ID   GCH1L_ECO57             Reviewed;         247 AA.
AC   P0AFP8; P75743;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   Name=ybgI; OrderedLocusNames=Z0861, ECs0735;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Provides significant protection from radiation damage and may
CC       be involved in the degradation of radiation-damaged nucleotides.
CC       {ECO:0000250|UniProtKB:P0AFP6}.
CC   -!- SUBUNIT: Toroid-shaped homohexamer. In the hexamer, 3 dimers assemble
CC       to form a ring-like structure surrounding a central hole.
CC       {ECO:0000250|UniProtKB:P0AFP6}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005174; AAG55033.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34158.1; -; Genomic_DNA.
DR   PIR; E85571; E85571.
DR   PIR; G90720; G90720.
DR   RefSeq; NP_308762.1; NC_002695.1.
DR   RefSeq; WP_000798871.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFP8; -.
DR   SMR; P0AFP8; -.
DR   STRING; 155864.EDL933_0776; -.
DR   EnsemblBacteria; AAG55033; AAG55033; Z0861.
DR   EnsemblBacteria; BAB34158; BAB34158; ECs_0735.
DR   GeneID; 66671021; -.
DR   GeneID; 917104; -.
DR   KEGG; ece:Z0861; -.
DR   KEGG; ecs:ECs_0735; -.
DR   PATRIC; fig|386585.9.peg.851; -.
DR   eggNOG; COG0327; Bacteria.
DR   HOGENOM; CLU_037423_3_0_6; -.
DR   OMA; HGLFWRG; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Metal-binding; Reference proteome.
FT   CHAIN           1..247
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147308"
FT   BINDING         63
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         64
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         101
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         215
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ   SEQUENCE   247 AA;  26892 MW;  07436A9E410DF007 CRC64;
     MKNTELEQLI NEKLNSAAIS DYAPNGLQVE GKETVQKIVT GVTASQALLD EAVRLGADAV
     IVHHGYFWKG ESPVIRGMKR NRLKTLLAND INLYGWHLPL DAHPELGNNA QLAALLGITV
     MGEIEPLVPW GELTMPVPGL ELASWIEARL GRKPLWCGDT GPEVVQRVAW CTGGGQSFID
     SAARFGVDAF ITGEVSEQTI HSAREQGLHF YAAGHHATER GGIRALSEWL NENTDLDVTF
     IDIPNPA