ID   PUR5_LEPIN              Reviewed;         344 AA.
AC   Q8F242;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 111.
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};
GN   OrderedLocusNames=LA_2935;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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=AAN50133.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE010300; AAN50133.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_713115.2; NC_004342.2.
DR   AlphaFoldDB; Q8F242; -.
DR   SMR; Q8F242; -.
DR   STRING; 189518.LA_2935; -.
DR   PaxDb; 189518-LA_2935; -.
DR   EnsemblBacteria; AAN50133; AAN50133; LA_2935.
DR   KEGG; lil:LA_2935; -.
DR   PATRIC; fig|189518.3.peg.2914; -.
DR   HOGENOM; CLU_047116_0_0_12; -.
DR   InParanoid; Q8F242; -.
DR   OrthoDB; 9802507at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001408; Chromosome I.
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..344
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_0000148220"
SQ   SEQUENCE   344 AA;  37761 MW;  266AF4D7F5C837EE CRC64;
     MEEKITYKNA GVDTEKGREF IQKIKRNVES THGPRVIGGL GGFAGAYDVS VLKKYKHPIL
     LSGTDGVGTK IELARLLKIY NTIGIDLVAM CVNDILVCGG EPLFFLDYIA CGKLDPEKMD
     QIVSGIVQGC KMSNASLLGG ETAEHPGTMK EDEFDLAGFV VGAVEKDSMI DGSTIRSGDK
     ILGLESSGPH SNGFSLIRKL LLKEGKYLPT DPQQVKFLKD YALKPTRIYV SSILKLLQQV
     SVKGMVHITG GGYQENVPRI LPQGTQSKFF KEKIPSGYFF EKIKKDHKIE ELELFATFNM
     GIGYMVIVSE ENAELAKKIM ESSGEVVHEI GEIVSGNKEE VQFV
//