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P35433 (PUR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amidophosphoribosyltransferase

Short name=ATase
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPAT
Gene names
Name:Ppat
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processPurine biosynthesis
   DomainGlutamine amidotransferase
   Ligand4Fe-4S
Iron
Iron-sulfur
Magnesium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical termAllosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

G1/S transition of mitotic cell cycle

Inferred from expression pattern Ref.3. Source: RGD

cellular response to drug

Inferred from expression pattern PubMed 3012070. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern PubMed 2185659. Source: RGD

glutamine catabolic process

Inferred from direct assay Ref.1. Source: RGD

kidney development

Inferred from expression pattern PubMed 476627. Source: RGD

lactation

Inferred from expression pattern PubMed 2451510. Source: RGD

maternal process involved in female pregnancy

Inferred from expression pattern PubMed 2451510. Source: RGD

nucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

organ regeneration

Inferred from expression pattern PubMed 2430469. Source: RGD

protein homotetramerization

Inferred from direct assay Ref.1. Source: RGD

purine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

purine ribonucleoside monophosphate biosynthetic process

Inferred from direct assay Ref.1. Source: RGD

response to drug

Inferred from expression pattern PubMed 7078346. Source: RGD

ribose phosphate metabolic process

Inferred from direct assay PubMed 447621. Source: RGD

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

amidophosphoribosyltransferase activity

Inferred from direct assay Ref.1. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111
PRO_0000029285
Chain12 – 517506Amidophosphoribosyltransferase
PRO_0000029286

Regions

Domain12 – 261250Glutamine amidotransferase type-2

Sites

Active site121For GATase activity By similarity
Metal binding2801Iron-sulfur (4Fe-4S) By similarity
Metal binding3271Magnesium By similarity
Metal binding3891Magnesium By similarity
Metal binding3901Magnesium By similarity
Metal binding4261Iron-sulfur (4Fe-4S) By similarity
Metal binding5031Iron-sulfur (4Fe-4S) By similarity
Metal binding5061Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P35433 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 8AD3D05A380C120F

FASTA51757,437
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10853 mRNA. Translation: BAA01626.1.
BC086999 mRNA. Translation: AAH86999.1.
D37978 Genomic DNA. Translation: BAA21036.1.
PIRA46088.
RefSeqNP_476546.1. NM_057198.2.
UniGeneRn.18690.

3D structure databases

ProteinModelPortalP35433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000002905.

Protein family/group databases

MEROPSC44.001.

PTM databases

PhosphoSiteP35433.

Proteomic databases

PaxDbP35433.
PRIDEP35433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002905; ENSRNOP00000002905; ENSRNOG00000002128.
GeneID117544.
KEGGrno:117544.
UCSCRGD:620237. rat.

Organism-specific databases

CTD5471.
RGD620237. Ppat.

Phylogenomic databases

eggNOGCOG0034.
GeneTreeENSGT00390000003428.
HOGENOMHOG000033688.
HOVERGENHBG002589.
InParanoidP35433.
KOK00764.
OMADSMFEDQ.
OrthoDBEOG789C9W.
PhylomeDBP35433.
TreeFamTF106370.

Enzyme and pathway databases

SABIO-RKP35433.
UniPathwayUPA00074; UER00124.

Gene expression databases

GenevestigatorP35433.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio620369.
PROP35433.

Entry information

Entry namePUR1_RAT
AccessionPrimary (citable) accession number: P35433
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways