ID   GCH4_DESVV              Reviewed;         264 AA.
AC   A1VAN0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 69.
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=Dvul_0473;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM27496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000527; ABM27496.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043629168.1; NC_008751.1.
DR   AlphaFoldDB; A1VAN0; -.
DR   SMR; A1VAN0; -.
DR   EnsemblBacteria; ABM27496; ABM27496; Dvul_0473.
DR   KEGG; dvl:Dvul_0473; -.
DR   HOGENOM; CLU_062816_1_1_7; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000009173; 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.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..264
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000289490"
FT   SITE            145
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   264 AA;  29864 MW;  5AC9408C0CA5E113 CRC64;
     MEDVQNSPAQ VAMPIDRVGV KNLQLPLVVS DRAQGRQHTV ATVDIGVDLP AHFKGTHMSR
     FVEALENWTE ELDYASMKRL LEDVKTRLEA RKAYVLFRFP YFIRKKAPAT GSPGLVCYQC
     RLTGELEEGR PSFLLEVEVP VMTVCPCSKA ISDEGAHSQR AVVRIAVRMT RFSWLEEFID
     LAEVSGSSPV YTLLKREDEK FVTEDAFAHP TFVEDVVRAA AQRLERHPQI SWFRVEVESF
     ESIHCHNAFA SIERTITPET QPGS