GCH1L_SALTY
ID GCH1L_SALTY Reviewed; 247 AA.
AC P67270; Q8XFW7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN Name=ybgI; OrderedLocusNames=STM0711;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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}.
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DR EMBL; AE006468; AAL19655.1; -; Genomic_DNA.
DR RefSeq; NP_459696.1; NC_003197.2.
DR RefSeq; WP_000798844.1; NC_003197.2.
DR AlphaFoldDB; P67270; -.
DR SMR; P67270; -.
DR STRING; 99287.STM0711; -.
DR PaxDb; P67270; -.
DR EnsemblBacteria; AAL19655; AAL19655; STM0711.
DR GeneID; 1252231; -.
DR KEGG; stm:STM0711; -.
DR PATRIC; fig|99287.12.peg.743; -.
DR HOGENOM; CLU_037423_3_0_6; -.
DR OMA; HGLFWRG; -.
DR PhylomeDB; P67270; -.
DR BioCyc; SENT99287:STM0711-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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_0000147325"
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; 26946 MW; 77DBD96968C8C27A CRC64;
MKNTELEQLI NDKLNSAAIS DYAPNGLQVE GKETVQKIVT GVTASQALLD EAVRLQADAV
IVHHGYFWKG ESPVIRGMKR RRLKTLLAND INLYGWHLPL DAHPELGNNA QLAALLGITV
KGEIEPLVPW GELSMPVPGL ELASWIEARL GRKPLWCGDT GPENVQRVAW CTGGGQSFID
SAARFGVDAF ITGEVSEQTI HSAREQGLHF YAAGHHATER GGIRALSEWL NENTALDVTF
IDIPNPA
