ID   PURO_METST              Reviewed;         202 AA.
AC   Q2NEI3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00705};
DE            EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00705};
DE   AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00705};
DE   AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00705};
GN   Name=purO {ECO:0000255|HAMAP-Rule:MF_00705}; OrderedLocusNames=Msp_1398;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Catalyzes the cyclization of 5-formylamidoimidazole-4-
CC       carboxamide ribonucleotide to IMP. {ECO:0000255|HAMAP-Rule:MF_00705}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00705};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC       from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00705}.
CC   -!- SIMILARITY: Belongs to the archaeal IMP cyclohydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00705}.
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DR   EMBL; CP000102; ABC57770.1; -; Genomic_DNA.
DR   RefSeq; WP_011406969.1; NC_007681.1.
DR   AlphaFoldDB; Q2NEI3; -.
DR   SMR; Q2NEI3; -.
DR   STRING; 339860.Msp_1398; -.
DR   EnsemblBacteria; ABC57770; ABC57770; Msp_1398.
DR   GeneID; 41325970; -.
DR   KEGG; mst:Msp_1398; -.
DR   eggNOG; arCOG04727; Archaea.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   OMA; HVDPIAE; -.
DR   OrthoDB; 106750at2157; -.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.20.20; -; 1.
DR   HAMAP; MF_00705; IMP_cyclohydrol; 1.
DR   InterPro; IPR010191; IMP_cyclohydrolase.
DR   InterPro; IPR020600; IMP_cyclohydrolase-like.
DR   InterPro; IPR036795; IMP_cyclohydrolase-like_sf.
DR   Pfam; PF07826; IMP_cyclohyd; 1.
DR   PIRSF; PIRSF004866; IMP_cclhdr_arch; 1.
DR   SUPFAM; SSF75569; SSF75569; 1.
DR   TIGRFAMs; TIGR01922; purO_arch; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..202
FT                   /note="IMP cyclohydrolase"
FT                   /id="PRO_0000349168"
SQ   SEQUENCE   202 AA;  22479 MW;  B42D65EB025715F7 CRC64;
     MYLGRIISIG SSKDGVYASY RVSSRSFPNR KSVVNNQKVA IIPTQGSEDD IYKNPYISYN
     CIDIIDDICV VTNGSHTDII AGKIREGMNM KDAVALSLLT MDYEKDDYNT PRIGGAINTK
     GEGYIGIVTH EGIEVKKVNP GESFYVSTYE HNTPREVDYT ATNAKEATEF IFNGGIFSEF
     THPVTSCAAF NKDEWEIDFK NP