ID   PUR5_STAES              Reviewed;         343 AA.
AC   Q8CT29;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE            EC=6.3.3.1;
DE   AltName: Full=AIR synthase;
DE   AltName: Full=AIRS;
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN   Name=purM; OrderedLocusNames=SE_0769;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO04366.1; -; Genomic_DNA.
DR   RefSeq; NP_764324.1; NC_004461.1.
DR   RefSeq; WP_001831685.1; NZ_WBME01000028.1.
DR   AlphaFoldDB; Q8CT29; -.
DR   SMR; Q8CT29; -.
DR   GeneID; 50019091; -.
DR   KEGG; sep:SE_0769; -.
DR   PATRIC; fig|176280.10.peg.741; -.
DR   eggNOG; COG0150; Bacteria.
DR   HOGENOM; CLU_047116_0_0_9; -.
DR   OrthoDB; 9802507at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001411; 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.
FT   CHAIN           1..343
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000148251"
SQ   SEQUENCE   343 AA;  37391 MW;  EDA595E1C7ADDBD1 CRC64;
     MSKAYEESGV NIQAGYEAVE RITSHVERTL RKEVLGGLGG FGATFDLSQL KMKAPVLVSG
     TDGVGTKLKL AIDYGKHDTI GIDAVAMCVN DILTTGAEPL YFLDYIATNK VVPSTIEQIV
     KGISDGCEQT NTALIGGETA EMGEMYHEGE YDIAGFAVGA VEKEDYIDGS NVEEGQAIIG
     LASSGIHSNG YSLVRKMIKE SGVQLHDQFN GQTFLETFLA PTKLYVKPIL ELKKHIDIKA
     MSHITGGGFY ENIPRALPKG LSAKIDTQSF PTLEVFNWLQ KQGNISTNEM YNIFNMGIGY
     TIIVDKKDVQ TTLTTLRAMD TTAYEIGEII KDDDTPIHLL EVE
//