ID   GCH4_RUEST              Reviewed;         367 AA.
AC   Q1GF96;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=TM1040_1937;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
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., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-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; CP000377; ABF64670.1; -; Genomic_DNA.
DR   RefSeq; WP_011539263.1; NC_008044.1.
DR   AlphaFoldDB; Q1GF96; -.
DR   SMR; Q1GF96; -.
DR   STRING; 292414.TM1040_1937; -.
DR   EnsemblBacteria; ABF64670; ABF64670; TM1040_1937.
DR   KEGG; sit:TM1040_1937; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_1_5; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000636; 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   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   PANTHER; PTHR36445; PTHR36445; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..367
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289521"
FT   SITE            225
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   367 AA;  41242 MW;  7A136D643A257BA2 CRC64;
     MNIHSRDVNE TPDRSDAEQA LAVLRRWAGE ASETEVAQLD PAIARLLPGQ ELQNYPDLKR
     QYPDDFDANE SYRATLPDLQ NGPSSLIRGA KEQIQHVGIS NFRLPIRFHT RDNGDLTLET
     SVTGTVSLDA EKKGINMSRI MRSFYKHAEK VFSFDVMEAA LEDYLSDLES GDARLQMRFS
     FPVKVQSLRS GLSGYQYYDV ALELVQMAGQ RHRIVHLDYV YSSTCPCSLE LSEHARQARG
     QLATPHSQRS VARISVQMEQ DGGCLWFEDL IDHCRRAVPT ETQVMVKRED EQAFAELNAA
     NPIFVEDAAR LFCEALQSDA RVGDFRVVAS HQESLHSHDA VSVLTQGTMF AAPSLDPQLF
     STLIHRG