ID PUR1_VIGAC Reviewed; 485 AA. AC P52419; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 108. 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; Fragment; GN Name=PUR1; OS Vigna aconitifolia (Moth bean) (Phaseolus aconitifolius). 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; Vigna. OX NCBI_TaxID=3918; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L23834; AAA73944.1; -; mRNA. DR PIR; T10792; T10792. DR AlphaFoldDB; P52419; -. DR SMR; P52419; -. DR MEROPS; C44.001; -. DR UniPathway; UPA00074; UER00124. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; 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 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 2: Evidence at transcript level; KW 4Fe-4S; Chloroplast; Glutamine amidotransferase; Glycosyltransferase; Iron; KW Iron-sulfur; Magnesium; Metal-binding; Plastid; Purine biosynthesis; KW Transferase; Transit peptide. FT TRANSIT <1..18 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 19..485 FT /note="Amidophosphoribosyltransferase, chloroplastic" FT /id="PRO_0000029290" FT DOMAIN 19..237 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" FT ACT_SITE 19 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" FT BINDING 253 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 300 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 362 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 363 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 399 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 450 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 453 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT NON_TER 1 SQ SEQUENCE 485 AA; 53205 MW; EE9CD20AE5BEDD82 CRC64; KTTNTFASVN DDEKPREECG VVGIYGDPEA SRLCSLALHA LQHRGQEGAG IVAVHDNLFH QVNGVGLVSD VFNEAKLSEL PGSCAIGHVR YSTAGHSKLV NVQPFVAGYR FGSVAVAHNG NFVNYRSLRA KLEDNGSIFN TTSDTEVVLH LIATSKHRPF LLRVVDACEN LKGAYSLVFL TEDKLVAVRD FGFRPLVMGR RKNGAVVFAS ETCALDLIDA TYEREVNPGE VVVVDHTGIQ SLCLVTHQEP KQCIFEHIYF ALPNSVVFGR SVYESRRKFG EILATESPVE CDVVIAVPDS GVVAALGYAA KAGVPFQQGL IRSHHVGRTF IEPSQKIRDF GVKLKLFPVR GVLEGKRVVV VDDSIVRGTT SSKIVRLIKE AGAKEVHMRI ACPPIVASCY YGVDTPSKEE LISNRMDVEE IRKFIGSDSL AFLPLDTLKS LLEDDAPNYC YACFSGKYPV QPENLNPTAS MSLTGTMFQW QFETY //