ID   PURO_HALMA              Reviewed;         202 AA.
AC   Q5UZ65;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=rrnAC2659;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47438.1; -; Genomic_DNA.
DR   RefSeq; WP_004959818.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UZ65; -.
DR   SMR; Q5UZ65; -.
DR   STRING; 272569.rrnAC2659; -.
DR   EnsemblBacteria; AAV47438; AAV47438; rrnAC2659.
DR   GeneID; 40153534; -.
DR   GeneID; 64824067; -.
DR   KEGG; hma:rrnAC2659; -.
DR   PATRIC; fig|272569.17.peg.3253; -.
DR   eggNOG; arCOG04727; Archaea.
DR   HOGENOM; CLU_1352116_0_0_2; -.
DR   OMA; HVDPIAE; -.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000001169; Chromosome I.
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_0000349157"
FT   REGION          29..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   202 AA;  21452 MW;  5394B45893E70A52 CRC64;
     MYVGRFVVVS PEVGAYRVSS RSFPNRQAVQ RDGTVTVEPT PDAPETDNPY ISYNGVRVTE
     RGAVVGNGSH VDPIAEKLEL GYPARDAIAE PLLSLDFEKD DYDTPRVAGI VGVDAADPTT
     NADGPGAVIG TVRRDALLVE EVTEPTLVAT YEENSPTAFD LAATDASDVA REVYDHEYEH
     AVCSAGVAGS AGEFDVAVYN GE