ID A0R8Z7_BACAH Unreviewed; 477 AA. AC A0R8Z7; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931}; DE Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931}; DE EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931}; DE Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931}; GN Name=purF {ECO:0000256|HAMAP-Rule:MF_01931, GN ECO:0000313|EMBL:ABK83690.1}; GN OrderedLocusNames=BALH_0289 {ECO:0000313|EMBL:ABK83690.1}; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK83690.1, ECO:0000313|Proteomes:UP000000761}; RN [1] {ECO:0000313|EMBL:ABK83690.1, ECO:0000313|Proteomes:UP000000761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK83690.1, RC ECO:0000313|Proteomes:UP000000761}; RX PubMed=17337577; DOI=10.1128/JB.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP- CC Rule:MF_01931}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-2}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01931, CC ECO:0000256|PIRSR:PIRSR000485-2}; 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:0000256|ARBA:ARBA00005209, CC ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}. CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138, CC ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01931}. 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; CP000485; ABK83690.1; -; Genomic_DNA. DR AlphaFoldDB; A0R8Z7; -. DR MEROPS; C44.001; -. DR KEGG; btl:BALH_0289; -. DR HOGENOM; CLU_022389_3_1_9; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000000761; Chromosome. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. 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: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. PE 3: Inferred from homology; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_01931}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485- KW 2}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRSR:PIRSR000485-2}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01931}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485}. FT DOMAIN 18..236 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" FT ACT_SITE 18 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-1" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-2" FT BINDING 361 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-2" FT BINDING 362 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-2" SQ SEQUENCE 477 AA; 52089 MW; E92AA1B798521BB8 CRC64; MERGNPMLAE IKGLNEECGV FGIWGHENAA QVSYYGLHSL QHRGQEGAGI VVNNGEKIVG HKGLGLISEV FSRGELEGLN GKSAIGHVRY ATAGGSEVAN VQPLLFRFSD HSMALAHNGN LINAKMLRRE LEAEGSIFQT SSDTEVLLHL IKRSTKDSLI ESVKEALNKV KGAFAYLLLT GNEMIVALDP NGFRPLSIGK MGDAYVVASE TCAFDVVGAT YIRDVEPGEL LIINDEGIHV DRFTNEVDHA ICSMEYIYFA RPDSNIAGIN VHAARKNMGK RLAAEAPIEA DVVTGVPDSS ISAAIGYAEA TGIPYELGLI KNRYVGRTFI QPSQELREQG VKMKLSAVRG VVEGKRVVMI DDSIVRGTTS KRIVRMLREA GATEVHVRIA SPPLKYPCFY GIDIQTRKEL IAANHTVEEI REMIGADSLT FLSEDGLVDA IGRPYEGKYG GLCMAYFNGD YPTALYDYEQ ELLESMK //