ID   PUR5_BACSU              Reviewed;         346 AA.
AC   P12043;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 143.
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; Synonyms=ath; OrderedLocusNames=BSU06500;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036807; DOI=10.1016/s0021-9258(18)47560-6;
RA   Ebbole D.J., Zalkin H.;
RT   "Cloning and characterization of a 12-gene cluster from Bacillus subtilis
RT   encoding nine enzymes for de novo purine nucleotide synthesis.";
RL   J. Biol. Chem. 262:8274-8287(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 203-204; 219 AND 222.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(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   -!- 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; J02732; AAA22681.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12470.2; -; Genomic_DNA.
DR   PIR; H29326; AJBSCL.
DR   RefSeq; NP_388532.2; NC_000964.3.
DR   RefSeq; WP_003242485.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; P12043; -.
DR   SMR; P12043; -.
DR   STRING; 224308.BSU06500; -.
DR   PaxDb; 224308-BSU06500; -.
DR   EnsemblBacteria; CAB12470; CAB12470; BSU_06500.
DR   GeneID; 936044; -.
DR   KEGG; bsu:BSU06500; -.
DR   PATRIC; fig|224308.179.peg.706; -.
DR   eggNOG; COG0150; Bacteria.
DR   InParanoid; P12043; -.
DR   OrthoDB; 9802507at2; -.
DR   PhylomeDB; P12043; -.
DR   BioCyc; BSUB:BSU06500-MONOMER; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..346
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000148197"
FT   CONFLICT        203..204
FT                   /note="EL -> AW (in Ref. 1; AAA22681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="E -> Q (in Ref. 1; AAA22681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="L -> V (in Ref. 1; AAA22681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  37052 MW;  1A9524A69DFC3DA5 CRC64;
     MSEAYKNAGV DIEAGYEAVK RMKKHVERTK RLGVMGSLGG FGGMFDLSEL SYQKPVLISG
     TDGVGTKLKL AFSMDKHDTI GVDAVAMCVN DVLAQGAEPL FFLDYLAVGK ADPVKIEQIV
     QGVAEGCEQS GSALVGGETA EMPGLYTADE YDIAGFSVGV AEKDEIVTGE KIEEGHLLIG
     LSSSGLHSNG FSLVRKVLLD DAELDLDTTY EPFERPLGEE LLEPTRIYVK PVLAAVKSGK
     IDGMAHVTGG GFIENIPRML PEGLSAEIDH GSWPIPPIFS FLQEYGKLKE EDMFNVFNMG
     IGFVLAVKEE HLTDVIGTLE SHGEKAYLIG RVKKGEGVTF GGAALS
//