ID   GCH4_NITEU              Reviewed;         268 AA.
AC   Q82VD1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=NE1163;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS).
RG   Midwest center for structural genomics (MCSG);
RT   "The crystal structure of duf198 from Nitrosomonas europaea ATCC 19718.";
RL   Submitted (SEP-2007) to the PDB data bank.
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; AL954747; CAD85074.1; -; Genomic_DNA.
DR   RefSeq; WP_011111754.1; NC_004757.1.
DR   PDB; 2R5R; X-ray; 3.05 A; A=1-268.
DR   PDBsum; 2R5R; -.
DR   AlphaFoldDB; Q82VD1; -.
DR   SMR; Q82VD1; -.
DR   STRING; 228410.NE1163; -.
DR   EnsemblBacteria; CAD85074; CAD85074; NE1163.
DR   KEGG; neu:NE1163; -.
DR   eggNOG; COG1469; Bacteria.
DR   HOGENOM; CLU_062816_1_1_4; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 757842at2; -.
DR   PhylomeDB; Q82VD1; -.
DR   UniPathway; UPA00848; UER00151.
DR   EvolutionaryTrace; Q82VD1; -.
DR   Proteomes; UP000001416; 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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..268
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147717"
FT   SITE            154
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
FT   STRAND          24..37
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          45..57
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           63..67
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           68..75
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           85..95
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          99..114
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          121..135
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          139..153
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           155..160
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          167..180
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           184..194
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           205..216
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   HELIX           222..234
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          239..249
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   TURN            251..253
FT                   /evidence="ECO:0007829|PDB:2R5R"
FT   STRAND          254..264
FT                   /evidence="ECO:0007829|PDB:2R5R"
SQ   SEQUENCE   268 AA;  30604 MW;  DAA9B16495ED23E4 CRC64;
     MNKQIDLPIA DVQGSLDTRH IAIDRVGIKA IRHPVVVADK GGGSQHTVAQ FNMYVNLPHN
     FKGTHMSRFV EILNSHEREI SVESFEEILR SMVSRLESDS GHIEMAFPYF INKSAPVSGV
     KSLLDYEVTF IGEIKHGNQY SFTMKVIVPV TSLCPCSKKI SDYGAHNQRS HVTISVRTNS
     FIWIEDIIRI AEEQASCELY GLLKRPDEKY VTERAYNNPK FVEDIVRDVA EVLNHDDRID
     AYIVESENFE SIHNHSAYAL IERDKRIR