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A2BUP7 (PUR9_PROM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:P9515_02991
OrganismProchlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]
Taxonomic identifier167542 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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_1000018928

Sequences

Sequence LengthMass (Da)Tools
A2BUP7 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: AE9C2D43313409ED

FASTA51757,437
        10         20         30         40         50         60 
MSPLALVSVS DKTNIIPFCK DLVEKFGYNI LSSGGTAEYL TEAKVPVLKV ADFTESPEIL 

        70         80         90        100        110        120 
DGRVKTLHPK IHGGILAKRS NEEHQREILE NKLELIDLVV VNLYPFKKKV EEQCPWEEAI 

       130        140        150        160        170        180 
ENIDIGGPSM IRSAAKNHAD VAVLVDPNQY QNYIEEIKKG PLSKDFKTKL AFEAFQHTAS 

       190        200        210        220        230        240 
YDSAISNWIS KEKDLRPSNF IESYPLIKQL RYGENPHQKA LWYGLNNIGW NSAEQLQGKE 

       250        260        270        280        290        300 
LSYNNILDLE SALLTVLEFG YETKPNIKTE SIAAVILKHN NPCGASISNS ASSSFKNALK 

       310        320        330        340        350        360 
CDSVSAFGGI VAFNANVDKE TALILKDIFL ECVVAPSFDK EALEIFKTKK NLRVLKLTKE 

       370        380        390        400        410        420 
MLPKENQTCS KSIMGGILIQ DSDNQENSED SWISVTKKNP TEQEYLDLKF AWKICKHVKS 

       430        440        450        460        470        480 
NAIVVAKDQQ TLGIGAGQMN RVGASKIALE AAKEIDSGGV LASDGFFPFA DTVRLADKYG 

       490        500        510 
ISSIIQPGGS IRDEESIKMC DSRGISMIFT HKRHFLH 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9515.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000552 Genomic DNA. Translation: ABM71508.1.
RefSeqYP_001010615.1. NC_008817.1.

3D structure databases

ProteinModelPortalA2BUP7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167542.P9515_02991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM71508; ABM71508; P9515_02991.
GeneID4720172.
KEGGpmc:P9515_02991.
PATRIC23014124. VBIProMar113831_0303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR167542:GI3N-305-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_PROM5
AccessionPrimary (citable) accession number: A2BUP7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: February 19, 2014
This is version 50 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