PUR1_CHICK
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 03-AUG-2022, entry version 133.
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; P28173; -.
DR GeneID; 422743; -.
DR KEGG; gga:422743; -.
DR CTD; 5471; -.
DR VEuPathDB; HostDB:geneid_422743; -.
DR eggNOG; KOG0572; Eukaryota.
DR InParanoid; P28173; -.
DR OrthoDB; 400911at2759; -.
DR Reactome; R-GGA-419140; De novo synthesis of IMP.
DR UniPathway; UPA00074; UER00124.
DR PRO; PR:P28173; -.
DR Proteomes; UP000000539; Unplaced.
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; IEA:UniProtKB-EC.
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 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 Pfam; PF00156; Pribosyltran; 1.
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; 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
