Reviewed, UniProtKB/Swiss-Prot Q55621 (PUR1_SYNY3)

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:	sll0757

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	495 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	Complete proteome
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro 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 – 28	28	By similarity		PRO_0000029273
	Chain	29 – 495	467	Amidophosphoribosyltransferase		PRO_0000029274
Regions
	Domain	29 – 254	226	Glutamine amidotransferase type-2
Sites
	Active site	29	1	For GATase activity By similarity
	Metal binding	270	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	317	1	Magnesium By similarity
	Metal binding	379	1	Magnesium By similarity
	Metal binding	380	1	Magnesium By similarity
	Metal binding	416	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	467	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	470	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55621-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 417DC5FB4B21207D	FASTA	495	53,670
	10 20 30 40 50 60 MFPPSSDLTE LNDGQPLSGH HADKPEEACG VFGIYAPEEA VAKLTYFGLY ALQHRGQESA 70 80 90 100 110 120 GIATFAGTTV HCHKDMGLVS QVFQESKLNE MVGTLAVGHT RYSTTGSSHR VNAQPAVLPT 130 140 150 160 170 180 RLGPLALAHN GNLVNTNQLR EALAERGCED FVTTTDSEMI AVAIANEVDK GKDWVEGTIA 190 200 210 220 230 240 ALTLCAGAYS LVIGTPEGII GVRDPHGIRP LVIGVLEEET PRYVLASETC ALDIIGATYV 250 260 270 280 290 300 RTVEAGELVH ITESGLVSHR LAESADRKLC VFEMIYFSRP DSVVNDESLY TYRMRIGKHL 310 320 330 340 350 360 AKESPVDADL VMGVPDSGIP AAIGFSQASG IPYAEGLIKN RYVGRTFIQP TQHMREHGIR 370 380 390 400 410 420 MKLNPLKDVL AGKRIIIVDD SIVRGTTSRK IVRALREAGA TEVHMRISSP PVTHPCFYGI 430 440 450 460 470 480 DTDSQDQLIA ARLTVAEIAE QIEVDSLAYL SQEGMLLCTG EDISHFCSAC FNGRYPITVP 490 DAVRRSKLML ENITA

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000022 Genomic DNA. Translation: BAA10132.1.
PIR	S76280.
RefSeq	NP_442062.1.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55621.
Genome annotation databases
GeneID	952767.
GenomeReviews	Gene locus sll0757 in contig BA000022_GR.
KEGG	syn:sll0757.
NMPDR	fig|1148.1.peg.2163.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q55621.
OMA	GIPFELG.
Enzyme and pathway databases
BioCyc	SSP1148:SLL0757-MON.
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. 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_SYNY3

Accession

Primary (citable) accession number: Q55621

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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