ID   PUR5_STRPS              Reviewed;         340 AA.
AC   B2IR37;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=SPCG_0049;
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14;
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(2009).
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; CP001033; ACB89301.1; -; Genomic_DNA.
DR   RefSeq; WP_001284588.1; NC_010582.1.
DR   AlphaFoldDB; B2IR37; -.
DR   SMR; B2IR37; -.
DR   EnsemblBacteria; ACB89301; ACB89301; SPCG_0049.
DR   KEGG; spw:SPCG_0049; -.
DR   HOGENOM; CLU_047116_0_0_9; -.
DR   OMA; EPLFMTD; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001682; 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..340
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_1000193047"
SQ   SEQUENCE   340 AA;  36472 MW;  1EB06FCCE547377E CRC64;
     MANKNAYAQS GVDVEAGYEV VERIKKHVAR TERAGVMGAL GGFGGMFDLS KTGVKEPVLI
     SGTDGVGTKL MLAIKYDKHD TIGQDCVAMC VNDIIAAGAE PLYFLDYVAT GKNEPAKLEQ
     VVAGVAEGCV QAGAALIGGE TAEMPGMYGE DDYDLAGFAV GVAEKSQIID GSKVVEGDVL
     LGLASSGIHS NGYSLVRRVF ADYTGEEVLP ELEGKKLKEV LLEPTRIYVK AVLPLIKEEL
     VNGIAHITGG GFIENVPRMF ADDLAAEIDE SKVPVLPIFK ALEKYGQIKH EEMFEIFNMG
     VGLMLAVSPE NVERVKELLD EAVYEIGRIV KKENESVIIK