GCH1_YERPE
ID GCH1_YERPE Reviewed; 220 AA.
AC Q8ZG15; Q0WGR7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=YPO1505, y2664, YP_1395;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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=AAM86217.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS61636.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL20151.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86217.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS61636.1; ALT_INIT; Genomic_DNA.
DR PIR; AE0183; AE0183.
DR RefSeq; WP_002211960.1; NZ_WUCM01000063.1.
DR RefSeq; YP_002346521.1; NC_003143.1.
DR PDB; 4DU6; X-ray; 2.11 A; A/B/C/D/E=1-220.
DR PDBsum; 4DU6; -.
DR AlphaFoldDB; Q8ZG15; -.
DR SMR; Q8ZG15; -.
DR STRING; 214092.YPO1505; -.
DR PaxDb; Q8ZG15; -.
DR DNASU; 1147611; -.
DR EnsemblBacteria; AAM86217; AAM86217; y2664.
DR EnsemblBacteria; AAS61636; AAS61636; YP_1395.
DR GeneID; 66842047; -.
DR KEGG; ype:YPO1505; -.
DR KEGG; ypk:y2664; -.
DR KEGG; ypm:YP_1395; -.
DR PATRIC; fig|214092.21.peg.1836; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_2_6; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..220
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119470"
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"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:4DU6"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4DU6"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:4DU6"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4DU6"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4DU6"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:4DU6"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4DU6"
SQ SEQUENCE 220 AA; 24714 MW; 5B497C8B4FA301F8 CRC64;
MSSLSKEAEL VHQALLARGL ETPLRKPELD AETRKTRIQA HMTEVMHLLN LDLTDDSLAD
TPRRIAKMYV DEIFSGLDYE NFPKITLIQN KMKVDEMVTV RDITLTSTCE HHFVTIDGKA
TVAYIPKDSV IGLSKINRIV QFFAQRPQVQ ERLTQQILLA LQTLLGTNNV AVSIDAVHYC
VKARGIRDAT SATTTTSLGG LFKSSQNTRQ EFLRAVRHHG
