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B0JL55 (PUR9_MICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:MAE_62320
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis

Protein attributes

Sequence length511 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 – 511511Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076485

Sequences

Sequence LengthMass (Da)Tools
B0JL55 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: BAED3E34D2F8B3D0

FASTA51154,930
        10         20         30         40         50         60 
MGRLALISVT DKTGIVDFAR QLTEEFDFEI ISSGGTAKTL QSAGIPVIKV GEYTGSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARRD WQSDLAEMEA NQIRPFDLVV VNLYPFEQTI ANPDVTTAQA 

       130        140        150        160        170        180 
IEQIDIGGPA MLRASAKNFA HLTVISNPKY YEQYLSQLRQ NNGEISLEFR QKMAGETFAL 

       190        200        210        220        230        240 
TNAYDGAIAA YFASLNGETT RFNLAGNALQ TLRYGENPHQ SATWYGSGTM AQGWGKATLL 

       250        260        270        280        290        300 
QGKELSYNNL VDLEAARRLI AEFGSEEPAA AILKHTNPCG VAIGGSLVEA YTKAFNADAI 

       310        320        330        340        350        360 
SAFGGIVALN QAIDEATAKE LTKTFLECVV APDCSPEAQD ILAKKSKVRI LLLPDLTTGE 

       370        380        390        400        410        420 
KQTVKVIAGG FLVQAADDVV ETPDEWRVVT EKQPTPAQLA ELLFAWKVSK HVKSNAIVVT 

       430        440        450        460        470        480 
KNQTTLGVGA GQMNRVGSVK IALEQAAEAA KGGYLASDGF FPFDDSVRTA AQFGIEAIVQ 

       490        500        510 
PGGSLKDQDS INAANELGLI MVLTGIRHFL H 

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIES-843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009552 Genomic DNA. Translation: BAG06054.1.
RefSeqYP_001661246.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JL55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING449447.MAE_62320.

Proteomic databases

PaxDbB0JL55.
PRIDEB0JL55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG06054; BAG06054; MAE_62320.
GeneID5867080.
KEGGmar:MAE_62320.
PATRIC22636836. VBIMicAer59304_5712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycMAER449447:GHO8-6284-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_MICAN
AccessionPrimary (citable) accession number: B0JL55
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 43 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