PUR5_BACC4
ID PUR5_BACC4 Reviewed; 346 AA.
AC B7H4T8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=BCB4264_A0342;
OS Bacillus cereus (strain B4264).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405532;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4264;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus B4264.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001176; ACK58990.1; -; Genomic_DNA.
DR RefSeq; WP_001262439.1; NZ_VEHB01000009.1.
DR AlphaFoldDB; B7H4T8; -.
DR SMR; B7H4T8; -.
DR EnsemblBacteria; ACK58990; ACK58990; BCB4264_A0342.
DR GeneID; 67505027; -.
DR KEGG; bcb:BCB4264_A0342; -.
DR HOGENOM; CLU_047116_0_0_9; -.
DR OMA; EPLFMTD; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000007096; 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; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..346
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_1000192994"
SQ SEQUENCE 346 AA; 37288 MW; 8912A1596E8C4EB9 CRC64;
MANAYKQAGV DIEAGYEAVS RMKKHVQTTM RKEVLGGLGG FGGMFDLSKF ALEEPVLVSG
TDGVGTKLML AFMADKHDTI GIDAVAMCVN DIVVQGAEPL FFLDYIACGK AEPSKIENIV
KGISEGCRQA GCALIGGETA EMPGMYSTEE YDLAGFTVGI VDKKKIVTGE KIEAGHVLIG
LASSGIHSNG YSLVRKVLLE DGELSLERIY GRLELPLGEE LLKPTKIYVK PILELLKKHE
VYGMAHITGG GFIENIPRML PEGIGAEIEL GSWEIQPIFS LLQEVGKLEE KEMFNIFNMG
IGMVVAVKEE DAKDVVRLLE EQGEMARIIG RTIQGAGVTF NGGTAL
