ID GCH1_CHRVO Reviewed; 206 AA. AC Q7NYZ2; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=GTP cyclohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00223}; DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223}; DE AltName: Full=GTP cyclohydrolase I {ECO:0000255|HAMAP-Rule:MF_00223}; DE Short=GTP-CH-I {ECO:0000255|HAMAP-Rule:MF_00223}; GN Name=folE {ECO:0000255|HAMAP-Rule:MF_00223}; GN OrderedLocusNames=CV_1130; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC OS 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00223}; CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00223}. CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five CC dimers. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. CC {ECO:0000255|HAMAP-Rule:MF_00223}. 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; AE016825; AAQ58805.1; -; Genomic_DNA. DR RefSeq; WP_011134685.1; NC_005085.1. DR AlphaFoldDB; Q7NYZ2; -. DR SMR; Q7NYZ2; -. DR STRING; 243365.CV_1130; -. DR GeneID; 66366831; -. DR KEGG; cvi:CV_1130; -. DR eggNOG; COG0302; Bacteria. DR HOGENOM; CLU_049768_3_3_4; -. DR OrthoDB; 9801207at2; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000001424; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1130.10; -; 1. DR HAMAP; MF_00223; FolE; 1. DR InterPro; IPR043133; GTP-CH-I_C/QueF. DR InterPro; IPR001474; GTP_CycHdrlase_I. DR InterPro; IPR018234; GTP_CycHdrlase_I_CS. DR InterPro; IPR020602; GTP_CycHdrlase_I_dom. DR PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1. DR PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1. DR Pfam; PF01227; GTP_cyclohydroI; 1. DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1. DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1. PE 3: Inferred from homology; KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding; KW One-carbon metabolism; Reference proteome; Zinc. FT CHAIN 1..206 FT /note="GTP cyclohydrolase 1" FT /id="PRO_0000119397" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223" FT BINDING 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223" SQ SEQUENCE 206 AA; 23162 MW; 800443D34D495DBD CRC64; MSFTDDHDHA ACQRPLERVR PFDAAAFERA VADMLTASGI AIDPIHTGKT AQRVRELWQK RLLDGYDTVP AEALGSGFAD ERRDMVVIRS LAVHGMCPHH LLPFRGVAHV AYLPGGRLHG FGRIARMVDA ISHRYTYQEW ITHEIARTLV EHGEARGAAC LIEAEQLCLL MGENRRGDER VITQCYAGDF ETDAEARNQF LRAIER //