ID PUR5_BACAC Reviewed; 346 AA. AC C3L534; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741}; DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741}; GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741}; GN OrderedLocusNames=BAMEG_0354; OS Bacillus anthracis (strain CDC 684 / NRRL 3495). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=568206; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 684 / NRRL 3495; RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C., RA Sutton G., Sims D.; RT "Genome sequence of Bacillus anthracis str. CDC 684."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00741}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_00741}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}. CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000255|HAMAP- CC Rule:MF_00741}. 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; CP001215; ACP13155.1; -; Genomic_DNA. DR RefSeq; WP_001262436.1; NC_012581.1. DR AlphaFoldDB; C3L534; -. DR SMR; C3L534; -. DR GeneID; 45020355; -. DR KEGG; bah:BAMEG_0354; -. DR HOGENOM; CLU_047116_0_0_9; -. DR UniPathway; UPA00074; UER00129. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02196; PurM; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_00741; AIRS; 1. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR004733; PurM_cligase. DR NCBIfam; TIGR00878; purM; 1. DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1. DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis. FT CHAIN 1..346 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000148265" SQ SEQUENCE 346 AA; 37256 MW; 6A4825D9FF515A43 CRC64; MANAYKQAGV DIEAGYEAVS RMKKHVQTTM RKEVLGGLGG FGGMFDLSKF ALEEPVLVSG TDGVGTKLML AFMADKHDTI GIDAVAMCVN DIVVQGAEPL FFLDYIACGK AEPSKIENIV KGISEGCRQA GCALIGGETA EMPGMYSTEE YDLAGFTVGI VDKKKIVTGE KIEAGHVLIG LASSGIHSNG YSLVRKVLLE DGELSLDRIY GRLELPLGEE LLKPTKIYVK PILELLKNHE VYGMAHITGG GFIENIPRML PEGIGAEIEL GSWKIQPIFS LLQEVGKLEE KEMFNIFNMG IGMVVAVKEE DAKDIVRLLE EQGETARIIG RTVQGAGVTF NGGKAL //