ID PUR5_PSEAE Reviewed; 353 AA. AC Q9I513; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-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}; OrderedLocusNames=PA0945; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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; AE004091; AAG04334.1; -; Genomic_DNA. DR PIR; A83529; A83529. DR RefSeq; NP_249636.1; NC_002516.2. DR RefSeq; WP_003112583.1; NZ_QZGE01000007.1. DR AlphaFoldDB; Q9I513; -. DR SMR; Q9I513; -. DR STRING; 208964.PA0945; -. DR PaxDb; 208964-PA0945; -. DR DNASU; 879549; -. DR GeneID; 879549; -. DR KEGG; pae:PA0945; -. DR PATRIC; fig|208964.12.peg.981; -. DR PseudoCAP; PA0945; -. DR HOGENOM; CLU_047116_0_0_6; -. DR InParanoid; Q9I513; -. DR OrthoDB; 9777881at2; -. DR PhylomeDB; Q9I513; -. DR BioCyc; PAER208964:G1FZ6-965-MONOMER; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. 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..353 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_0000148233" SQ SEQUENCE 353 AA; 37123 MW; F50169F97482E553 CRC64; MSSKQPSLSY KDAGVDIDAG EALVERIKGV AKRTARPEVM GGLGGFGALC EIPAGYKQPV LVSGTDGVGT KLRLALNLNK HDSIGQDLVA MCVNDLVVCG AEPLFFLDYY ATGKLNVDVA ATVVTGIGAG CELAGCSLVG GETAEMPGMY EGEDYDLAGF CVGVVEKAEI IDGSRVQAGD ALIALPSSGP HSNGYSLIRK IIEVSGADIA QVQLDGKPLA DLLMAPTRIY VKPLLQLIKQ TGAVKAMAHI TGGGLLDNIP RVLPDNAQAV IDVASWNRPA VFDWLQEQGN VDETEMHRVL NCGVGMVICV AQSDAEKALE VLRAAGEQPW QIGRIETCGA DAERVVLNNL KNH //