ID PUR1_MYCBO Reviewed; 527 AA. AC P65830; A0A1R3XWI2; O06626; X2BG87; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931}; DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Flags: Precursor; GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; GN OrderedLocusNames=BQ2027_MB0831; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01931}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01931}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01931}; 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:0000255|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|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; LT708304; SIT99430.1; -; Genomic_DNA. DR RefSeq; NP_854489.1; NC_002945.3. DR AlphaFoldDB; P65830; -. DR SMR; P65830; -. DR MEROPS; C44.001; -. DR PATRIC; fig|233413.5.peg.903; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. 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. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW 4Fe-4S; Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur; KW Magnesium; Metal-binding; Purine biosynthesis; Reference proteome; KW Transferase. FT PROPEP 1..34 FT /evidence="ECO:0000250" FT /id="PRO_0000029259" FT CHAIN 35..527 FT /note="Amidophosphoribosyltransferase" FT /id="PRO_0000029260" FT DOMAIN 35..261 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..29 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 35 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 276 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 323 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 385 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 386 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 422 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 478 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 481 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" SQ SEQUENCE 527 AA; 56162 MW; A2FE9D1DD08FA572 CRC64; MAVDSDYVTD RAAGSRQTVT GQQPEQDLNS PREECGVFGV WAPGEDVAKL TYYGLYALQH RGQEAAGIAV ADGSQVLVFK DLGLVSQVFD EQTLAAMQGH VAIGHCRYST TGDTTWENAQ PVFRNTAAGT GVALGHNGNL VNAAALAARA RDAGLIATRC PAPATTDSDI LGALLAHGAA DSTLEQAALD LLPTVRGAFC LTFMDENTLY ACRDPYGVRP LSLGRLDRGW VVASETAALD IVGASFVRDI EPGELLAIDA DGVRSTRFAN PTPKGCVFEY VYLARPDSTI AGRSVHAARV EIGRRLAREC PVEADLVIGV PESGTPAAVG YAQESGVPYG QGLMKNAYVG RTFIQPSQTI RQLGIRLKLN PLKEVIRGKR LIVVDDSIVR GNTQRALVRM LREAGAVELH VRIASPPVKW PCFYGIDFPS PAELIANAVE NEDEMLEAVR HAIGADTLGY ISLRGMVAAS EQPTSRLCTA CFDGKYPIEL PRETALGKNV IEHMLANAAR GAALGELAAD DEVPVGR //