GCH1_LISMO
ID GCH1_LISMO Reviewed; 189 AA.
AC Q8Y5X1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=lmo1933;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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; AL591981; CAD00011.1; -; Genomic_DNA.
DR PIR; AE1316; AE1316.
DR RefSeq; NP_465457.1; NC_003210.1.
DR RefSeq; WP_003724029.1; NZ_CP023861.1.
DR PDB; 4UQF; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=2-189.
DR PDBsum; 4UQF; -.
DR AlphaFoldDB; Q8Y5X1; -.
DR SMR; Q8Y5X1; -.
DR STRING; 169963.lmo1933; -.
DR PaxDb; Q8Y5X1; -.
DR EnsemblBacteria; CAD00011; CAD00011; CAD00011.
DR GeneID; 987987; -.
DR KEGG; lmo:lmo1933; -.
DR PATRIC; fig|169963.11.peg.1979; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_3_9; -.
DR OMA; CEHMCMS; -.
DR PhylomeDB; Q8Y5X1; -.
DR BioCyc; LMON169963:LMO1933-MON; -.
DR BRENDA; 3.5.4.16; 15002.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000817; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome; Zinc.
FT CHAIN 1..189
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119421"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00223"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:4UQF"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:4UQF"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:4UQF"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4UQF"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:4UQF"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:4UQF"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:4UQF"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4UQF"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:4UQF"
SQ SEQUENCE 189 AA; 21321 MW; A28B2E0133A5459F CRC64;
MEQIDKQKIA DAVKVILEAV GENPDREGLI DTPMRVARMY EEVFAGLKKD PSVHFDTIFE
EQHEELVLVK DIRFSSMCEH HLVPFFGVAH VAYLPQNGRV AGLSKLARVV DDVSRRPQLQ
ERITTTVAEI MMEKLKPLGV MVIMEAEHMC MTIRGVNKPG TKTITSAVRG AFKNDDKLRS
EVLALIKHN
