ID PUR5_AERS4 Reviewed; 345 AA. AC A4SL28; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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=ASA_1510; OS Aeromonas salmonicida (strain A449). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449; RX PubMed=18801193; DOI=10.1186/1471-2164-9-427; RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., RA Brown L.L.; RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into RT the evolution of a fish pathogen."; RL BMC Genomics 9:427-427(2008). 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; CP000644; ABO89600.1; -; Genomic_DNA. DR RefSeq; WP_005320174.1; NC_009348.1. DR AlphaFoldDB; A4SL28; -. DR SMR; A4SL28; -. DR STRING; 29491.GCA_000820065_04002; -. DR KEGG; asa:ASA_1510; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_6; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000225; 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..345 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000046418" SQ SEQUENCE 345 AA; 36697 MW; 8A31977A83C94AF1 CRC64; MTDKTSLSYK DAGVDIDAGN ALVERIKGVS KRTRRPEVLG GLGGFGALCQ IPAGYKEPVL VSGTDGVGTK LRLAIDLKKH DTVGIDLVAM CVNDLIVQGA EPLFFLDYYA TGKLDVDTAA AVVTGIGVGC EQSGCALVGG ETAEMPGMYE GEDYDIAGFC VGVVEKSEII DGSKVGDGDA LIALAASGPH SNGFSLVRKI LEVSKADVHQ PLGDTTLASA LLEPTRIYVK PVLKLIKECE IHALSHITGG GFWENIPRVL PANTQAVIDE QSWQWPAVFS WLQQAGNVTR HEMYRTFNCG VGMIIALPAD QLEKALTLLK AEGENAWHIG HIAKAVDGEE QVIIQ //