ID PUR5_AERHH Reviewed; 345 AA. AC A0KM24; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 93. 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=AHA_2821; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / RC KCTC 2358 / NCIMB 9240 / NCTC 8049; RX PubMed=16980456; DOI=10.1128/jb.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."; RL J. Bacteriol. 188:8272-8282(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; CP000462; ABK37366.1; -; Genomic_DNA. DR RefSeq; WP_011706623.1; NC_008570.1. DR RefSeq; YP_857325.1; NC_008570.1. DR AlphaFoldDB; A0KM24; -. DR SMR; A0KM24; -. DR STRING; 380703.AHA_2821; -. DR EnsemblBacteria; ABK37366; ABK37366; AHA_2821. DR KEGG; aha:AHA_2821; -. DR PATRIC; fig|380703.7.peg.2831; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_6; -. DR OrthoDB; 9777881at2; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000756; 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..345 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000046417" SQ SEQUENCE 345 AA; 36759 MW; B20B308F4F4C3490 CRC64; MTDKTSLSYK DAGVDIDAGN ALVERIKGVS KRTRRPEVLG GLGGFGALCQ IPAGYKEPVL VSGTDGVGTK LRLAIDLKKH DTVGIDLVAM CVNDLIVQGA EPLFFLDYYA TGKLDVDTAA AVVTGIGAGC EQSGCALVGG ETAEMPGMYE GEDYDIAGFC VGVVEKSEII DGSKVGEGDA LIALAASGPH SNGFSLVRKI LEVSKADVQQ PLGDTTLANA LLEPTRIYVK PVLKLIKECE IHALSHITGG GFWENIPRVL PANTQAVIDE QSWQWPAVFS WLQQAGNVTR HEMYRTFNCG VGMIIALPAD QLEKALTLLK TEGENAWHIG YITKAADGEE QVIIQ //