Reviewed, UniProtKB/Swiss-Prot P07244 (PUR2_YEAST)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthetic protein ADE5,7
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylamine--glycine ligase
              EC=6.3.4.13
        Alternative name(s):
            Glycinamide ribonucleotide synthetase
              Short name=GARS
            Phosphoribosylglycinamide synthetase
    2- Recommended name:
            Phosphoribosylformylglycinamidine cyclo-ligase
              EC=6.3.3.1
        Alternative name(s):
            Phosphoribosyl-aminoimidazole synthetase
            AIR synthase
              Short name=AIRS

Gene names

Name:	ADE5,7
Ordered Locus Names:	YGL234W

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	802 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5. Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
Miscellaneous	Present with 35800 molecules/cell in log phase SD medium.
Sequence similarities	In the N-terminal section; belongs to the GARS family. In the C-terminal section; belongs to the AIR synthase family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	purine base metabolic process Traceable author statement. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-323,EBI-323

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 802	802	Bifunctional purine biosynthetic protein ADE5,7
Regions
	Domain	114 – 330	217	ATP-grasp
	Nucleotide binding	140 – 203	64	ATP By similarity
	Region	1 – 450	450	GARS
	Region	451 – 802	352	AIRS
Sites
	Metal binding	298	1	Manganese By similarity
	Metal binding	300	1	Manganese By similarity
Amino acid modifications
	Modified residue	165	1	Phosphoserine
	Modified residue	247	1	Phosphothreonine
	Modified residue	249	1	Phosphoserine
	Modified residue	406	1	Phosphothreonine
	Modified residue	455	1	Phosphoserine
	Modified residue	458	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	P07244-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 1583C6F3E64085D2	FASTA	802	86,068
	10 20 30 40 50 60 MLNILVLGNG AREHVLVTKL AQSPTVGKIY VAPGNGGTAT MDPSRVINWD ITPDVANFAR 70 80 90 100 110 120 LQSMAVEHKI NLVVPGPELP LVNGITSVFH SVGIPVFGPS VKAAQLEASK AFSKRFMSKH 130 140 150 160 170 180 NIPTASYDVF TNPEEAISFL QAHTDKAFVI KADGIAAGKG VIIPSSIDES VQAIKDIMVT 190 200 210 220 230 240 KQFGEEAGKQ VVIEQFLEGD EISLLTIVDG YSHFNLPVAQ DHKRIFDGDK GLNTGGMGAY 250 260 270 280 290 300 APAPVATPSL LKTIDSQIVK PTIDGMRRDG MPFVGVLFTG MILVKDSKTN QLVPEVLEYN 310 320 330 340 350 360 VRFGDPETQA VLSLLDDQTD LAQVFLAAAE HRLDSVNIGI DDTRSAVTVV VAAGGYPESY 370 380 390 400 410 420 AKGDKITLDT DKLPPHTQIF QAGTKYDSAT DSLLTNGGRV LSVTSTAQDL RTAVDTVYEA 430 440 450 460 470 480 VKCVHFQNSY YRKDIAYRAF QNSESSKVAI TYADSGVSVD NGNNLVQTIK EMVRSTRRPG 490 500 510 520 530 540 ADSDIGGFGG LFDLAQAGFR QNEDTLLVGA TDGVGTKLII AQETGIHNTV GIDLVAMNVN 550 560 570 580 590 600 DLVVQGAEPL FFLDYFATGA LDIQVASDFV SGVANGCIQS GCALVGGETS EMPGMYPPGH 610 620 630 640 650 660 YDTNGTAVGA VLRQDILPKI NEMAAGDVLL GLASSGVHSN GFSLVRKIIQ HVALPWDAPC 670 680 690 700 710 720 PWDESKTLGE GILEPTKIYV KQLLPSIRQR LLLGLAHITG GGLVENIPRA IPDHLQARVD 730 740 750 760 770 780 MSTWEVPRVF KWFGQAGNVP HDDILRTFNM GVGMVLIVKR ENVKAVCDSL TEEGEIIWEL 790 800 GSLQERPKDA PGCVIENGTK LY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae ADE5,7 protein is homologous to overlapping Drosophila melanogaster Gart polypeptides." Henikoff S. J. Mol. Biol. 190:519-528(1986) [PubMed: 3097325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index." Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P., Perrot M. Yeast 11:601-613(1995) [PubMed: 7483834] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 1-13. 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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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 SER-165; THR-247; SER-249; THR-406; SER-455 AND SER-458, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X04337 Genomic DNA. Translation: CAA27867.1. Z72756 Genomic DNA. Translation: CAA96952.1.
PIR	A26343.
RefSeq	NP_011280.1.
3D structure databases
HSSP	HSSP built from PDB template 1CLI based on UniProtKB P08178.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4080N.
IntAct	P07244.
Proteomic databases
PeptideAtlas	P07244.
Genome annotation databases
Ensembl	YGL234W. Saccharomyces cerevisiae. [Contig view]
GeneID	852617.
GenomeReviews	Gene locus YGL234W in contig Y13135_GR.
KEGG	sce:YGL234W.
NMPDR	fig|4932.3.peg.2383.
Organism-specific databases
CYGD	YGL234w.
SGD	S000003203. ADE5,7.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P07244.
Gene expression databases
ArrayExpress	P07244.
GermOnline	YGL234W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000728. AIR_synth. IPR010918. AIR_synth_C. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR000115. Gars. IPR013817. Pre-ATP_grasp. IPR004733. PurM_cligase. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF00586. AIRS. 1 hit. PF02769. AIRS_C. 1 hit. PF01071. GARS_A. 1 hit. PF02843. GARS_C. 1 hit. PF02844. GARS_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00877. purD. 1 hit. TIGR00878. purM. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00184. GARS. 1 hit. [Graphical view]
ProDom	P07244. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P07244.
ProtoNet	Search...

Entry information

Entry name

PUR2_YEAST

Accession

Primary (citable) accession number: P07244

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	September 2, 2008
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)