ID PUR5_BRUA4 Reviewed; 363 AA. AC A6X235; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, 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=Oant_2576; OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=439375; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / RC NBRC 15819 / NCTC 12168 / Alc 37; RX PubMed=21685287; DOI=10.1128/jb.05335-11; RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., RA Ugalde R.A., Garcia E., Tolmasky M.E.; RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic RT pathogen and symbiont of several eukaryotic hosts."; RL J. Bacteriol. 193:4274-4275(2011). 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; CP000758; ABS15289.1; -; Genomic_DNA. DR RefSeq; WP_012092376.1; NC_009667.1. DR AlphaFoldDB; A6X235; -. DR SMR; A6X235; -. DR STRING; 439375.Oant_2576; -. DR KEGG; oan:Oant_2576; -. DR PATRIC; fig|439375.7.peg.2714; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_5; -. DR PhylomeDB; A6X235; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000002301; Chromosome 1. 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..363 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000046452" SQ SEQUENCE 363 AA; 37811 MW; 2C1FFA529F252DE6 CRC64; MTMENKPADK PVGQNGLTYA QAGVDIDAGN LMVEKIKPLV RSTRRPGADG EIGGFGGLFD LKAAGFKDPV LVAANDGVGT KLKIAIDADK HDTVGIDLVA MCVNDLVVQG AEPLFFLDYF ATGKLSPDQG VDIVAGIAEG CRQAGSALIG GETAEMPGMY RDGDYDLAGF AVGAAERDRL LPRGDIAEGD VILGLASSGV HSNGFSLVRR IVELSGLGWK SDAPFQPGAT LGEALLTPTR IYVKPLLAAI RASDGIKALA HITGGGFPDN IPRVLPEGLA AEIDLESISV PAVFSWLAKT GGVEPNEMLR TFNCGIGMIA VVKPEKVEEV VAALAAEGEK VVTLGQMVKR DKDGVVYKGT LSL //