GCH1_CLOAB
ID GCH1_CLOAB Reviewed; 195 AA.
AC Q97D54;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=CA_C3626;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81549.1; -; Genomic_DNA.
DR PIR; B97345; B97345.
DR RefSeq; NP_350209.1; NC_003030.1.
DR RefSeq; WP_010966889.1; NC_003030.1.
DR AlphaFoldDB; Q97D54; -.
DR SMR; Q97D54; -.
DR STRING; 272562.CA_C3626; -.
DR EnsemblBacteria; AAK81549; AAK81549; CA_C3626.
DR GeneID; 45000124; -.
DR KEGG; cac:CA_C3626; -.
DR PATRIC; fig|272562.8.peg.3816; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_2_9; -.
DR OMA; CEHMCMS; -.
DR OrthoDB; 1632367at2; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000814; Chromosome.
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.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome; Zinc.
FT CHAIN 1..195
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119398"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
SQ SEQUENCE 195 AA; 22108 MW; 75F0949E84FBC5E9 CRC64;
MSIDTKAIEK HIRGILIALG DDPDREGLKE TPKRVAKMYE EVFKGMEYSN DDIAEMFNKT
FEEDLKESEE DNIVLVKDIE IFSHCEHHLT LMYNMTVAVA YIPNKRLIGL SKIARIADMV
SRRLQLQERI GKDIAEIMEK VTASKDIAVI IKGEHGCMTS RGIKKPGALT TTMTLKGRFK
NDDSLVTKLM ALYKA
