Q5HH14 (PUR1_STAAC) 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=GPATase

Gene names

Name:	purF
Ordered Locus Names:	SACOL1079

Organism

Staphylococcus aureus (strain COL) [Complete proteome] [HAMAP]

Taxonomic identifier

93062 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	494 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.
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	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete 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
Molecular_function	amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC 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 – 10	10	By similarity		PRO_0000045298
	Chain	11 – 494	484	Amidophosphoribosyltransferase		PRO_0000045299
Regions
	Domain	11 – 231	221	Glutamine amidotransferase type-2
Sites
	Active site	11	1	For GATase activity By similarity
	Metal binding	356	1	Magnesium By similarity
	Metal binding	357	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HH14 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: FED58A366B36AD8A	FASTA	494	54,397
	10 20 30 40 50 60 MFNYSGLNEE CGVFGIWNHP EAAQLTYMGL HSLQHRGQEG AGIVVSDQNE LKGERGLGLL 70 80 90 100 110 120 TEAIKDDQME RLKGYQHAIG HVRYATSGNK GIENIQPFLY HFYDMSVGIC HNGNLINAKS 130 140 150 160 170 180 LRQNLEKQGA IFHSSSDTEV IMHLIRRSKA PTFEEALKES LRKVKGGFTF AILTKDALYG 190 200 210 220 230 240 AVDPNAIRPL VVGKMKDGTY ILASETCAID VLGAEFVQDI HAGEYVVIND KGITVKSYTH 250 260 270 280 290 300 HTTTAISAME YIYFARPDST IAGKNVHAVR KASGKKLAQE SPVNADMVIG VPNSSLSAAS 310 320 330 340 350 360 GYAEEIGLPY EMGLVKNQYV ARTFIQPTQE LREQGVRVKL SAVKDIVDGK NIILVDDSIV 370 380 390 400 410 420 RGTTIRRIVK MLKDSGANKV HVRIASPEFM FPSFYGIDVS TTAELISASK SPEEIKDYIG 430 440 450 460 470 480 ADSLAYLSVD GLIESIGLDY DAPYSGLCVE SFTGDYPAGL YDYEANYKAH LSHRQKQYIS 490 KNKHFFDSEG NLNV

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: COL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000046 Genomic DNA. Translation: AAW37959.1.
RefSeq	YP_185943.1. NC_002951.2.
3D structure databases
ProteinModelPortal	Q5HH14.
SMR	Q5HH14. Positions 11-461.
ModBase	Search...
Protein-protein interaction databases
STRING	93062.SACOL1079.
Proteomic databases
PRIDE	Q5HH14.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW37959; AAW37959; SACOL1079.
GeneID	3236103.
KEGG	sac:SACOL1079.
PATRIC	19528392. VBIStaAur112458_1049.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HOG000033688.
KO	K00764.
OMA	GIPFELG.
ProtClustDB	PRK07272.
Enzyme and pathway databases
UniPathway	UPA00074; UER00124.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	PF13537. GATase_7. 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...

Entry information

Entry name

PUR1_STAAC

Accession

Primary (citable) accession number: Q5HH14

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program