PUR1_SOYBN
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 03-AUG-2022, entry version 124.
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.GLYMA04G00930.1; -.
DR MEROPS; C44.001; -.
DR PRIDE; P52418; -.
DR ProMEX; P52418; -.
DR GeneID; 548065; -.
DR KEGG; gmx:548065; -.
DR eggNOG; KOG0572; Eukaryota.
DR InParanoid; P52418; -.
DR OrthoDB; 400911at2759; -.
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; -; 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; PF13537; GATase_7; 1.
DR Pfam; PF00156; Pribosyltran; 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 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
