ID PUR5_LISW6 Reviewed; 349 AA. AC A0AJM1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 92. 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=lwe1785; OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 / OS NCTC 11857 / SLCC 5334 / V8). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=386043; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / RC V8; RX PubMed=16936040; DOI=10.1128/jb.00758-06; RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T., RA Lampidis R., Kreft J., Goebel W., Chakraborty T.; RT "Whole-genome sequence of Listeria welshimeri reveals common steps in RT genome reduction with Listeria innocua as compared to Listeria RT monocytogenes."; RL J. Bacteriol. 188:7405-7415(2006). 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; AM263198; CAK21203.1; -; Genomic_DNA. DR RefSeq; WP_011702562.1; NC_008555.1. DR AlphaFoldDB; A0AJM1; -. DR SMR; A0AJM1; -. DR STRING; 386043.lwe1785; -. DR GeneID; 61189683; -. DR KEGG; lwe:lwe1785; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_9; -. DR OrthoDB; 9802507at2; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000779; Chromosome. 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..349 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000046443" SQ SEQUENCE 349 AA; 37653 MW; C3248374200293A8 CRC64; MAENAYSKAG VDVEAGYQVV ERIKKHVART ERMGVMGALG SFGGMFDLSS LNLKEPVLVS GTDGVGTKLL LAIEADKHDT IGIDCVAMCV NDILAQGAEP LFFLDYIATG KTDPIKMEQI VKGVADGCEQ AGAALIGGET AEMPDMYGAD DYDLAGFTVG AVEKKKLITE GAVKAGDTLI GIPSSGIHSN GYSLVRKIFF KDNDFKLNAE ITELDVPLVE ELLKPTRIYV KPVLEVLKKV DVHGITHVTG GGFVENLPRM LTKDLAVKVE LGSWPILPIF DVMQKYGQLN ELEMYEIFNM GIGMVLAVKK EDVEKTLEVL VQNGEAAYVI GEVTTRENDS VIFSGGLNK //