ID   PUR5_RHILO              Reviewed;         369 AA.
AC   Q984K6;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=mll7962;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB53624.1; -; Genomic_DNA.
DR   RefSeq; WP_010915250.1; NC_002678.2.
DR   AlphaFoldDB; Q984K6; -.
DR   SMR; Q984K6; -.
DR   STRING; 266835.14027355; -.
DR   EnsemblBacteria; BAB53624; BAB53624; BAB53624.
DR   GeneID; 66684871; -.
DR   KEGG; mlo:mll7962; -.
DR   eggNOG; COG0150; Bacteria.
DR   HOGENOM; CLU_047116_0_0_5; -.
DR   OMA; EPLFMTD; -.
DR   OrthoDB; 923547at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000000552; 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.
FT   CHAIN           1..369
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000148238"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  38418 MW;  2DC3BA404506C81D CRC64;
     MSKRDTSQPK TGQPKTSKRR NGLTYAEAGV DIDAGNLMVE KIKPLVRATR RPGADGEIGG
     FGGLFDLKAA GFTDPVLVAA NDGVGTKLKI AIDAGKHDTI GIDLVAMCVN DIVVQGAEPL
     FFLDYFATGK LDPDQGAAIV GGIAEGCRQA GCALIGGETA EMPGMYHGND YDLAGFAVGA
     AERGQLLPTD DIVEGDVLLG LASSGLHSNG FSLVRRIVAA SGLAWSDPAP FNDEATLAEA
     LLEPTRIYVK SILKAIRNTH GIKALAHITG GGFPENIPRV LPKDFSAELD LEAIDVPPVF
     SWLAKTGGVA PEEMMRTFNC GVGMILAVAS GQAAQVAAVL QEAGETVTPI GRIVPRRDAG
     VIYRGSIGL