ID   PUR5_STRSU              Reviewed;         340 AA.
AC   Q9F1T6;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
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};
OS   Streptococcus suis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DAT1 / Serotype 2;
RX   PubMed=11133943; DOI=10.1128/jb.183.2.500-511.2001;
RA   Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.;
RT   "Evidence for horizontal transfer of the SsuDAT1I restriction-modification
RT   genes to the Streptococcus suis genome.";
RL   J. Bacteriol. 183:500-511(2001).
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; AB045609; BAB20825.1; -; Genomic_DNA.
DR   RefSeq; WP_009908859.1; NZ_VKJM01000010.1.
DR   AlphaFoldDB; Q9F1T6; -.
DR   SMR; Q9F1T6; -.
DR   STRING; 996306.SSUR61_1390; -.
DR   UniPathway; UPA00074; UER00129.
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_0000148265"
SQ   SEQUENCE   340 AA;  36358 MW;  E043F5BD1BE19288 CRC64;
     MTNKNAYAQS GVDVEAGYEV VERIKKHVAR TERLGVMGAL GGFGGMFDLT KLDVKEPVLV
     SGTDGVGTKL MLAIQYDKHD TIGQDCVAMC VNDIIAAGAE PLYFLDYIAT GKNEPAKLEQ
     VVAGVAEGCV QAGCGLIGGE TAEMPGMYGE DDYDLAGFAV GIAEKYQIID GSKVKEGDIL
     LGLASSGIHS NGYSLVRRVF ADVSGDALLP ELNGRALKDV LLEPTRIYVQ QVLPLVKAGL
     VNGIAHITGG GFIENVPRMF ADNLAAEIEE DKIPVLPIFT ALEKYGKIKH EEMFEIFNMG
     IGLVLAVSPD KVDSVCQLVD EEVYTIGRII AKEDKSVVIK