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Q89B23 (PUR9_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:bbp_032
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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.

Sequence caution

The sequence AAO26775.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192078

Sequences

Sequence LengthMass (Da)Tools
Q89B23 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: 940058B815B31047

FASTA52960,084
        10         20         30         40         50         60 
MTNRNVIKNV LISVSDTSNI IEFSKSLISK NIKLFATKGT ANFLKKNNIY ATDITNYTNF 

        70         80         90        100        110        120 
PEIMNGRIKT LHHKIYASIL AQPKHDKKTI EKYNIILMDI VVINFYPFEE ASNNTNLHLN 

       130        140        150        160        170        180 
DIIEHIDIGG PAIVRAAAKN YKNVLVVTQP NLYQSIVNEM NLNNNIISET TKLKFATIAF 

       190        200        210        220        230        240 
KHTMNYDNNI YQYLSKKNKT VPKNTQLQTL LPSHLTINFK KKQDLCYGEN KQQQASWYTN 

       250        260        270        280        290        300 
TSKNTSGRMK IKQLQGKILS YNNLSDIHLA LSCIHEFNKT TCAIIKHGNP CGVATAKNND 

       310        320        330        340        350        360 
QAYKLAYETD PISAFGGIIV FNQKLNDVTA RKIIKTQFSE IILAPDFTQE AKKIFDKKPN 

       370        380        390        400        410        420 
LRIIKYDPNY NYLNYNIDIK SIYGDILVQS NTNSIININQ WDIVSKKRPN EQEINDAKFA 

       430        440        450        460        470        480 
LRVVKHLKSN SIVLIKNQIT ISIGSGQTSR IDATKIAIYK ANNNNISLNH TTLASDAFFP 

       490        500        510        520 
FSDSIDLISK SGITCIVQPG GSIRDNEIIM SANKYNISMI FTKQRYFKH 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26775.1. Different initiation.
RefSeqNP_777670.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89B23.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26775; AAO26775; bbp_032.
GeneID1058351.
KEGGbab:bbp032.
PATRIC21244835. VBIBucAph80364_0032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
KOK00602.
OMACGVATGP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-32-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_BUCBP
AccessionPrimary (citable) accession number: Q89B23
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: May 14, 2014
This is version 74 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