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B2JGU1 (PUR9_BURP8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Bphy_2553
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

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 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. HAMAP MF_00139

Sequence similarities

Belongs to the PurH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Bifunctional purine biosynthesis protein PurH HAMAP MF_00139
PRO_1000096047

Sequences

Sequence LengthMass (Da)Tools
B2JGU1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 944CFAB78D1A1C74

FASTA52156,217
        10         20         30         40         50         60 
MIKQALISVS DKSGIVDFAK SLSDLGVKIL STGGTAKLLA DAGLPVTEVA DYTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRDL PEHMAALEKH DIPTIDLLVV NLYPFVQTVS KEECTLEDAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRSAAKNHRD VTVVVDPADY ATVLDEMRAN GNTVGYKTNF RLATKVFAHT 

       190        200        210        220        230        240 
AQYDGAITNY LTSLTEQLQH RDRNTYPATL NMAFEKVQDL RYGENPHQSA AFYRDIAAPA 

       250        260        270        280        290        300 
GALANYRQLQ GKELSYNNIA DSDAAWECVK TFDAPACVII KHANPCGVAV GANPHEAYSK 

       310        320        330        340        350        360 
AFQTDPTSAF GGIIAFNREV DETAAQAVAK QFVEVLIAPS FSEAAKQLFA AKQNVRLLEI 

       370        380        390        400        410        420 
ALGEGHNAFD LKRVGGGLLV QSLDAKNVQP HELRVVTKRH PTPKEMDDLL FAWRVAKFVK 

       430        440        450        460        470        480 
SNAIVFCANG MTMGVGAGQM SRVDSARIAS IKAQNAGLTL SGTAVASDAF FPFRDGLDVV 

       490        500        510        520 
VNAGATCVIQ PGGSMRDDEV IAAADEHNIA MVVTGIRHFR H 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17167 / STM815.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001043 Genomic DNA. Translation: ACC71725.1.
RefSeqYP_001858771.1. NC_010622.1.

3D structure databases

ProteinModelPortalB2JGU1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2JGU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6244036.
GenomeReviewsGene locus Bphy_2553 in contig CP001043_GR.
KEGGbph:Bphy_2553.
PATRIC19191599. VBIBurPhy25146_2710.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG498048.
OMAFTGTRHF.
ProtClustDBPRK00881.

Family and domain databases

HAMAPMF_00139. PurH.
[Tree]
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits.
G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
KOK00602.
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.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
TIGRFAMsTIGR00355. PurH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_BURP8
AccessionPrimary (citable) accession number: B2JGU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families