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A3PAY7 (PUR9_PROM0) 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:P9301_02891
OrganismProchlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP]
Taxonomic identifier167546 [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_1000018925

Sequences

Sequence LengthMass (Da)Tools
A3PAY7 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: D20C7F8759A4F712

FASTA51757,214
        10         20         30         40         50         60 
MSPLALVSVS DKKNIIPFCK ELIEQFNYKI LSSGGTAKHL IDAKIPVIKV ADFTNSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPK IHGGILAKRT DEEHKKDVET NNLELIDLVV VNLYPFKKTV DQGAQWEDAI 

       130        140        150        160        170        180 
ENIDIGGPSM IRSAAKNHKD VSVLVDPSQY QNFLEESKKG ELKDAYKAKL ALEAFQHTAD 

       190        200        210        220        230        240 
YDTAISNWIR KERDLQSSKY IESYPLIKTL RYGENPHQKA FWYGLSNIGW NSAEQLQGKD 

       250        260        270        280        290        300 
LSYNNLLDLE SALSTVLEFG YTEKDELKTD MFASVILKHN NPCGASISNS ASKAFLNALE 

       310        320        330        340        350        360 
CDSVSAFGGI VAFNSNVDSD TAVHLKDIFL ECVVAPSFDE EALEILKVKK NLRILKFSKD 

       370        380        390        400        410        420 
QLPKKNQNST KSIMGGLLVQ DTDDSQEKTE DWISVTNKNA NNQANLDLNF AWKICKHVKS 

       430        440        450        460        470        480 
NAIVIAKDQK TIGIGAGQMN RVGAAKIALK AAGSLCSDAV LASDGFFPFA DTVELAHEYG 

       490        500        510 
IKAIIQPGGS LRDQESIDMC NLKGISMIFT QKRHFLH 

« 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 9301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000576 Genomic DNA. Translation: ABO16912.1.
RefSeqYP_001090513.1. NC_009091.1.

3D structure databases

ProteinModelPortalA3PAY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167546.P9301_02891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO16912; ABO16912; P9301_02891.
GeneID4911155.
KEGGpmg:P9301_02891.
PATRIC22994169. VBIProMar103344_0286.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR167546:GH1Y-295-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_PROM0
AccessionPrimary (citable) accession number: A3PAY7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 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