Reviewed, UniProtKB/Swiss-Prot Q55038 (PUR1_SYNE7)

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:	Synpcc7942_0004

Organism

Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]

Taxonomic identifier

1140 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length	493 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 – 26	26	By similarity		PRO_0000029271
	Chain	27 – 493	467	Amidophosphoribosyltransferase		PRO_0000029272
Regions
	Domain	27 – 252	226	Glutamine amidotransferase type-2
Sites
	Active site	27	1	For GATase activity By similarity
	Metal binding	268	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	315	1	Magnesium By similarity
	Metal binding	377	1	Magnesium By similarity
	Metal binding	378	1	Magnesium By similarity
	Metal binding	414	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	465	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	468	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55038-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E03508F8A922910C	FASTA	493	53,809
	10 20 30 40 50 60 MIPTQPLTAD LDCDLGLERP DRPEEACGVF ALYAPGEEVA RMAYFGLYAL QHRGQESAGI 70 80 90 100 110 120 AVFEGDRVML HKDMGLVSQV FDPEILQQLQ GSLAVGHTRY STTGSSRIAN AQPALLETRL 130 140 150 160 170 180 GPVALAHNGN LVNTVELRQE LLAKNHELTT TTDSELIAFA IMEAVAEGQD WRGAIESACR 190 200 210 220 230 240 RSQGAFSLTI GTPEALYGTR DPNGIRPLVL GTLESNGQTR YVLSSETCGL DIIGADYVRD 250 260 270 280 290 300 IAPGEMVRIT DAGLESWTWA EAPQPKLCVF EMIYFARPDS LFHGESLYSY RRRIGQRLAK 310 320 330 340 350 360 EAPADVDLVL GVPDSGIPAA IGFSEALGIP YAEGLIKNRY VGRTFIQPTQ SMRETGIRMK 370 380 390 400 410 420 LNPLKDVLAG KRIAIIDDSI VRGTTSRKLV KALRDAGATE VHMRISSPPV THPCFYGIDT 430 440 450 460 470 480 DTQDQLIAAT RSVSEITEQI GVDSLAYLTE QGMLEATRES IGNFCTACFN GRYPIAIPEE 490 IKRSKLMLET VTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Circadian expression of genes involved in the purine biosynthetic pathway of the cyanobacterium Synechococcus sp. strain PCC 7942." Liu Y., Tsinoremas N.F., Golden S.S., Kondo T., Johnson C.H. Mol. Microbiol. 20:1071-1081(1996) [PubMed: 8809759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33211 Genomic DNA. Translation: AAA75107.1. CP000100 Genomic DNA. Translation: ABB56036.1.
PIR	S77612.
RefSeq	YP_399023.1.
3D structure databases
SMR	Q55038. Positions 27-485.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55038.
Protein family/group databases
MEROPS	C44.001.
Genome annotation databases
GeneID	3774224.
GenomeReviews	Gene locus Synpcc7942_0004 in contig CP000100_GR.
KEGG	syf:Synpcc7942_0004.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HBG392416.
Enzyme and pathway databases
BioCyc	SELO1140:SYNPCC7942_0004-MONOMER.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR1_SYNE7

Accession

Primary (citable) accession number: Q55038
Secondary accession number(s): Q31SD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 67 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)