Reviewed, UniProtKB/Swiss-Prot P35433 (PUR1_RAT)

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:

Ppat

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
Enzyme regulation	Activated by the substrate 5-phospho-alpha-D-ribosyl-1-pyrophosphate and inhibited by the purine ribonucleotides, the end products of purine biosynthesis.
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.
Subunit structure	Homotetramer.
Tissue specificity	Expressed at a high level in brain, heart, liver and stomach.
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
PTM	Acetylation
Technical term	Allosteric enzyme Direct protein sequencing
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 – 11	11			PRO_0000029285
	Chain	12 – 517	506	Amidophosphoribosyltransferase		PRO_0000029286
Regions
	Domain	12 – 261	250	Glutamine amidotransferase type-2
Sites
	Active site	12	1	For GATase activity By similarity
	Metal binding	280	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	327	1	Magnesium By similarity
	Metal binding	389	1	Magnesium By similarity
	Metal binding	390	1	Magnesium By similarity
	Metal binding	426	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	503	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	506	1	Iron-sulfur (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	81	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35433-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 8AD3D05A380C120F	FASTA	517	57,437
	10 20 30 40 50 60 MELEESGIRE ECGVFGCIAS GDWPTQLDVP HVITLGLVGL QHRGQESAGI VTSDGSSVPK 70 80 90 100 110 120 FRVHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC ELENCQPFVV ETLHGKIAVA 130 140 150 160 170 180 HNGELVNAAR LRKKLLRHGI GLSTSSDSEM ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA 190 200 210 220 230 240 PAAYSLVIMH RDVIYAVRDP YGNRPLCIGR LMPVSDINDK EKKSSETEGW VVSSESCSFL 250 260 270 280 290 300 SIGARYCHEV KPGEIVEISR HGVRTLDIIP RSNGDPVAFC IFEYVYFARP DSMFEDQMVY 310 320 330 340 350 360 TVRYRCGQQL AVEAPVEADL VSTVPESATP AALGYATKCG LPYVEVLCKN RYVGRTFIQP 370 380 390 400 410 420 NMRLRQLGVA KKFGVLSDNF KGKRIVLIDD SIVRGNTISP IIKLLKESGA KEVHIRVASP 430 440 450 460 470 480 PIKHPCFMGI NIPTKEELIA NKPEFEYLAE YLGANSVVYL SVEGLVSSVQ QEIKFKKQKV 490 500 510 KKRDITIQEN GNGLEYFEKT GHCTACLTGQ YPVDLEW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of rat amidophosphoribosyltransferase." Iwahana H., Yamaoka T., Mizutani M., Mizusawa N., Ii S., Yoshimoto K., Itakura M. J. Biol. Chem. 268:7225-7237(1993) [PubMed: 8463258] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-29. Strain: Wistar. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[3]	"Rat genomic structure of amidophosphoribosyltransferase, cDNA sequence of aminoimidazole ribonucleotide carboxylase, and cell cycle-dependent expression of these two physically linked genes." Iwahana H., Honda S., Tsujisawa T., Takahashi Y., Adzuma K., Katashima R., Yamaoka T., Moritani M., Yoshimoto K., Itakura M. Biochim. Biophys. Acta 1261:369-380(1995) [PubMed: 7742366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43. Strain: Wistar. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D10853 mRNA. Translation: BAA01626.1. BC086999 mRNA. Translation: AAH86999.1. D37978 Genomic DNA. Translation: BAA21036.1.
IPI	IPI00198619.
PIR	A46088.
RefSeq	NP_476546.1.
UniGene	Rn.18690
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Protein-protein interaction databases
STRING	P35433.
Protein family/group databases
MEROPS	C44.001.
Genome annotation databases
Ensembl	ENSRNOT00000002905; ENSRNOP00000002905; ENSRNOG00000002128; Rattus norvegicus. [Genome view]
GeneID	117544.
KEGG	rno:117544.
NMPDR	fig|10116.3.peg.10270.
UCSC	BC086999. rat.
Organism-specific databases
CTD	117544.
RGD	620237. Ppat.
Phylogenomic databases
HOVERGEN	P35433.
OMA	SSETEGW.
Enzyme and pathway databases
BRENDA	2.4.2.14. 248.
Gene expression databases
ArrayExpress	P35433.
Genevestigator	P35433.
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...
Other Resources
NextBio	620369.

Entry information

Entry name

PUR1_RAT

Accession

Primary (citable) accession number: P35433

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)