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Protein

Amidophosphoribosyltransferase

Gene

Ppat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Enzyme regulationi

Activated by the substrate 5-phospho-alpha-D-ribosyl-1-pyrophosphate and inhibited by the purine ribonucleotides, the end products of purine biosynthesis.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121NucleophilePROSITE-ProRule annotation
Metal bindingi280 – 2801Iron-sulfur (4Fe-4S)By similarity
Metal bindingi327 – 3271MagnesiumBy similarity
Metal bindingi389 – 3891MagnesiumBy similarity
Metal bindingi390 – 3901MagnesiumBy similarity
Metal bindingi426 – 4261Iron-sulfur (4Fe-4S)By similarity
Metal bindingi503 – 5031Iron-sulfur (4Fe-4S)By similarity
Metal bindingi506 – 5061Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. amidophosphoribosyltransferase activity Source: RGD
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. cellular response to drug Source: RGD
  3. cellular response to insulin stimulus Source: RGD
  4. G1/S transition of mitotic cell cycle Source: RGD
  5. glutamine catabolic process Source: RGD
  6. kidney development Source: RGD
  7. lactation Source: RGD
  8. maternal process involved in female pregnancy Source: RGD
  9. nucleoside metabolic process Source: InterPro
  10. organ regeneration Source: RGD
  11. protein homotetramerization Source: RGD
  12. purine nucleobase biosynthetic process Source: InterPro
  13. purine ribonucleoside monophosphate biosynthetic process Source: RGD
  14. response to drug Source: RGD
  15. ribose phosphate metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_217264. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP35433.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase (EC:2.4.2.14)
Short name:
ATase
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name:
GPAT
Gene namesi
Name:Ppat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 14

Organism-specific databases

RGDi620237. Ppat.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 11111 PublicationPRO_0000029285Add
BLAST
Chaini12 – 517506AmidophosphoribosyltransferasePRO_0000029286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP35433.
PRIDEiP35433.

PTM databases

PhosphoSiteiP35433.

Expressioni

Tissue specificityi

Expressed at a high level in brain, heart, liver and stomach.

Gene expression databases

GenevestigatoriP35433.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002905.

Structurei

3D structure databases

ProteinModelPortaliP35433.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 261250Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiP35433.
KOiK00764.
OMAiIAGVNVH.
OrthoDBiEOG789C9W.
PhylomeDBiP35433.
TreeFamiTF106370.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELEESGIRE ECGVFGCIAS GDWPTQLDVP HVITLGLVGL QHRGQESAGI
60 70 80 90 100
VTSDGSSVPK FRVHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC
110 120 130 140 150
ELENCQPFVV ETLHGKIAVA HNGELVNAAR LRKKLLRHGI GLSTSSDSEM
160 170 180 190 200
ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA PAAYSLVIMH RDVIYAVRDP
210 220 230 240 250
YGNRPLCIGR LMPVSDINDK EKKSSETEGW VVSSESCSFL SIGARYCHEV
260 270 280 290 300
KPGEIVEISR HGVRTLDIIP RSNGDPVAFC IFEYVYFARP DSMFEDQMVY
310 320 330 340 350
TVRYRCGQQL AVEAPVEADL VSTVPESATP AALGYATKCG LPYVEVLCKN
360 370 380 390 400
RYVGRTFIQP NMRLRQLGVA KKFGVLSDNF KGKRIVLIDD SIVRGNTISP
410 420 430 440 450
IIKLLKESGA KEVHIRVASP PIKHPCFMGI NIPTKEELIA NKPEFEYLAE
460 470 480 490 500
YLGANSVVYL SVEGLVSSVQ QEIKFKKQKV KKRDITIQEN GNGLEYFEKT
510
GHCTACLTGQ YPVDLEW
Length:517
Mass (Da):57,437
Last modified:June 1, 1994 - v1
Checksum:i8AD3D05A380C120F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10853 mRNA. Translation: BAA01626.1.
BC086999 mRNA. Translation: AAH86999.1.
D37978 Genomic DNA. Translation: BAA21036.1.
PIRiA46088.
RefSeqiNP_476546.1. NM_057198.2.
UniGeneiRn.18690.

Genome annotation databases

EnsembliENSRNOT00000002905; ENSRNOP00000002905; ENSRNOG00000002128.
GeneIDi117544.
KEGGirno:117544.
UCSCiRGD:620237. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10853 mRNA. Translation: BAA01626.1.
BC086999 mRNA. Translation: AAH86999.1.
D37978 Genomic DNA. Translation: BAA21036.1.
PIRiA46088.
RefSeqiNP_476546.1. NM_057198.2.
UniGeneiRn.18690.

3D structure databases

ProteinModelPortaliP35433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002905.

Protein family/group databases

MEROPSiC44.001.

PTM databases

PhosphoSiteiP35433.

Proteomic databases

PaxDbiP35433.
PRIDEiP35433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002905; ENSRNOP00000002905; ENSRNOG00000002128.
GeneIDi117544.
KEGGirno:117544.
UCSCiRGD:620237. rat.

Organism-specific databases

CTDi5471.
RGDi620237. Ppat.

Phylogenomic databases

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiP35433.
KOiK00764.
OMAiIAGVNVH.
OrthoDBiEOG789C9W.
PhylomeDBiP35433.
TreeFamiTF106370.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
ReactomeiREACT_217264. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP35433.

Miscellaneous databases

NextBioi620369.
PROiP35433.

Gene expression databases

GenevestigatoriP35433.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPUR1_RAT
AccessioniPrimary (citable) accession number: P35433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 4, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.