ID   PUR1_SOYBN              Reviewed;         569 AA.
AC   P52418;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Amidophosphoribosyltransferase, chloroplastic;
DE            Short=ATase;
DE            EC=2.4.2.14;
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE            Short=GPAT;
DE   Flags: Precursor;
GN   Name=PUR1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Prize; TISSUE=Root nodule;
RX   PubMed=7894513; DOI=10.1046/j.1365-313x.1995.07010077.x;
RA   Kim J.H., Delauney A.J., Verma D.P.S.;
RT   "Control of de novo purine biosynthesis genes in ureide-producing legumes:
RT   induction of glutamine phosphoribosylpyrophosphate amidotransferase gene
RT   and characterization of its cDNA from soybean and Vigna.";
RL   Plant J. 7:77-86(1995).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
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DR   EMBL; L23833; AAA73943.1; -; mRNA.
DR   PIR; T07158; T07158.
DR   RefSeq; NP_001238270.1; NM_001251341.1.
DR   AlphaFoldDB; P52418; -.
DR   SMR; P52418; -.
DR   STRING; 3847.P52418; -.
DR   MEROPS; C44.001; -.
DR   PaxDb; 3847-GLYMA04G00930-1; -.
DR   ProMEX; P52418; -.
DR   GeneID; 548065; -.
DR   KEGG; gmx:548065; -.
DR   eggNOG; KOG0572; Eukaryota.
DR   InParanoid; P52418; -.
DR   OrthoDB; 4975at2759; -.
DR   SABIO-RK; P52418; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:SF27; AMIDOPHOSPHORIBOSYLTRANSFERASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   Pfam; PF00156; Pribosyltran; 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   2: Evidence at transcript level;
KW   4Fe-4S; Chloroplast; Glutamine amidotransferase; Glycosyltransferase; Iron;
KW   Iron-sulfur; Magnesium; Metal-binding; Plastid; Purine biosynthesis;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..80
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           81..569
FT                   /note="Amidophosphoribosyltransferase, chloroplastic"
FT                   /id="PRO_0000029289"
FT   DOMAIN          81..301
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   BINDING         317
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         426
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         514
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         517
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   569 AA;  62205 MW;  33E36AB22F616491 CRC64;
     MAAASNLSTL SSSSLSKPSS SFPFRNTPTN NNASFLHNKS LPNQNSLSHK LSSPLPLACN
     PKNQNTCVFF DDEDQKPREE CGVVGIYGDP EASRLCSLAL HALQHRGQEG AGIVAVHDNH
     LQSVTGVGLV SDVFEQSKLS RLPGTSAIGH VRYSTAGQSM LKNVQPFLAD YRFAAVAVAH
     NGNFVNYRSL RARLEHNNGS IFNTTSDTEV VLHLIATSKH RPFLLRIVDA CEHLQGAYSL
     VFVTEDKLVA VRDPFGFRPL VMGRRTNGAV VLASETCALD LIEATYEREV YPGEVIVVDH
     TGIQSLCLVS HPEPKQCIFE HIYFALPNSV VFGRSVYESR KKFGEILASE SPVECDVVIA
     VPDSGVVAAL GYAAKAGVPF QQGLIRSHYV GRTFIEPSQK IRDFGVKLKL SPVHAVLEGK
     RVVVVDDSIV RGTTSSKIVR LLKEAGAKEV HMRIACPPIV ASCYYGVDTP SSEELISNRM
     SVEEIRKFIG SDSLAFLPLD KLKTLLGDDA LNYCYACFSG KYPVEPEELQ MKRLGVAHFN
     WDDDFNGNFE SIDVGGWVTN QDGFKIGSV
//