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Reviewed, UniProtKB/Swiss-Prot Q8KA70 (PUR9_BUCAP)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: purH
Ordered Locus Names: BUsg_032
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP 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 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.

Sequence similarities

Belongs to the purH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_0000192077

Sequences

Sequence LengthMass (Da)Tools
Q8KA70-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 7F0F13954EF902A5

FASTA52659,422
        10         20         30         40         50         60 
MSLNNIIKNA LVSLSDKTDL LKISKILAEK KINLFCTGGT ADVLKKNKIP VLEISDYTNF 

        70         80         90        100        110        120 
PEIMNGRLKT LHPKIIGGIL GRREKDQKIM KLHNLIPIDI VIVNFYPFEK IQNRKEFTIE 

       130        140        150        160        170        180 
EIIDNIDIGG PTLVRAAAKN YKDVIVIVDL SDFTSCIQLI NTNTVSLETR FDLATKAFKY 

       190        200        210        220        230        240 
TALYEEIISK YFLKKNPYRK KHQKNIFPNE FQLNFIKKQD LRYGENQHQK SSFYIEKEIL 

       250        260        270        280        290        300 
KSGTISSSNQ IQGKNLSYNN ICDADIALEC VKEFSKPTCV IVKHGNPCGV SESNSLIKAY 

       310        320        330        340        350        360 
FSAYNADPIS AFGGIIAFNC LLDLDTAQEI VKKQFVEVII APEIDEMAVK ILKRKKNIRL 

       370        380        390        400        410        420 
LICGKIEKNK KGLDFKRITN GLLIQEYDCD EINAKNFDFV TNRLPTEKEL EDAIFSWKVA 

       430        440        450        460        470        480 
KFVKSNAIVY SLNKTTIGIG AGQTSRIDAT KLANLKVKDR NHNNTTGATM ASDAFFPFRD 

       490        500        510        520 
GIDNAALIGI SCIIQPGGSI RDKEVIESAN EHNISMIFTK KRHFKH 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE013218 Genomic DNA. Translation: AAM67603.1.
RefSeqNP_660392.1.

3D structure databases

HSSPHSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBaseSearch...

Genome annotation databases

GeneID1005848.
GenomeReviewsGene locus BUsg_032 in contig AE013218_GR.
KEGGbas:BUsg032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8KA70.
OMAVVKHVKS.

Enzyme and pathway databases

BioCycBAPH198804:BUSG032-MON.

Family and domain databases

HAMAPMF_00139.
[Tree]
InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHas_formly.
IPR011607. MGS.
[Graphical view]
PANTHERPTHR11692. AICARFT_IMPCHas. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
[Graphical view]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_BUCAP
AccessionPrimary (citable) accession number: Q8KA70
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents