Reviewed, UniProtKB/Swiss-Prot Q27601 (PUR1_DROME)

Names and origin

Protein names

Recommended name:
    Amidophosphoribosyltransferase
      Short name=ATase
    EC=2.4.2.14
Alternative name(s):
    Glutamine phosphoribosylpyrophosphate amidotransferase
      Short name=GPAT

Gene names

Name:	Prat
ORF Names:	CG2867

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 By similarity. Binds 1 4Fe-4S cluster per subunit By similarity.
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.
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	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	determination of adult lifespan Inferred from mutant phenotype. Source: FlyBase embryonic cleavage Inferred from mutant phenotype. Source: FlyBase glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro oogenesis Inferred from mutant phenotype. Source: FlyBase purine base biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Ref.1 Inferred from mutant phenotype. Source: FlyBase iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 53	53	Probable		PRO_0000029287
	Chain	54 – 546	493	Amidophosphoribosyltransferase		PRO_0000029288
Regions
	Domain	54 – 302	249	Glutamine amidotransferase type-2
Sites
	Active site	54	1	For GATase activity By similarity
	Metal binding	321	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	368	1	Magnesium By similarity
	Metal binding	430	1	Magnesium By similarity
	Metal binding	431	1	Magnesium By similarity
	Metal binding	467	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	528	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	531	1	Iron-sulfur (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	113	1	Phosphoserine Ref.5
	Modified residue	114	1	Phosphothreonine Ref.5
	Modified residue	120	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	150	1	E → V in AAC39084. Ref.1
	Sequence conflict	185	1	T → S in AAC39084. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q27601-1 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 4CA4D981EF2C34CC	FASTA	546	59,520
	10 20 30 40 50 60 MSAPQQQQQS QQKQQQHVRV VEQQQVEPAE AVTSSMESES ISASKELTGL THECGVFGAI 70 80 90 100 110 120 ACGDWPTQMD IAHVICLGLV ALQHRGQESA GIATSEGKCS KNFNVHKGMG MISTLFNDDS 130 140 150 160 170 180 MKKLRGNLGI GHTRYSTAGG SGVVNCQPFE VHTTHGALAL AHNGELVNNE SLRREVLARG 190 200 210 220 230 240 VGLSTHSDSE LIAQSLCCAP EDVSELDGPN WPARIRHFMM LAPLSYSLVI MLKDKIYAVR 250 260 270 280 290 300 DTYGNRPLCI GKIVPINAGH GNNLDTPADG WVVSSESCGF LSIGARYVRE VEPGEIVELS 310 320 330 340 350 360 RSGYRTVDIV ERPDFKRMAF CIFEYVYFAR GDSIFEGQMV YTVRLQCGRQ LWREAPVEAD 370 380 390 400 410 420 IVSSVPESGT AAAHGYARES GIEFAEVLCR NRYVGRTFIQ PSTRLRQLGV AKKFGALSEN 430 440 450 460 470 480 VAGKRLVLID DSIVRGNTIG PIIKLLRDAG AREVHIRIAS PPLQYPCYMG INIPTREELI 490 500 510 520 530 540 ANKLNPDQLA RHVGADSLAY LSVEGLVEAV QLKHRDAGDS KSKGTGHCTA CLTGEYPGGL PDELSW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and genetic analyses of Drosophila Prat, which encodes the first enzyme of de novo purine biosynthesis." Clark D.V. Genetics 136:547-557(1994) [PubMed: 8150282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-114 AND SER-120, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF017096 Genomic DNA. Translation: AAC39084.1. Different initiation. AE014297 Genomic DNA. Translation: AAF54163.2. AY069652 mRNA. Translation: AAL39797.1.
PIR	S47860.
RefSeq	NP_524271.2.
UniGene	Dm.9919
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Protein-protein interaction databases
STRING	Q27601.
Protein family/group databases
MEROPS	C44.001.
Genome annotation databases
Ensembl	FBtr0081764; FBpp0081261; FBgn0004901; Drosophila melanogaster. [Genome view]
GeneID	40935.
KEGG	dme:Dmel_CG2867.
NMPDR	fig|7227.3.peg.11611.
Organism-specific databases
CTD	40935.
FlyBase	FBgn0004901. Prat.
Phylogenomic databases
HOGENOM	Q27601.
OMA	IVPINAG.
Enzyme and pathway databases
BRENDA	2.4.2.14. 48.
Gene expression databases
ArrayExpress	Q27601.
GermOnline	CG2867. Drosophila melanogaster.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. IPR002375. Pr/py_Pribosyl_transf_CS. IPR000836. PRibTrfase. [Graphical view]
PANTHER	PTHR11907. Amd_phspho_trans. 1 hit.
Pfam	PF00310. GATase_2. 2 hits. 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 Resources
NextBio	821362.

Entry information

Entry name

PUR1_DROME

Accession

Primary (citable) accession number: Q27601
Secondary accession number(s): Q8T009, Q9VHY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 13, 2005
Last modified:	November 3, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project