ID   GCH4_ROSDO              Reviewed;         367 AA.
AC   Q168P4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 78.
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=RD1_1941;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG31549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000362; ABG31549.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044033044.1; NZ_FOOO01000003.1.
DR   AlphaFoldDB; Q168P4; -.
DR   SMR; Q168P4; -.
DR   STRING; 375451.RD1_1941; -.
DR   PRIDE; Q168P4; -.
DR   EnsemblBacteria; ABG31549; ABG31549; RD1_1941.
DR   KEGG; rde:RD1_1941; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_1_5; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000007029; 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_0000289519"
FT   SITE            225
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   367 AA;  41167 MW;  7D3964D00E10495F CRC64;
     MNIHTPGLEL TPDRDEAQAA LDVLRQWAKQ ATPAEISELD PSVARLVPGM DGVEYPALSR
     EYPSDFSLDD GYKETLPDLQ NGPSSLIRGT KQQIQHVGIS NFRLPIRFHT RSGGDITLET
     SVTGSVSLEA DKKGINMSRI MRSFYKHAEE TFSFEVIEAA LDAYINDLES FDARIQMRFS
     FPMKVDSLRS GLSGYQYYDI ALELVDQGGV RKKIMHLDYV YSSTCPCSLE LSEHARATRG
     QLATPHSQRS VARISVEVEN DGQCLWFEDL IEACRRAVPT ETQVMVKRED EQAFAELNAA
     NPIFVEDAAR LFCEQLHSDT RIGDFRVIAS HQESLHSHDA VSVLMEGETF KSESLDPKLF
     NTLFHVG