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Reviewed, UniProtKB/Swiss-Prot P38009 (PUR92_YEAST)

Last modified November 3, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein ADE17
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: ADE17
Ordered Locus Names: YMR120C
ORF Names: YM8564.02C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. Ref.3

Sequence similarities

Belongs to the purH family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein ADE17
PRO_0000192160

Amino acid modifications

Modified residue4341Phosphotyrosine Ref.4

Experimental info

Sequence conflict3891R → A AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P38009-1 [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

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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: 9169872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"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: 7895733] [Abstract]
Cited for: PROTEIN SEQUENCE OF 140-150 AND 389-400.
Strain: ATCC 204508 / S288c.
[3]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-434, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

Z49273 Genomic DNA. Translation: CAA89269.1.
PIRS54489.
RefSeqNP_013839.1.

3D structure databases

HSSPHSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6288N.
IntActP38009. 69 interactions.
STRINGP38009.

Proteomic databases

PeptideAtlasP38009.
PRIDEP38009.

Genome annotation databases

EnsemblYMR120C; YMR120C; YMR120C; Saccharomyces cerevisiae. [Genome view]
GeneID855149.
GenomeReviewsGene locus YMR120C in contig Z71257_GR.
KEGGsce:YMR120C.
NMPDRfig|4932.3.peg.4887.

Organism-specific databases

CYGDYMR120c.
SGDS000004727. ADE17.

Phylogenomic databases

HOGENOMP38009.
OMATITHAPE.

Enzyme and pathway databases

BioCycMetaCyc:MON-508.
BRENDA2.1.2.3. 250.
3.5.4.10. 250.

Gene expression databases

ArrayExpressP38009.
GenevestigatorP38009.
GermOnlineYMR120C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHas_formly.
IPR011607. MGS.
[Graphical view]
PANTHERPTHR11692. AICARFT_IMPCHas. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
[Graphical view]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Other Resources

NextBio978551.

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Entry information

Entry namePUR92_YEAST
AccessionPrimary (citable) accession number: P38009
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: November 3, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents