PUR1_RAT
ID PUR1_RAT Reviewed; 517 AA.
AC P35433;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000303|PubMed:8463258};
DE Short=ATase {ECO:0000303|PubMed:8463258};
DE EC=2.4.2.14 {ECO:0000269|PubMed:8463258};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE Short=GPAT;
DE Flags: Precursor;
GN Name=Ppat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-29, TISSUE SPECIFICITY,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8463258; DOI=10.1016/s0021-9258(18)53167-7;
RA Iwahana H., Yamaoka T., Mizutani M., Mizusawa N., Ii S., Yoshimoto K.,
RA Itakura M.;
RT "Molecular cloning of rat amidophosphoribosyltransferase.";
RL J. Biol. Chem. 268:7225-7237(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7742366; DOI=10.1016/0167-4781(95)00036-g;
RA Iwahana H., Honda S., Tsujisawa T., Takahashi Y., Adzuma K., Katashima R.,
RA Yamaoka T., Moritani M., Yoshimoto K., Itakura M.;
RT "Rat genomic structure of amidophosphoribosyltransferase, cDNA sequence of
RT aminoimidazole ribonucleotide carboxylase, and cell cycle-dependent
RT expression of these two physically linked genes.";
RL Biochim. Biophys. Acta 1261:369-380(1995).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine.
CC {ECO:0000269|PubMed:8463258}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14;
CC Evidence={ECO:0000269|PubMed:8463258};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14907;
CC Evidence={ECO:0000305|PubMed:8463258};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00497};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00497};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P00497};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P00497};
CC -!- ACTIVITY REGULATION: Activated by the substrate 5-phospho-alpha-D-
CC ribosyl-1-pyrophosphate and inhibited by the purine ribonucleotides,
CC the end products of purine biosynthesis.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000269|PubMed:8463258}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00497}.
CC -!- TISSUE SPECIFICITY: Expressed at a high level in brain, heart, liver
CC and stomach. {ECO:0000269|PubMed:8463258}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; D10853; BAA01626.1; -; mRNA.
DR EMBL; BC086999; AAH86999.1; -; mRNA.
DR EMBL; D37978; BAA21036.1; -; Genomic_DNA.
DR PIR; A46088; A46088.
DR RefSeq; NP_476546.1; NM_057198.2.
DR AlphaFoldDB; P35433; -.
DR SMR; P35433; -.
DR STRING; 10116.ENSRNOP00000002905; -.
DR MEROPS; C44.001; -.
DR iPTMnet; P35433; -.
DR PhosphoSitePlus; P35433; -.
DR jPOST; P35433; -.
DR PaxDb; P35433; -.
DR PRIDE; P35433; -.
DR Ensembl; ENSRNOT00000002905; ENSRNOP00000002905; ENSRNOG00000002128.
DR GeneID; 117544; -.
DR KEGG; rno:117544; -.
DR UCSC; RGD:620237; rat.
DR CTD; 5471; -.
DR RGD; 620237; Ppat.
DR eggNOG; KOG0572; Eukaryota.
DR GeneTree; ENSGT00390000003428; -.
DR HOGENOM; CLU_022389_3_1_1; -.
DR InParanoid; P35433; -.
DR OMA; ENAQPTF; -.
DR OrthoDB; 400911at2759; -.
DR PhylomeDB; P35433; -.
DR TreeFam; TF106370; -.
DR Reactome; R-RNO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR SABIO-RK; P35433; -.
DR UniPathway; UPA00074; UER00124.
DR PRO; PR:P35433; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002128; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; P35433; RN.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; ISO:RGD.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:RGD.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEP:RGD.
DR GO; GO:0006543; P:glutamine catabolic process; IDA:RGD.
DR GO; GO:0006177; P:GMP biosynthetic process; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IDA:RGD.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Allosteric enzyme; Direct protein sequencing;
KW Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW Magnesium; Metal-binding; Purine biosynthesis; Reference proteome;
KW Transferase.
FT PROPEP 1..11
FT /evidence="ECO:0000269|PubMed:8463258"
FT /id="PRO_0000029285"
FT CHAIN 12..517
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000029286"
FT DOMAIN 12..261
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 280
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 426
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 503
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 506
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q06203"
SQ SEQUENCE 517 AA; 57437 MW; 8AD3D05A380C120F CRC64;
MELEESGIRE ECGVFGCIAS GDWPTQLDVP HVITLGLVGL QHRGQESAGI VTSDGSSVPK
FRVHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC ELENCQPFVV ETLHGKIAVA
HNGELVNAAR LRKKLLRHGI GLSTSSDSEM ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA
PAAYSLVIMH RDVIYAVRDP YGNRPLCIGR LMPVSDINDK EKKSSETEGW VVSSESCSFL
SIGARYCHEV KPGEIVEISR HGVRTLDIIP RSNGDPVAFC IFEYVYFARP DSMFEDQMVY
TVRYRCGQQL AVEAPVEADL VSTVPESATP AALGYATKCG LPYVEVLCKN RYVGRTFIQP
NMRLRQLGVA KKFGVLSDNF KGKRIVLIDD SIVRGNTISP IIKLLKESGA KEVHIRVASP
PIKHPCFMGI NIPTKEELIA NKPEFEYLAE YLGANSVVYL SVEGLVSSVQ QEIKFKKQKV
KKRDITIQEN GNGLEYFEKT GHCTACLTGQ YPVDLEW
