GCH1_VIBC1
ID GCH1_VIBC1 Reviewed; 217 AA.
AC A7N6L2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=VIBHAR_06235;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000790; ABU74127.1; -; Genomic_DNA.
DR RefSeq; WP_005373478.1; NC_022270.1.
DR AlphaFoldDB; A7N6L2; -.
DR SMR; A7N6L2; -.
DR EnsemblBacteria; ABU74127; ABU74127; VIBHAR_06235.
DR GeneID; 67379993; -.
DR KEGG; vha:VIBHAR_06235; -.
DR PATRIC; fig|338187.25.peg.4103; -.
DR OMA; CEHMCMS; -.
DR OrthoDB; 1632367at2; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000008152; Chromosome II.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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: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; Zinc.
FT CHAIN 1..217
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_1000043757"
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; 24394 MW; 557CF99B0744EF69 CRC64;
MSGLSESAKL VKEALEQRGL ETPMRPNNVS REEKKEKIEH HMREILGLLQ LDLTDDSLEE
TPHRIAKMYV DEIFSGLDYS NFPKITVIEN KMNVSEMVRV KDITVTSTCE HHLVTIDGKA
AVAYIPRGKI IGLSKINRIV RFFAQRPQVQ ERMTQQILVA LQTLLESDDV AVTIDATHYC
VKSRGVMDAT SETTTTALGG IFKSNPATRA EFLHGLR
