ID   GCH4_PSYIN              Reviewed;         304 AA.
AC   A1STF0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   18-JUN-2025, entry version 86.
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=Ping_0923;
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17664 / CCUG 51855 / 37;
RX   PubMed=18460197; DOI=10.1186/1471-2164-9-210;
RA   Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J.,
RA   Land M.L., Thompson L.S.;
RT   "Genomics of an extreme psychrophile, Psychromonas ingrahamii.";
RL   BMC Genomics 9:210-210(2008).
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=ABM02765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000510; ABM02765.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011769328.1; NC_008709.1.
DR   AlphaFoldDB; A1STF0; -.
DR   SMR; A1STF0; -.
DR   STRING; 357804.Ping_0923; -.
DR   KEGG; pin:Ping_0923; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_0_0_6; -.
DR   OrthoDB; 239637at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000639; Chromosome.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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   NCBIfam; NF010200; PRK13674.1-1; 1.
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..304
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289513"
FT   SITE            151
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   304 AA;  34214 MW;  7BEC562D962AA553 CRC64;
     MPDIANSAQA QTEGKLDRVG MSNIELPLMV QTDDCPPQQV SANAEVFVNL GDAQAKGIHM
     SRLYLQLDEL STESELNIST LTALLQGFIT SHHELSQRAF VKFSFDYHLR RKSLISEKRG
     WKAYPVIIIG RLSEGNFEVE LQVNVPYSST CPCSAALARQ LIQQAFSQKY DQQTEVNKEE
     IFAWLGSTKG IVATPHSQRS IVEVKVKLNS LNQSFPIIEL IDLIEKTLKT PVQAAVKRED
     EQEFALLNGQ NLMFCEDAAR HLQHSLHQET KFDDFWLRVN HYESLHAHDA VAMTTKGIEG
     GYLA
//