ID   PUR1_CHICK              Reviewed;         510 AA.
AC   P28173;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   08-NOV-2023, entry version 138.
DE   RecName: Full=Amidophosphoribosyltransferase;
DE            Short=ATase;
DE            EC=2.4.2.14 {ECO:0000269|PubMed:2123487};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000303|PubMed:2123487};
DE            Short=GPAT {ECO:0000303|PubMed:2123487};
DE   Flags: Precursor;
GN   Name=PPAT; Synonyms=GPAT {ECO:0000303|PubMed:2123487};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2123487; DOI=10.1016/s0021-9258(17)45339-7;
RA   Zhou G., Dixon J.E., Zalkin H.;
RT   "Cloning and expression of avian glutamine phosphoribosylpyrophosphate
RT   amidotransferase. Conservation of a bacterial propeptide sequence supports
RT   a role for posttranslational processing.";
RL   J. Biol. Chem. 265:21152-21159(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-42.
RX   PubMed=8336716; DOI=10.1128/mcb.13.8.4784-4792.1993;
RA   Gavalas A., Dixon J.E., Brayton K.A., Zalkin H.;
RT   "Coexpression of two closely linked avian genes for purine nucleotide
RT   synthesis from a bidirectional promoter.";
RL   Mol. Cell. Biol. 13:4784-4792(1993).
RN   [3]
RP   ERRATUM OF PUBMED:8336716.
RA   Gavalas A., Dixon J.E., Brayton K.A., Zalkin H.;
RL   Mol. Cell. Biol. 13:7977-7977(1993).
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine.
CC       {ECO:0000269|PubMed:2123487}.
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:2123487};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14907;
CC         Evidence={ECO:0000269|PubMed:2123487};
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   -!- 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:2123487}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00497}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
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DR   EMBL; M60069; AAA62736.1; -; mRNA.
DR   EMBL; L12533; AAA17895.1; -; Unassigned_DNA.
DR   PIR; A38337; A38337.
DR   RefSeq; NP_001004401.1; NM_001004401.1.
DR   AlphaFoldDB; P28173; -.
DR   SMR; P28173; -.
DR   STRING; 9031.ENSGALP00000022273; -.
DR   MEROPS; C44.001; -.
DR   PaxDb; 9031-ENSGALP00000022273; -.
DR   GeneID; 422743; -.
DR   KEGG; gga:422743; -.
DR   CTD; 5471; -.
DR   VEuPathDB; HostDB:geneid_422743; -.
DR   eggNOG; KOG0572; Eukaryota.
DR   InParanoid; P28173; -.
DR   Reactome; R-GGA-419140; De novo synthesis of IMP.
DR   UniPathway; UPA00074; UER00124.
DR   PRO; PR:P28173; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 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; Allosteric enzyme; Glutamine amidotransferase; Glycosyltransferase;
KW   Iron; Iron-sulfur; Magnesium; Metal-binding; Purine biosynthesis;
KW   Reference proteome; Transferase.
FT   PROPEP          1..11
FT                   /evidence="ECO:0000305|PubMed:2123487"
FT                   /id="PRO_0000029281"
FT   CHAIN           12..510
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000029282"
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         496
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P00497"
FT   BINDING         499
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P00497"
SQ   SEQUENCE   510 AA;  56257 MW;  F4371FE1FEC7C744 CRC64;
     MELEELGIRE ECGVFGCIAA GVWPTELDVP HVITLGLVGL QHRGQESAGI VTSDGESSQA
     FKVHKGMGLI NHVFNADSLK KLYVSNLGIG HTRYSTSGIS ELQNCQPFVV ETLHGKIAVA
     HNGELTNAVR LRRKLMRHGV GLSTSSDSEL ITQLLAFTPP LENDDTADWV ARIKNLMNET
     PTSYSLLIMH KDIIYAVRDP YGNRPLCIGR LIPVGDINGK GKDNSETEGW VVSSESCSFL
     SIGAEYYREV LPGEIVKISR YDVQTLDVVP RPEGDPSAFC IFEYVYFARP DSIFEGQMVY
     SVRRRCGQQL AIEAPVEADL VSTVPESATP AALGYAQKCG LPYVEVLCKN RYVGRTFIQP
     NMRLRQLGVA KKFGVLSDNF KGKRVVIIDD SIVRGNTISP IIKLLRESGA KEVHIRVASP
     PIRFPCYMGI NIPTKEELIA NRPEFHDLAN YIGADSVVYL SVEGLVSSVQ ESIKARKENE
     NSLKTQKSRV GKIGHCTACL TGDYPVELEW
//