ID PURO_THEKO Reviewed; 198 AA. AC Q5JD29; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 29-OCT-2014, entry version 62. 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=TK0430; OS Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OS (Pyrococcus kodakaraensis (strain KOD1)). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=69014; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1; RX PubMed=15710748; DOI=10.1101/gr.3003105; RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; RT "Complete genome sequence of the hyperthermophilic archaeon RT Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus RT genomes."; RL Genome Res. 15:352-363(2005). CC -!- FUNCTION: Catalyzes the cyclization of 5-formylamidoimidazole-4- CC carboxamide ribonucleotide to IMP. {ECO:0000255|HAMAP- CC Rule:MF_00705}. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. {ECO:0000255|HAMAP- CC Rule:MF_00705}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00705}. CC -!- SIMILARITY: Belongs to the archaeal IMP cyclohydrolase family. CC {ECO:0000255|HAMAP-Rule:MF_00705}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006878; BAD84619.1; -; Genomic_DNA. DR RefSeq; YP_182843.1; NC_006624.1. DR ProteinModelPortal; Q5JD29; -. DR STRING; 69014.TK0430; -. DR EnsemblBacteria; BAD84619; BAD84619; TK0430. DR GeneID; 3235123; -. DR KEGG; tko:TK0430; -. DR eggNOG; COG3363; -. DR HOGENOM; HOG000015497; -. DR InParanoid; Q5JD29; -. DR KO; K11176; -. DR OMA; YIGRFLV; -. DR BioCyc; TKOD69014:GH72-438-MONOMER; -. DR UniPathway; UPA00074; UER00135. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. 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 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 Complete proteome; Hydrolase; Purine biosynthesis; Reference proteome. FT CHAIN 1 198 IMP cyclohydrolase. FT /FTId=PRO_0000349170. SQ SEQUENCE 198 AA; 22625 MW; BC2E7E7E0D8FAE6F CRC64; MRYVGRTLGI GLNNGKPFAF YLLCSRSFPN RRAVVKGNGV YILNQTETEN PYVSYPVVRL MEDYAVVTNG LHTDFIAQAL EWERPRKALV HVLDALDYER DDYSTPRIAG IIQHGGRRGW LGFVGRDMLW MRELELEEGK AFLTATYNME GFESIELAFS TPEELAEKVM ELPFEHKVLA IGIVENEKGW ELSFTPSL //