ID Q9CBC2_MYCLE Unreviewed; 364 AA. AC Q9CBC2; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 02-SEP-2026, entry version 139. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367, ECO:0000256|HAMAP-Rule:MF_00741}; DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047, ECO:0000256|HAMAP-Rule:MF_00741}; DE AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931, ECO:0000256|HAMAP-Rule:MF_00741}; DE AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093, ECO:0000256|HAMAP-Rule:MF_00741}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908, ECO:0000256|HAMAP-Rule:MF_00741}; GN Name=purM {ECO:0000256|HAMAP-Rule:MF_00741, GN ECO:0000313|EMBL:CAC31160.1}; GN OrderedLocusNames=ML2205 {ECO:0000313|EMBL:CAC31160.1}; OS Mycobacterium leprae (strain TN). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC31160.1, ECO:0000313|Proteomes:UP000000806}; RN [1] {ECO:0000313|EMBL:CAC31160.1, ECO:0000313|Proteomes:UP000000806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN {ECO:0000313|EMBL:CAC31160.1, RC ECO:0000313|Proteomes:UP000000806}; RX PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). 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 + phosphate + CC H(+); Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, CC ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000256|ARBA:ARBA00049057, ECO:0000256|HAMAP- CC 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. CC {ECO:0000256|ARBA:ARBA00004686, ECO:0000256|HAMAP-Rule:MF_00741}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}. CC -!- SIMILARITY: Belongs to the AIR synthase family. CC {ECO:0000256|ARBA:ARBA00010280, ECO:0000256|HAMAP-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; AL583924; CAC31160.1; -; Genomic_DNA. DR PIR; H87184; H87184. DR RefSeq; WP_010908766.1; NC_002677.1. DR AlphaFoldDB; Q9CBC2; -. DR SMR; Q9CBC2; -. DR STRING; 272631.gene:17576062; -. DR KEGG; mle:ML2205; -. DR PATRIC; fig|272631.5.peg.4177; -. DR Leproma; ML2205; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_11; -. DR OrthoDB; 9777881at2; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000806; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:TreeGrafter. 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 GO; GO:0046084; P:adenine biosynthetic process; IEA:TreeGrafter. DR CDD; cd02196; PurM; 1. DR FunFam; 3.30.1330.10:FF:000001; Phosphoribosylformylglycinamidine cyclo-ligase; 1. DR FunFam; 3.90.650.10:FF:000016; Phosphoribosylformylglycinamidine cyclo-ligase; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00741}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00741}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00741}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00741}; KW Reference proteome {ECO:0000313|Proteomes:UP000000806}. FT DOMAIN 69..174 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 186..352 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" SQ SEQUENCE 364 AA; 38352 MW; A51DD47CB3BEABD0 CRC64; MMDPGKSPGG QLGNHGITYA STGVDIEAGD RSVELFKPMA VKAIRTEVLG GLGGFAGLFA LRSGYREPVL AASTDGVGTK LAVAQAMDKH DTVGLDLVAM VVDDLVVCGA EPLFLQDYIA VGRTVPERLS AIVDGIAEGC MLAGCALLGG ETAEHPGLME VDHYDIAATG VGVVEADDTL GPDRVKPGDV IIALRSSGLH SNGYSLARSV LLEIDRMNLA GYVEEFGRTL GEELLEPTRI YAKDCLALAA ETHVRTFCHV TGGGLAGNLQ RVIPHGLVAE VDRGTWTPAP VFAMIAQRGR VAREEMEKTF NMGVGMIAVV APEDTDRALA ILTARHLDCW VLGTVCKGSK VGPRAKLVGQ HPRF //