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Q0BI80 (PUR9_BURCM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:Bamb_0584
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length521 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 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018853

Sequences

Sequence LengthMass (Da)Tools
Q0BI80 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 8BA275C6EF042929

FASTA52155,521
        10         20         30         40         50         60 
MIKQALISVS DKTGIVDFAK SLSDLGVKLL STGGTAKLLA DAGLPVTEVA DYTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRDL PEHMQALEQH DIPTIDLLVV NLYPFVATIA KDDCTLADAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRSAAKNHRD VTVVVDPADY AVVLDEMKAN GNAIGYATNF RLATKVFAHT 

       190        200        210        220        230        240 
AQYDGAITNY LTSLTDELQH ASRSAYPATL NMAFDKVQDL RYGENPHQSA AFYRDLAAPA 

       250        260        270        280        290        300 
GALANYRQLQ GKELSYNNIA DSDAAWECVK TFDVPACVII KHANPCGVAV GNDSADAYAK 

       310        320        330        340        350        360 
AFQTDPTSAF GGIIAFNREV DEAAAQAVAK QFVEVLIAPS FSDAAKQVFA AKQNVRLLEI 

       370        380        390        400        410        420 
ALGDGHNAFD LKRVGGGLLV QSLDSKNVQP SELRVVTKRQ PSAKEMDDLL FAWRVAKYVK 

       430        440        450        460        470        480 
SNAIVFCGNG MTLGVGAGQM SRVDSARIAS IKAQNAGLTL AGSAVASDAF FPFRDGLDVV 

       490        500        510        520 
VAAGATCVIQ PGGSMRDDEV IAAADEHGIA MILTGVRHFR H 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000440 Genomic DNA. Translation: ABI86143.1.
RefSeqYP_772477.1. NC_008390.1.

3D structure databases

ProteinModelPortalQ0BI80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339670.Bamb_0584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI86143; ABI86143; Bamb_0584.
GeneID4308531.
KEGGbam:Bamb_0584.
PATRIC19016676. VBIBurAmb61564_0648.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBAMB339670:GH48-605-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_BURCM
AccessionPrimary (citable) accession number: Q0BI80
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 60 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