ID PUR5_LATSS Reviewed; 342 AA. AC Q93MM7; Q38XW5; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 119. 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=LCA_0660; OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei OS subsp. sakei). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Latilactobacillus. OX NCBI_TaxID=314315; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11832506; DOI=10.1099/00221287-148-2-421; RA Dudez A.-M., Chaillou S., Hissler L., Stentz R., Champomier-Verges M.-C., RA Alpert C.-A., Zagorec M.; RT "Physical and genetic map of the Lactobacillus sakei 23K chromosome."; RL Microbiology 148:421-431(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=23K; RX PubMed=16273110; DOI=10.1038/nbt1160; RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V., RA Zagorec M.; RT "The complete genome sequence of the meat-borne lactic acid bacterium RT Lactobacillus sakei 23K."; RL Nat. Biotechnol. 23:1527-1533(2005). 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; AF401037; AAK92512.1; -; Genomic_DNA. DR EMBL; CR936503; CAI54964.1; -; Genomic_DNA. DR RefSeq; WP_011374369.1; NC_007576.1. DR AlphaFoldDB; Q93MM7; -. DR SMR; Q93MM7; -. DR STRING; 314315.LCA_0660; -. DR KEGG; lsa:LCA_0660; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_9; -. DR OrthoDB; 9802507at2; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000002707; 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; KW Reference proteome. FT CHAIN 1..342 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_0000148218" SQ SEQUENCE 342 AA; 36399 MW; 7F0C4561E12B266F CRC64; MTDAYQKAGV DVTAGYEVVA RIQKKVGADN HNIGSFGGQY ALEMAQYQKP VLVSSTDGVG TKLMVAFAAD QHATIGIDCV AMCVNDIVAQ GAQPLYFLDY LATGKTDPDK IEDIVAGVLE GCKQANMALI GGETAEMPGM YAAKHYDVAG FAVGIAEQDA LVTGETIQAG DVLIGLASSG IHSNGYSLVR KIFFEQNNLT VASQLPELPG KTLGDWLLTP TKIYVEDLQP LLQQRVIKGA AHITGGGFIE NVPRMLPADL AAHLTLGSWP ILPIFKALQQ YGQLAEMEMY NIFNMGIGMV LAVAPEAAPA VLAQLNAKQE QAYQIGTVQK RQQAAVELVT AK //