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P38009 (PUR92_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein ADE17

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:ADE17
Ordered Locus Names:YMR120C
ORF Names:YM8564.02C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length592 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.

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

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.

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Subunit structure

Homodimer (Possible).

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.

Miscellaneous

Present with 60900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PurH family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADE16P541133EBI-14223,EBI-14213

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein ADE17
PRO_0000192160

Experimental info

Sequence conflict3891R → A AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P38009 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 8ABA71761B512242

FASTA59265,263
        10         20         30         40         50         60 
MANYTKTAIL SVYDKTGLLD LARGLIEKNV RILASGGTAR MIRDAGFPIE DVSAITHAPE 

        70         80         90        100        110        120 
MLGGRVKTLH PAVHGGILAR DIDSDEKDLK EQHIEKVDYV VCNLYPFKET VAKVGVTIPE 

       130        140        150        160        170        180 
AVEEIDIGGV TLLRAAAKNH ARVTILSDPK DYSEFLSELS SNGEISQDLR NRLALKAFEH 

       190        200        210        220        230        240 
TADYDAAISD FFRKQYSEGQ AQITLRYGAN PHQKPAQAYV SQQDSLPFKV LCGSPGYINL 

       250        260        270        280        290        300 
LDALNSWPLV KELSASLNLP AAASFKHVSP AGAAVGIPLS DVEKQVYFVA DIENLSPLAC 

       310        320        330        340        350        360 
AYARARGADR MSSFGDWIAL SNIVDVPTAK IISREVSDGV IAPGYEPEAL AILSKKKGGK 

       370        380        390        400        410        420 
YCILQIDPNY VPEAVERRQV YGVTLEQKRN DAIINQSTFK EIVSQNKNLT EQAIIDLTVA 

       430        440        450        460        470        480 
TIAIKYTQSN SVCYARNGMV VGLGAGQQSR IHCTRLAGDK ADNWWFRQHP RVLEIKWAKG 

       490        500        510        520        530        540 
VKRPEKSNAI DLFVTGQIPT EEPELSEYQS KFEEIPKPFT PEERKEWLSK LTNVSLSSDA 

       550        560        570        580        590 
FFPFPDNVYR AVKSGVKYIA APSGSVMDKV VFSAADSFDL VYVENPIRLF HH 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 140-150 AND 389-400.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49273 Genomic DNA. Translation: CAA89269.1.
BK006946 Genomic DNA. Translation: DAA10017.1.
PIRS54489.
RefSeqNP_013839.1. NM_001182621.1.

3D structure databases

ProteinModelPortalP38009.
SMRP38009. Positions 6-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35297. 60 interactions.
DIPDIP-6288N.
IntActP38009. 28 interactions.
MINTMINT-696423.
STRING4932.YMR120C.

Proteomic databases

PaxDbP38009.
PeptideAtlasP38009.
PRIDEP38009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR120C; YMR120C; YMR120C.
GeneID855149.
KEGGsce:YMR120C.

Organism-specific databases

CYGDYMR120c.
SGDS000004727. ADE17.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMAPNQKPAR.
OrthoDBEOG7HXD0J.

Enzyme and pathway databases

BioCycMetaCyc:YMR120C-MONOMER.
YEAST:YMR120C-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Gene expression databases

GenevestigatorP38009.

Family and domain databases

Gene3D1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_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

NextBio978551.

Entry information

Entry namePUR92_YEAST
AccessionPrimary (citable) accession number: P38009
Secondary accession number(s): D6VZU3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways