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P35433

- PUR1_RAT

UniProt

P35433 - PUR1_RAT

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Protein
Amidophosphoribosyltransferase
Gene
Ppat
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Binds 1 magnesium ion per subunit By similarity.
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 – 121For GATase activity By similarity
Metal bindingi280 – 2801Iron-sulfur (4Fe-4S) By similarity
Metal bindingi327 – 3271Magnesium By similarity
Metal bindingi389 – 3891Magnesium By similarity
Metal bindingi390 – 3901Magnesium By 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
Complete GO annotation...

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. G1/S transition of mitotic cell cycle Source: RGD
  3. cellular response to drug Source: RGD
  4. cellular response to insulin stimulus 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 – 1111
PRO_0000029285Add
BLAST
Chaini12 – 517506Amidophosphoribosyltransferase
PRO_0000029286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By 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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
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

MELEESGIRE ECGVFGCIAS GDWPTQLDVP HVITLGLVGL QHRGQESAGI    50
VTSDGSSVPK FRVHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC 100
ELENCQPFVV ETLHGKIAVA HNGELVNAAR LRKKLLRHGI GLSTSSDSEM 150
ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA PAAYSLVIMH RDVIYAVRDP 200
YGNRPLCIGR LMPVSDINDK EKKSSETEGW VVSSESCSFL SIGARYCHEV 250
KPGEIVEISR HGVRTLDIIP RSNGDPVAFC IFEYVYFARP DSMFEDQMVY 300
TVRYRCGQQL AVEAPVEADL VSTVPESATP AALGYATKCG LPYVEVLCKN 350
RYVGRTFIQP NMRLRQLGVA KKFGVLSDNF KGKRIVLIDD SIVRGNTISP 400
IIKLLKESGA KEVHIRVASP PIKHPCFMGI NIPTKEELIA NKPEFEYLAE 450
YLGANSVVYL SVEGLVSSVQ QEIKFKKQKV KKRDITIQEN GNGLEYFEKT 500
GHCTACLTGQ YPVDLEW 517
Length:517
Mass (Da):57,437
Last modified:June 1, 1994 - v1
Checksum:i8AD3D05A380C120F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D10853 mRNA. Translation: BAA01626.1 .
BC086999 mRNA. Translation: AAH86999.1 .
D37978 Genomic DNA. Translation: BAA21036.1 .
PIRi A46088.
RefSeqi NP_476546.1. NM_057198.2.
UniGenei Rn.18690.

3D structure databases

ProteinModelPortali P35433.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000002905.

Protein family/group databases

MEROPSi C44.001.

PTM databases

PhosphoSitei P35433.

Proteomic databases

PaxDbi P35433.
PRIDEi P35433.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000002905 ; ENSRNOP00000002905 ; ENSRNOG00000002128 .
GeneIDi 117544.
KEGGi rno:117544.
UCSCi RGD:620237. rat.

Organism-specific databases

CTDi 5471.
RGDi 620237. Ppat.

Phylogenomic databases

eggNOGi COG0034.
GeneTreei ENSGT00390000003428.
HOGENOMi HOG000033688.
HOVERGENi HBG002589.
InParanoidi P35433.
KOi K00764.
OMAi IPVGDMN.
OrthoDBi EOG789C9W.
PhylomeDBi P35433.
TreeFami TF106370.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00124 .
Reactomei REACT_217264. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RK P35433.

Miscellaneous databases

NextBioi 620369.
PROi P35433.

Gene expression databases

Genevestigatori P35433.

Family and domain databases

Gene3Di 3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view ]
Pfami PF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view ]
PIRSFi PIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMi SSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01134. purF. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 117 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

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