ID   PUR5_NITMU              Reviewed;         352 AA.
AC   Q2Y5R7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 87.
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=Nmul_A2617;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB75904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000103; ABB75904.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041352649.1; NZ_FNVK01000020.1.
DR   AlphaFoldDB; Q2Y5R7; -.
DR   SMR; Q2Y5R7; -.
DR   STRING; 323848.Nmul_A2617; -.
DR   EnsemblBacteria; ABB75904; ABB75904; Nmul_A2617.
DR   KEGG; nmu:Nmul_A2617; -.
DR   eggNOG; COG0150; Bacteria.
DR   HOGENOM; CLU_047116_0_0_4; -.
DR   OrthoDB; 923547at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000002718; 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..352
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000258375"
SQ   SEQUENCE   352 AA;  37841 MW;  9DDA3FC809C4DAFB CRC64;
     MTTSKPHEEN LSPLSYRAAG VDIDAGERLV ENIRPYAKRT LRPEVLAGIG GFGALFEISR
     KFNNPVLVAG TDGVGTKLKL AFESGRHDTV GIDLVAMSVN DILVQGAEPL FFLDYFACGK
     LDVDTATLVV KGIAAGCEQA GCALIGGETA EMPGMYPEGE YDLAGFAVGA VEKDRIITGT
     TIKAGDAVLG LASSGAHSNG YSLIRKIIEK NNVDLSADFH GRALIDVIMA PTRIYVKPLL
     ELMRQVPVKG MAHITGGGLL ENIPRILPEG VTAVLKKETW EMPPLFAWLQ REGNVADNEM
     HRVFNCGIGM AVVVAPEYID AAAQLLQSKG EIAWRIGTIR EQRADEPRTI LE