ID PUR5_STRTD Reviewed; 339 AA. AC Q03MZ8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 90. 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=STER_0052; OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=322159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-491 / LMD-9; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000419; ABJ65424.1; -; Genomic_DNA. DR RefSeq; WP_011680592.1; NC_008532.1. DR AlphaFoldDB; Q03MZ8; -. DR SMR; Q03MZ8; -. DR KEGG; ste:STER_0052; -. 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..339 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000046478" SQ SEQUENCE 339 AA; 36323 MW; 7FDB73313040794B CRC64; MSKNAYAQSG VDVEAGYEVV ERIKKHVART ERAGVMGGLG GFGGMFDLSK TGVKEPVLIS GTDGVGTKLM LAIKYDKHDT IGQDCVAMCV NDIIAAGAEP LYFLDYVATG KNEPAKLEQV VAGVAEGCVQ SGVALIGGET AEMPGMYGED DYDLAGFAVG VAEKSQIIDG SKVAEGDVLL GLASSGIHSN GYSLVRRVFA DYTGEEVLPE LEGQKLKDVL LEPTRIYVKA ALPLIKEELV NGIAHITGGG FIENVPRMFS DDLAAEIDES KVPVLPIFKA LEKYGEIKHE EMFEIFNMGI GLMFAVKPEN VERVKELLDE PVYEIGRIVK KDGASVVIK //