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P15639 (PUR9_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:b4006, JW3970
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192091

Amino acid modifications

Modified residue2871N6-acetyllysine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P15639 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: DC034ED01915DA68

FASTA52957,329
        10         20         30         40         50         60 
MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM VVVNLYPFAQ TVAREGCSLE 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAAYDSMI ANYFGSMVPA YHGESKEAAG RFPRTLNLNF IKKLDMRYGE NSHQQAAFYI 

       250        260        270        280        290        300 
EENVKEASVA TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI 

       310        320        330        340        350        360 
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE EALKITAAKQ 

       370        380        390        400        410        420 
NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE LRVVTKRQPS EQELRDALFC 

       430        440        450        460        470        480 
WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SSMASDAFFP 

       490        500        510        520 
FRDGIDAAAA AGVTCVIQPG GSIRDDEVIA AADEHGIAML FTDMRHFRH 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli."
Aiba A., Mizobuchi K.
J. Biol. Chem. 264:21239-21246(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus."
Flannigan K.A., Hennigan S.H., Vogelbacker H.H., Gots J.S., Smith J.M.
Mol. Microbiol. 4:381-392(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[7]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05126 Genomic DNA. Translation: AAA24454.1.
X51950 Genomic DNA. Translation: CAA36212.1.
U00006 Genomic DNA. Translation: AAC43104.1.
U00096 Genomic DNA. Translation: AAC76980.1.
AP009048 Genomic DNA. Translation: BAE77313.1.
PIRDTECPH. B34193.
RefSeqNP_418434.1. NC_000913.3.
YP_491454.1. NC_007779.1.

3D structure databases

ProteinModelPortalP15639.
SMRP15639. Positions 4-529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15639. 7 interactions.
STRING511145.b4006.

2D gel databases

SWISS-2DPAGEP15639.

Proteomic databases

PaxDbP15639.
PRIDEP15639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76980; AAC76980; b4006.
BAE77313; BAE77313; BAE77313.
GeneID12933467.
948503.
KEGGecj:Y75_p3190.
eco:b4006.
PATRIC32123537. VBIEscCol129921_4121.

Organism-specific databases

EchoBASEEB0788.
EcoGeneEG10795. purH.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
PhylomeDBP15639.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycEcoCyc:AICARTRANSIMPCYCLO-CPLX.
ECOL316407:JW3970-MONOMER.
MetaCyc:AICARTRANSIMPCYCLO-CPLX.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Gene expression databases

GenevestigatorP15639.

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...

Other

PROP15639.

Entry information

Entry namePUR9_ECOLI
AccessionPrimary (citable) accession number: P15639
Secondary accession number(s): Q2M8U3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 122 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene