Amidophosphoribosyltransferase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P04046 (PUR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Amidophosphoribosyltransferase
Short name=ATase
EC=2.4.2.14

Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase

Gene names

Name:	ADE4
Ordered Locus Names:	YMR300C
ORF Names:	YM9952.02C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H₂O.
Cofactor	Binds 1 magnesium ion per subunit.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Miscellaneous	Present with 18700 molecules/cell in log phase SD medium.
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from mutant phenotype PubMed 11689683. Source: SGD glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	amidophosphoribosyltransferase activity Inferred from direct assay PubMed 11689683. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-14238,EBI-14238

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 510

510

Amidophosphoribosyltransferase

PRO_0000139647

Regions

Domain

2 – 239

238

Glutamine amidotransferase type-2

Sites

Active site

For GATase activity By similarity

Metal binding

373

Magnesium By similarity

Metal binding

374

Magnesium By similarity

Amino acid modifications

Modified residue

488

Phosphoserine Ref.6

Experimental info

Sequence conflict

46 – 47

IY → VC in AAA34403. Ref.1

Sequence conflict

46 – 47

IY → VC in AAA34404. Ref.1

Sequence conflict

Missing in AAA34403. Ref.1

Sequence conflict

Missing in AAA34404. Ref.1

Sequence conflict

82 – 87

GSSANS → PLRLIL Ref.1

Sequence conflict

156 – 158

VFH → GFSN in AAA34403. Ref.1

Sequence conflict

156 – 158

VFH → GFSN in AAA34404. Ref.1

Sequence conflict

234

V → G in AAA34403. Ref.1

Sequence conflict

234

V → G in AAA34404. Ref.1

Sequence conflict

291

E → Q in AAA34403. Ref.1

Sequence conflict

291

E → Q in AAA34404. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P04046 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 1FE7A6F5B7C96710
Show »

FASTA

510

56,719

        10         20         30         40         50         60 
MCGILGIVLA NQTTPVAPEL CDGCIFLQHR GQDAAGIATC GSRGRIYQCK GNGMARDVFT 

        70         80         90        100        110        120 
QQRVSGLAGS MGIAHLRYPT AGSSANSEAQ PFYVNSPYGI NLAHNGNLVN TASLKRYMDE 

       130        140        150        160        170        180 
DVHRHINTDS DSELLLNIFA AELEKHNKYR VNNEDVFHAL EGVYRLCRGG YACVGLLAGF 

       190        200        210        220        230        240 
ALFGFRDPNG IRPLLFGERE NPDGTKDYML ASESVVFKAH NFTKYRDLKP GEAVIIPKNC 

       250        260        270        280        290        300 
SKGEPEFKQV VPINSYRPDL FEYVYFARPD SVLDGISVYH TRLAMGSKLA ENILKQLKPE 

       310        320        330        340        350        360 
DIDVVIPVPD TARTCALECA NVLGKPYREG FVKNRYVGRT FIMPNQRERV SSVRRKLNPM 

       370        380        390        400        410        420 
ESEFKGKKVL IVDDSIVRGT TSKEIVNMAK ESGATKVYFA SAAPAIRYNH IYGIDLTDTK 

       430        440        450        460        470        480 
NLIAYNRTDE EVAEVIGCER VIYQSLEDLI DCCKTDKITK FEDGVFTGNY VTGVEDGYIQ 

       490        500        510 
ELEEKRESIA NNSSDMKAEV DIGLYNCADY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glutamine nucleotide sequence of Saccharomyces cerevisiae ADE4 encoding phosphoribosylpyrophosphate amidotransferase." Maentsaelae P., Zalkin H. J. Biol. Chem. 259:8478-8484(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Deletion analysis of the 5' flanking region of yeast ADE4 gene." Lahti R., Glumoff V., Haemaelaeinen H., Paerssinen R., Maentsaelae P. Eur. Congr. Biotechnol. 1:420-423(1987) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
[5]	"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].
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K02203 Genomic DNA. Translation: AAA34403.1. M57633 Genomic DNA. Translation: AAA34405.1. M74309 Genomic DNA. Translation: AAA34404.1. Z49212 Genomic DNA. Translation: CAA89133.1. BK006946 Genomic DNA. Translation: DAA10201.1.
PIR	S53970.
RefSeq	NP_014029.1. NM_001182809.1.
3D structure databases
ProteinModelPortal	P04046.
SMR	P04046. Positions 2-490.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6727N.
IntAct	P04046. 8 interactions.
MINT	MINT-625374.
STRING	4932.YMR300C.
Proteomic databases
PaxDb	P04046.
PeptideAtlas	P04046.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR300C; YMR300C; YMR300C.
GeneID	855346.
KEGG	sce:YMR300C.
Organism-specific databases
CYGD	YMR300c.
SGD	S000004915. ADE4.
Phylogenomic databases
eggNOG	COG0034.
GeneTree	ENSGT00390000003428.
HOGENOM	HOG000033687.
KO	K00764.
OMA	YVTGVED.
OrthoDB	EOG4B5SDH.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-462.
UniPathway	UPA00074; UER00124.
Gene expression databases
Genevestigator	P04046.
GermOnline	YMR300C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	PF00310. GATase_2. 1 hit. PF00156. Pribosyltran. 1 hit. [Graphical view]
PIRSF	PIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMs	TIGR01134. purF. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979094.

Entry information

Entry name

PUR1_YEAST

Accession

Primary (citable) accession number: P04046
Secondary accession number(s): D6W0C7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents