ID   GCH4_NITMU              Reviewed;         263 AA.
AC   Q2YCH6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=Nmul_A0237;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB73545.1; -; Genomic_DNA.
DR   RefSeq; WP_011379599.1; NZ_FNVK01000010.1.
DR   AlphaFoldDB; Q2YCH6; -.
DR   SMR; Q2YCH6; -.
DR   STRING; 323848.Nmul_A0237; -.
DR   KEGG; nmu:Nmul_A0237; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_4; -.
DR   OrthoDB; 9774824at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002718; 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   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..263
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289502"
FT   SITE            149
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   263 AA;  29773 MW;  D696D2689AEA7A8C CRC64;
     MNKMLIADVQ SVADTRRIAI DKAGIRAIRH PVRIMDKAGV QHTVAVFNMY VNLAHHLKGV
     HMSRFVEMLN EHDSVISVET FEKLLISMVK KLEAESGDIE MRFPYFIGKT APVSGIKSLM
     DYDVTFIGQT RNGESRFTLK VVVPVTSLCP CSKEVSDDGA HNQRSHISIS IRANHFVWIE
     DLIRIAEDQA SCELYGLLKR SDEKYVTEKA YGNPKFVEDA VRDIASVLDR DERIDAYTVE
     AENFESIHNH SAYALIECDK LKN
//