Reviewed, UniProtKB/Swiss-Prot P38009 (PUR92_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 + H(2)O = 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.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from direct assay. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: InterPro phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RSP5	P39940	1	EBI-14223,EBI-16219
SSM4	P40318	1	EBI-14223,EBI-18208
URN1	Q06525	1	EBI-14223,EBI-35138

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 592	592	Bifunctional purine biosynthesis protein ADE17		PRO_0000192160
Amino acid modifications
	Modified residue	434	1	Phosphotyrosine
Experimental info
	Sequence conflict	389	1	R → A AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38009-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 8ABA71761B512242	FASTA	592	65,263
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49273 Genomic DNA. Translation: CAA89269.1.
PIR	S54489.
RefSeq	NP_013839.1.
3D structure databases
HSSP	HSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6288N.
IntAct	P38009.
Proteomic databases
PeptideAtlas	P38009.
Genome annotation databases
Ensembl	YMR120C. Saccharomyces cerevisiae. [Contig view]
GeneID	855149.
GenomeReviews	Gene locus YMR120C in contig Z71257_GR.
KEGG	sce:YMR120C.
NMPDR	fig|4932.3.peg.4887.
Organism-specific databases
CYGD	YMR120c.
SGD	S000004727. ADE17.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38009.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-508.
Gene expression databases
ArrayExpress	P38009.
GermOnline	YMR120C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002695. AICARFT_IMPCHas. IPR013982. AICARFT_IMPCHas_formly. IPR011607. MGS. [Graphical view]
PANTHER	PTHR11692. AICARFT_IMPCHas. 1 hit.
Pfam	PF01808. AICARFT_IMPCHas. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PIRSF	PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMART	SM00798. AICARFT_IMPCHas. 1 hit. [Graphical view]
TIGRFAMs	TIGR00355. purH. 1 hit.
ProtoNet	Search...
Other Resources
LinkHub	P38009.
NextBio	978551.

Entry information

Entry name

PUR92_YEAST

Accession

Primary (citable) accession number: P38009

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)