ID   PUR5_ACIAD              Reviewed;         356 AA.
AC   Q6F973;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=ACIAD2634;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69392.1; -; Genomic_DNA.
DR   RefSeq; WP_004928857.1; NC_005966.1.
DR   AlphaFoldDB; Q6F973; -.
DR   SMR; Q6F973; -.
DR   STRING; 62977.ACIAD2634; -.
DR   EnsemblBacteria; CAG69392; CAG69392; ACIAD2634.
DR   GeneID; 45234913; -.
DR   KEGG; aci:ACIAD2634; -.
DR   eggNOG; COG0150; Bacteria.
DR   HOGENOM; CLU_047116_0_0_6; -.
DR   OMA; EPLFMTD; -.
DR   OrthoDB; 923547at2; -.
DR   BioCyc; ASP62977:ACIAD_RS11980-MON; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000000430; 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..356
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000258324"
SQ   SEQUENCE   356 AA;  37697 MW;  F4309330D84DD540 CRC64;
     MSNSTSTPNT GLSYKDAGVD IEAGDALVDR IKSVAKRTTR PEVMGGLGGF GALCKIPKGY
     EEPVLVSGTD GVGTKLRLAL NLNRHDTIGQ DLVAMCVNDL LVCGAEPLFF LDYYATGHLN
     VDVAANVVTG IGKGCELAGC ALVGGETAEM PGMYEGEDYD LAGFAVGVVE QSKIIDGSKV
     KAGDVLIGVA SSGAHSNGYS LLRKILDVKN VDLTQEIDGR SLADAAMEPT RIYVKPVLEL
     CKQVDVHAMA HITGGGLPGN LPRVLPNGAQ AVIDEASWEW PELFKLLQRE GGVEQFEMYR
     TFNCGVGMVI AVDAADADKT IQVLNAQGEK SWKIGHIQDN AESIEGADEK IRVIFA