Reviewed, UniProtKB/Swiss-Prot P35853 (PUR1_LACCA)

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

Organism

Lactobacillus casei

Taxonomic identifier

1582 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	194 AA.
Sequence status	Fragment.
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 Potential. Binds 1 4Fe-4S cluster per subunit Potential.
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
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW purine base biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC 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 – 11	11	By similarity		PRO_0000029253
	Chain	12 – ›194	›183	Amidophosphoribosyltransferase		PRO_0000029254
Regions
	Domain	12 – ›194	›183	Glutamine amidotransferase type-2
Sites
	Active site	12	1	For GATase activity By similarity
Experimental info
	Non-terminal residue	194	1

Sequences

	Sequence		Length	Mass (Da)
	P35853-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 4A788CBC5365D5EC	FASTA	194	21,144
	10 20 30 40 50 60 MPHEPKGLNE ECGVFGVWGN PNAASITHLG LHTLQHRGQE GAGIVGLTKD GMRRHYGLGL 70 80 90 100 110 120 LSEVFTNTDQ LTPLIGRAAL GHVRYSTAGG RVLENIQPLL FRFSDEAIAL AHNGNLTNAI 130 140 150 160 170 180 SLRRQLEDQG AIFQSTSDTE VLMHLIRRQV GQPWLTQLKT ALNEVHGGFA FVLLTEHGLY 190 AAVDPHGFRP MVVG

References

[1]	"Isolation and complete sequence of the purL gene encoding FGAM synthase II in Lactobacillus casei." Gu Z.-M., Martindale D.W., Lee B.H. Gene 119:123-126(1992) [PubMed: 1398079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Erratum Gu Z.-M., Martindale D.W., Lee B.H. Gene 133:147-147(1993) [PubMed: 8224889] [Abstract]

Cross-references

Sequence databases
EMBLGenBankDDBJ	M85265 Genomic DNA. Translation: AAC36948.1.
PIR	PC1136.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.4.2.14. 610.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. IPR002375. Pr/py_Pribosyl_transf_CS. [Graphical view]
PANTHER	PTHR11907. Amd_phspho_trans. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. [Graphical view]
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR1_LACCA

Accession

Primary (citable) accession number: P35853

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)