Q86A85 (PUR1_DICDI) Reviewed, UniProtKB/Swiss-Prot

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:	purF
ORF Names:	DDB_G0274321

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 purine nucleobase metabolic process Inferred from sequence or structural similarity. Source: dictyBase purine nucleotide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: dictyBase
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB metal 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 – 21	21	By similarity		PRO_0000327801
	Chain	22 – 521	500	Amidophosphoribosyltransferase		PRO_0000327802
Regions
	Domain	22 – 259	238	Glutamine amidotransferase type-2
	Compositional bias	3 – 7	5	Poly-Asn
	Compositional bias	10 – 14	5	Poly-Glu
Sites
	Active site	22	1	For GATase activity By similarity
	Metal binding	276	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	329	1	Magnesium By similarity
	Metal binding	391	1	Magnesium By similarity
	Metal binding	392	1	Magnesium By similarity
	Metal binding	428	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	507	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	510	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q86A85 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: F9A53FBB08B63AC3	FASTA	521	57,429
	10 20 30 40 50 60 MENNNNNFIE EEEELSEPKE KCGVFAIYAP ELDVSRIAFF GLVALQHRGQ ESCGIATYDE 70 80 90 100 110 120 FQSVHVETGM GLVNQVFNET NLKPLKGKMA IGHTRYSTAG KSTLVNAQPV IVQTLHGQIG 130 140 150 160 170 180 IVQNGNLTTA KSLRKELMQK GVGFFIDSDV EVITQLLSNN PEGCDPHKPN WENRIAHFMS 190 200 210 220 230 240 KAEAAYALCL MTPNGIYGVR DSLGMRPLCL GSLEVPCKDD PTKTITRYVL TSESCAIGTI 250 260 270 280 290 300 GAKFIRDVRP GEIVHINENG ITSFIGRSPS DNPALCVFEY VYFSRPDSSM EGQLIHIVRQ 310 320 330 340 350 360 RMGETLARES PPPQTCSNND TIVIGVPDSS LPAAIGYAKQ SGIPFTEGLT KNRYIHRTFI 370 380 390 400 410 420 QPSDHLRQQG IKLKFNPLTE NIQGKKVILV DDSIVRANTI KALIKLIRGA GATEIHVRIS 430 440 450 460 470 480 SPPVLHPCHM GIDMATYDQL IGHNRTVEEI REYIGAESLQ YLTLEGLMKS VNIGIKPQAE 490 500 510 520 TNSTPCFSTS SPTTTKIKIN ENNQKHCVAC FTGDYPCSLD F

References

[1]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000012 Genomic DNA. Translation: EAL70053.1.
RefSeq	XP_643947.1. XM_638855.1.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ProteinModelPortal	Q86A85.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0230083.
Protein family/group databases
MEROPS	C44.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0230083; DDB0230083; DDB_G0274321.
GeneID	8619375.
KEGG	ddi:DDB_G0274321.
Organism-specific databases
dictyBase	DDB_G0274321. purF.
Phylogenomic databases
eggNOG	COG0034.
KO	K00764.
OMA	CASSESC.
ProtClustDB	CLSZ2431006.
Enzyme and pathway databases
UniPathway	UPA00074; UER00124.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	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...

Entry information

Entry name

PUR1_DICDI

Accession

Primary (citable) accession number: Q86A85
Secondary accession number(s): Q555W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)