ID   GCH4_MAGMM              Reviewed;         265 AA.
AC   A0L8I1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 65.
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=Mmc1_1766;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK44274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0L8I1; -.
DR   SMR; A0L8I1; -.
DR   STRING; 156889.Mmc1_1766; -.
DR   EnsemblBacteria; ABK44274; ABK44274; Mmc1_1766.
DR   KEGG; mgm:Mmc1_1766; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_5; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002586; 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.
DR   TIGRFAMs; TIGR00294; TIGR00294; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..265
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289496"
FT   SITE            152
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   265 AA;  30401 MW;  48CABA82215BCE11 CRC64;
     MNNCQLPLSD VQSRQDHRRL DIDKVGVKNI RYPIVVKDRS VGSQSTTARI NMYVNLPHQF
     KGTHMSRFLE VLAENQRAIS IENLPKLLKE VKQRLDAEEA HIELDFPYFI TKKAPVSGVE
     ALMDYQVHFS GVMRGNAYQL TLTVEVPVTS LCPCSKEISA YGAHNQRSHV KVSVQFSQFV
     WIEEVVDLVE RNASCELFTI LKRPDEKFVT EKAYDNPKFV EDMVRDLADE LTHDPRISWF
     AVESENFESI HNHSAYAFIE GGQRS