GCH1L_ECOL6
ID GCH1L_ECOL6 Reviewed; 247 AA.
AC P0AFP7; P75743;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN Name=ybgI; OrderedLocusNames=c0789;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
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DR EMBL; AE014075; AAN79262.1; -; Genomic_DNA.
DR RefSeq; WP_000798871.1; NC_004431.1.
DR AlphaFoldDB; P0AFP7; -.
DR SMR; P0AFP7; -.
DR STRING; 199310.c0789; -.
DR PRIDE; P0AFP7; -.
DR EnsemblBacteria; AAN79262; AAN79262; c0789.
DR GeneID; 66671021; -.
DR KEGG; ecc:c0789; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_3_0_6; -.
DR OMA; HGLFWRG; -.
DR BioCyc; ECOL199310:C0789-MON; -.
DR Proteomes; UP000001410; 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.
FT CHAIN 1..247
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147309"
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
