ID   GCH4_JANSC              Reviewed;         362 AA.
AC   Q28R88;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   OrderedLocusNames=Jann_1857;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
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_01527};
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_01527}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
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DR   EMBL; CP000264; ABD54774.1; -; Genomic_DNA.
DR   RefSeq; WP_011454979.1; NC_007802.1.
DR   AlphaFoldDB; Q28R88; -.
DR   SMR; Q28R88; -.
DR   STRING; 290400.Jann_1857; -.
DR   KEGG; jan:Jann_1857; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_1_5; -.
DR   OrthoDB; 239637at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000008326; Chromosome.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.270.10; Urate Oxidase; 1.
DR   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   PANTHER; PTHR36445; GTP CYCLOHYDROLASE MPTA; 1.
DR   PANTHER; PTHR36445:SF1; GTP CYCLOHYDROLASE MPTA; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..362
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289494"
FT   SITE            222
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   362 AA;  39886 MW;  E2F9E3878234C04E CRC64;
     MNVHVKTADQ TPSTVQAQDA LAILSAWASE ASADQIDALD PGIARLVRVQ AYPDLRAEYP
     GDFTVDEAYR ATLPDLQNGP ASLIKGANRR IQHVGISNFR LPIRYAVQDG SEVMLETSVT
     GTVSLEADQK GINMSRIMRS FYKHADASFG FDVIEAALDD YKADLGSFDA RIQMRLSYPM
     KVDSLRSGLS GWQYYDIALE LVERGGVRQR IVHLDYVYSS TCPCSLELSE HARATRGQLA
     TPHSQRSVAR ISVELQGQGV WFEDLIEMAR SGVPTETQVM VKREDEQAFA ELNAANPIFV
     EDAARLFAEQ LQAHSGVGDF RVMASHQESL HSHDAVSLLT EGDTFAEVSL DPKLFPSLIH
     VG
//