ID   GCH4_PSET1              Reviewed;         302 AA.
AC   Q3ILJ5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 90.
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=PSHAa0549;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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=CAI85637.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR954246; CAI85637.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q3ILJ5; -.
DR   SMR; Q3ILJ5; -.
DR   STRING; 326442.PSHAa0549; -.
DR   KEGG; pha:PSHAa0549; -.
DR   PATRIC; fig|326442.8.peg.518; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_6; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000006843; Chromosome I.
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..302
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289506"
FT   SITE            151
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   302 AA;  33539 MW;  FEDB0E3EC8D88873 CRC64;
     MPDIANTAPA LQTGTLDWVG MGEIELPFIF ESHGITPVTV NAKARAFVNL HKEDAKGIHM
     SRLFLALDTL STEQQVNPQT LAQALDFFIS SHEGLSDKAL IEFKFELPLR RKSLLSDKAG
     WKSYPVILTS TIEQGVINYE LSVDVTYSST CPCSAALARQ LIQNAFAEKF SQETLSQKEA
     LEWLGTTQGI VATPHSQRSI ANVKVKLDSN ITQFDVVNLI NTIEDELKTP VQAAVKREDE
     QEFARLNGQN LMFCEDAARK IKALLETQQY SDYWLQINHY ESLHAHDALA IAVKGVAGGY
     RA
//