ID   PURO_NATPD              Reviewed;         191 AA.
AC   Q3ITS6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=NP_0732A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48457.1; -; Genomic_DNA.
DR   RefSeq; WP_011322093.1; NC_007426.1.
DR   AlphaFoldDB; Q3ITS6; -.
DR   SMR; Q3ITS6; -.
DR   STRING; 348780.NP_0732A; -.
DR   EnsemblBacteria; CAI48457; CAI48457; NP_0732A.
DR   GeneID; 3703076; -.
DR   KEGG; nph:NP_0732A; -.
DR   eggNOG; arCOG04727; Archaea.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   OMA; HVDPIAE; -.
DR   OrthoDB; 106750at2157; -.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000002698; 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..191
FT                   /note="IMP cyclohydrolase"
FT                   /id="PRO_0000349169"
SQ   SEQUENCE   191 AA;  20776 MW;  4A64B740BE9897C2 CRC64;
     MYVGRFIVVA PDRAAYRVSS RSFPNRRIVD RDGTLTVGPT EDAPETDNPY ISYNCLRTVG
     DDYAVVGNGT QVDPIAEKLS LGYPPRDALA ESLLALDYEK DDYDTPRIAG VVGDESYIGT
     VRRDALIVEA VEEPTLVATY EKSEPEPTSL GADDPSELAA ELYDRDLEHP VCAAGVVADG
     DSFEVGYYNG E