ID   PURO_METTH              Reviewed;         202 AA.
AC   O27099;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
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=MTH_1020;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85516.1; -; Genomic_DNA.
DR   PIR; B69003; B69003.
DR   RefSeq; WP_010876651.1; NC_000916.1.
DR   PDB; 1KUU; X-ray; 2.20 A; A=1-202.
DR   PDB; 2NTK; X-ray; 2.03 A; A/B/C/D=1-202.
DR   PDB; 2NTL; X-ray; 2.60 A; A/B/C/D=1-202.
DR   PDB; 2NTM; X-ray; 2.60 A; A/B/C/D=1-202.
DR   PDBsum; 1KUU; -.
DR   PDBsum; 2NTK; -.
DR   PDBsum; 2NTL; -.
DR   PDBsum; 2NTM; -.
DR   AlphaFoldDB; O27099; -.
DR   SMR; O27099; -.
DR   STRING; 187420.MTH_1020; -.
DR   EnsemblBacteria; AAB85516; AAB85516; MTH_1020.
DR   GeneID; 1471428; -.
DR   KEGG; mth:MTH_1020; -.
DR   PATRIC; fig|187420.15.peg.1003; -.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   OMA; HVDPIAE; -.
DR   UniPathway; UPA00074; UER00135.
DR   EvolutionaryTrace; O27099; -.
DR   Proteomes; UP000005223; 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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..202
FT                   /note="IMP cyclohydrolase"
FT                   /id="PRO_0000145797"
FT   STRAND          5..12
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          15..23
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   HELIX           48..52
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          57..65
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   HELIX           76..85
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   HELIX           90..101
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          122..128
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   HELIX           163..172
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   HELIX           174..178
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          182..193
FT                   /evidence="ECO:0007829|PDB:2NTK"
FT   STRAND          195..201
FT                   /evidence="ECO:0007829|PDB:2NTK"
SQ   SEQUENCE   202 AA;  21839 MW;  CCAA360D1468BD1A CRC64;
     MYLGRILAVG RNSNGSFVAY RVSSRSFPNR TTSIQEERVA VVPVEGHERD VFRNPYIAYN
     CIRIVGDTAV VSNGSHTDTI ADKVALGMNL RDAIGLSLLA MDYEKDELNT PRIAAAINGS
     EAFIGIVTAD GLMVSRVPEE TPVYISTYEQ TEPAATEFKA GSPEEAAEFI LKGGEFAAFT
     HPVTAAAAFN DGEGWNLATR EM