR GVQLISTNGT ARLLVNAGIH VTEVSNYTGF 

        70         80         90        100        110        120 
PEIMDGRVKT LHPKIHGGIL ARRNIDDTIM QQYKIEHIDM VVVNLYPFAE VVASATCNHE 

       130        140        150        160        170        180 
KVVENIDIGG TALLRSAAKN YSNVVVVVSI NDYISIINEI DCNNGAVSLE TRLNLAIKAF 

       190        200        210        220        230        240 
QHTATYDSQI KDYFTSQVYT DSSKCSSIFP PILNINFVKK QDMRYGENQH QLAAFYLDTR 

       250        260        270        280        290        300 
NKEKSIATTK QLQGRALSYN NIADADAALE CVKEFSEPAC VIVKHINPCS VAMGKTILVA 

       310        320        330        340        350        360 
YQRAYETDPT SAFGGVIAFN RSLDLCTAQE IIARQFIEVI IAPTVDQEAL LILAKKKNIR 

       370        380        390        400        410        420 
VLSSGQWNKP IPNLNFRQVN GGLLVQERDL VMINLHDLRI VSQRQPTTME IQDALFCWKV 

       430        440        450        460        470        480 
VKFVKSNAIV YARNQRTIGI GAGQMSRIDS AKIASIKAID NKLNIRGSTM ASDAFFPFRD 

       490        500        510        520 
GLDSAAKVGV SCVIQPGGSI RDQEVITAAN EHNIAMIFTN IRHFRH 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13814.1.
RefSeqYP_588513.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LU51.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374463.BCI_0035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF13814; ABF13814; BCI_0035.
GeneID4056143.
KEGGbci:BCI_0035.
PATRIC21073559. VBIBauCic75062_0036.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBCIC374463:GI6Q-35-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_BAUCH
AccessionPrimary (citable) accession number: Q1LU51
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 56 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