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B7KGS0 (PUR9_CYAP7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:PCC7424_3609
OrganismCyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155)) [Complete proteome] [HAMAP]
Taxonomic identifier65393 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length517 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 – 517517Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000117868

Sequences

Sequence LengthMass (Da)Tools
B7KGS0 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 5A8E1503C17807A7

FASTA51755,629
        10         20         30         40         50         60 
MGRLVLLSVS DKTGLIELAR QLVEEFEFEI ISSGGTAKSL QDAGIPVIKV GDYTGSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARRD VPQDLKDLDA NNIRPLDLVV VNLYPFEQTI AKDNVTVAQA 

       130        140        150        160        170        180 
IEQIDIGGPA MLRATAKNFA HLTVLCNPKY YQPYLEELRQ HNGETSLAFR QKMAGETFAL 

       190        200        210        220        230        240 
TNAYDQAIAS YFASLTPEAT ENPLPTRFSV AGLELQSLRY GENPHQSASW YQSGTQPTGW 

       250        260        270        280        290        300 
TAATKLQGKE LSYNNLVDLE AARRIIVEFD RSEPSCAILK HTNPCGVAVG TTLAEAYNKA 

       310        320        330        340        350        360 
FNADSMSAFG GIVALNQPID PETAKALTKT FLECVVAPGC DEEAQKILSA KSNVRVLILP 

       370        380        390        400        410        420 
DLRSGPKQTV KVIAGGLLVQ ASDDALDNPE TWQVVTEKQP TPEMMAELLF GWKVAKHVKS 

       430        440        450        460        470        480 
NAIVVSKNRT TLGVGAGQMN RVGSVKIALE TAGEAAKGGY LASDGFFPFD DSVRTAAAAG 

       490        500        510 
ITGIIQPGGS LKDKDSIKAA NELGLVMVLT GMRHFLH 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001291 Genomic DNA. Translation: ACK71997.1.
RefSeqYP_002378865.1. NC_011729.1.

3D structure databases

ProteinModelPortalB7KGS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING65393.PCC7424_3609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK71997; ACK71997; PCC7424_3609.
GeneID7107483.
KEGGcyc:PCC7424_3609.
PATRIC21556208. VBICyaSp136448_3705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCSP65393:GJP7-3653-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_CYAP7
AccessionPrimary (citable) accession number: B7KGS0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 39 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