ID   PURO_METM7              Reviewed;         201 AA.
AC   A6VGP7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=MmarC7_0555;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65623.1; -; Genomic_DNA.
DR   RefSeq; WP_011976954.1; NC_009637.1.
DR   AlphaFoldDB; A6VGP7; -.
DR   SMR; A6VGP7; -.
DR   STRING; 426368.MmarC7_0555; -.
DR   EnsemblBacteria; ABR65623; ABR65623; MmarC7_0555.
DR   GeneID; 5328627; -.
DR   KEGG; mmz:MmarC7_0555; -.
DR   eggNOG; arCOG04727; Archaea.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   OMA; HVDPIAE; -.
DR   OrthoDB; 106750at2157; -.
DR   UniPathway; UPA00074; UER00135.
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.
FT   CHAIN           1..201
FT                   /note="IMP cyclohydrolase"
FT                   /id="PRO_0000349165"
SQ   SEQUENCE   201 AA;  22552 MW;  7BBADDAA8D6A51D2 CRC64;
     MYIGRFLVLG KTDEGNPFVT YRVSSRSFPN RVAKVMDDNT VAILPKDLEE MFKNPYITYN
     CVKLVGDVAI ATNGSHTDII ADKIKLGLPI RDALSYSLLT MDYEKDDYNT PRIAVVLTKD
     SAYMGYVSEN DVRIKKVELE SGKAYYLSVY EACNITKHQV ISVAGKTAEE VTKFVMDYEE
     FEKPVTAATV LLKDGFKLAT L