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GCH1_VIBCH
ID   GCH1_VIBCH              Reviewed;         217 AA.
AC   Q9KLX5;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000255|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000255|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000255|HAMAP-Rule:MF_00223}; OrderedLocusNames=VC_A0616;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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_00223};
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_00223}.
CC   -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC       dimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000255|HAMAP-Rule:MF_00223}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF96517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003853; AAF96517.1; ALT_INIT; Genomic_DNA.
DR   PIR; D82439; D82439.
DR   RefSeq; NP_233005.1; NC_002506.1.
DR   RefSeq; WP_000016195.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KLX5; -.
DR   SMR; Q9KLX5; -.
DR   STRING; 243277.VC_A0616; -.
DR   DNASU; 2612591; -.
DR   EnsemblBacteria; AAF96517; AAF96517; VC_A0616.
DR   GeneID; 57742013; -.
DR   GeneID; 66940156; -.
DR   KEGG; vch:VC_A0616; -.
DR   PATRIC; fig|243277.26.peg.3244; -.
DR   eggNOG; COG0302; Bacteria.
DR   HOGENOM; CLU_049768_3_2_6; -.
DR   OMA; CEHMCMS; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.286.10; -; 1.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   HAMAP; MF_00223; FolE; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR043134; GTP-CH-I_N.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   PANTHER; PTHR11109; PTHR11109; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Reference proteome; Zinc.
FT   CHAIN           1..217
FT                   /note="GTP cyclohydrolase 1"
FT                   /id="PRO_0000119460"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
SQ   SEQUENCE   217 AA;  24143 MW;  D5D3E776BD633213 CRC64;
     MSGLSESAKL VKDALERRGL ETPMQPNLAT PAEKKEKIEQ HMREILNLLG LDLTDDSLEE
     TPQRIAKMYV DEIFSGLDYA NFPKITVIEN KMKVSEMVKV KDITLTSTCE HHLVTIDGTA
     AVAYIPRGKI IGLSKINRIV RFFAQRPQVQ ERMTQQILVA LQTLLESDDV AVTIDATHYC
     VKSRGVMDAT SVTTTTALGG IFKSNPATRA EFLHGLR
 
 
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