ID   GCH4_CHRSD              Reviewed;         304 AA.
AC   Q1R153;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 97.
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}; OrderedLocusNames=Csal_0191;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE57555.1; -; Genomic_DNA.
DR   RefSeq; WP_011505501.1; NC_007963.1.
DR   AlphaFoldDB; Q1R153; -.
DR   SMR; Q1R153; -.
DR   STRING; 290398.Csal_0191; -.
DR   EnsemblBacteria; ABE57555; ABE57555; Csal_0191.
DR   KEGG; csa:Csal_0191; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_6; -.
DR   OMA; AKGIHMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000239; 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..304
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289485"
FT   SITE            153
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   304 AA;  32972 MW;  39011AF05A0127BC CRC64;
     MQEPKNSQTL HDVANGASDL EGPLAWVGME DIALPFRLAN SAVNGRASAG VSLDATSARG
     IHMSRLYLAL EALEHEEVTL SGLGAVLQRF LASHDGLART AFLDLSGDVL IKRPALISPR
     AGWKAYPCAL RCRQDTQGMQ AVLEVTIGYS STCPCSAALA RQSIQQAFDE DFTDMPISHE
     AVRTWLGSEQ GILATPHSQR SQAHLSLRLA DDLETLPVTA LIDTVEDALG TALQTAVKRV
     DEQAFALANG QNLMFCEDAA RRVRHALQAR DEVQGFRVRI VHAESLHAHD AVAHAEWNWT
     PNSP