ID   PURO_HALWD              Reviewed;         195 AA.
AC   Q18DI6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=HQ_1006A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(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; AM180088; CAJ51136.1; -; Genomic_DNA.
DR   RefSeq; WP_011570303.1; NC_008212.1.
DR   AlphaFoldDB; Q18DI6; -.
DR   SMR; Q18DI6; -.
DR   STRING; 362976.HQ_1006A; -.
DR   EnsemblBacteria; CAJ51136; CAJ51136; HQ_1006A.
DR   GeneID; 4194534; -.
DR   KEGG; hwa:HQ_1006A; -.
DR   eggNOG; arCOG04727; Archaea.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   OMA; HVDPIAE; -.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000001975; 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..195
FT                   /note="IMP cyclohydrolase"
FT                   /id="PRO_0000349159"
SQ   SEQUENCE   195 AA;  21320 MW;  8DA09F3562DC1FE8 CRC64;
     MYLGRFIIIG ETTAVYRVSS RSYPNRQIIS RDNMLTVVPT SEAAQTNNPY VSYNCMRQGG
     EKIVIGNGSH VDPIAEKIDR GYPARDALAE ALLALDYEKD DYNTPRIAGI VGSSSYVGII
     RQDAVIIRSI SEPTLVSTYE NDAPTTAQLS LKGDIEEIAQ KAYELEYEHP VCAAAVTHQG
     QGESGDIVAQ IYNGK