ID   PUR5_LACDA              Reviewed;         349 AA.
AC   Q1G9G0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Ldb1438;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC   11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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; CR954253; CAI98239.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1G9G0; -.
DR   SMR; Q1G9G0; -.
DR   STRING; 390333.Ldb1438; -.
DR   EnsemblBacteria; CAI98239; CAI98239; Ldb1438.
DR   KEGG; ldb:Ldb1438; -.
DR   PATRIC; fig|390333.13.peg.1930; -.
DR   eggNOG; COG0150; Bacteria.
DR   HOGENOM; CLU_047116_0_0_9; -.
DR   OMA; EPLFMTD; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001259; 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;
KW   Reference proteome.
FT   CHAIN           1..349
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000258364"
SQ   SEQUENCE   349 AA;  37160 MW;  22BF4BC11C100EBA CRC64;
     MIVNRYKDAG VDVNAGYELV RRIKGAVAST KRPGYVGNIG GFGGLFDLDS LGYDHPVLVS
     GTDGVGTKLI IAQKMDKNDT VGIDVVAMCV NDVLAQGAEP LFFLDYIACG HNDPALLASV
     VQGVAEGCKQ AGASLIGGET AEMPDMYAPD EYDLAGFTVG VAEKDRLLSV DTPQAGDVLL
     GLASSGVHSN GFSLVRKILF KDHDVKLTDK PAELKGKSVG ESLLAPTRIY IKSVLPLIKQ
     GLVHGVAHIT GGGLIENVPR MFNDGLRAEI AAGSWEVPDI FNYLKQVGNL SDDDCWQTFN
     MGLGMILAVP ADKKEEAKKL LLASGEKVFE VGHLSERTDG EKIFIKLVE