ID YIBF_ECOLI Reviewed; 202 AA.
AC P0ACA1; P32105; Q2M7Q5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Uncharacterized GST-like protein YibF;
GN Name=yibF; OrderedLocusNames=b3592, JW3565;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8387990; DOI=10.1128/jb.175.10.2799-2808.1993;
RA Zhao S., Sandt C.H., Feulner G., Vlazny D.A., Gray J.A., Hill C.W.;
RT "Rhs elements of Escherichia coli K-12: complex composites of shared and
RT unique components that have different evolutionary histories.";
RL J. Bacteriol. 175:2799-2808(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ECOR 32;
RX PubMed=8536964; DOI=10.1093/genetics/141.1.15;
RA Hill C.W., Feulner G., Brody M.S., Zhao S., Sadosky A.B., Sandt C.H.;
RT "Correlation of Rhs elements with Escherichia coli population structure.";
RL Genetics 141:15-24(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PUTATIVE FUNCTION IN SELENIUM BIOCHEMISTRY.
RX PubMed=14635120; DOI=10.1002/prot.10452;
RA Rife C.L., Parsons J.F., Xiao G., Gilliland G.L., Armstrong R.N.;
RT "Conserved structural elements in glutathione transferase homologues
RT encoded in the genome of Escherichia coli.";
RL Proteins 53:777-782(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RA Ladner J.E., Stournan N.V., Branch M.C., Harp J., Schaab M., Brown D.W.,
RA Armstrong R.N.;
RT "Structural and functional genomics of YibF, a glutathione transferase
RT homologue from Escherichia coli.";
RL Submitted (MAR-2012) to the PDB data bank.
CC -!- FUNCTION: Glutathione (GSH) transferase homolog, that might be involved
CC in selenium metabolism.
CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC {ECO:0000305}.
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DR EMBL; L19044; AAC95064.1; -; Genomic_DNA.
DR EMBL; U16247; AAA56754.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18569.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76616.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77701.1; -; Genomic_DNA.
DR PIR; S47813; S47813.
DR RefSeq; NP_418049.1; NC_000913.3.
DR RefSeq; WP_000779792.1; NZ_STEB01000018.1.
DR PDB; 3R2Q; X-ray; 1.05 A; A=1-202.
DR PDBsum; 3R2Q; -.
DR AlphaFoldDB; P0ACA1; -.
DR SMR; P0ACA1; -.
DR BioGRID; 4261877; 20.
DR BioGRID; 852420; 1.
DR IntAct; P0ACA1; 2.
DR STRING; 511145.b3592; -.
DR jPOST; P0ACA1; -.
DR PaxDb; 511145-b3592; -.
DR EnsemblBacteria; AAC76616; AAC76616; b3592.
DR GeneID; 83578893; -.
DR GeneID; 948113; -.
DR KEGG; ecj:JW3565; -.
DR KEGG; eco:b3592; -.
DR PATRIC; fig|1411691.4.peg.3119; -.
DR EchoBASE; EB1712; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_12_3_6; -.
DR InParanoid; P0ACA1; -.
DR OMA; RVICRYL; -.
DR OrthoDB; 8634103at2; -.
DR PhylomeDB; P0ACA1; -.
DR BioCyc; EcoCyc:EG11762-MONOMER; -.
DR PRO; PR:P0ACA1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR CDD; cd03205; GST_C_6; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..202
FT /note="Uncharacterized GST-like protein YibF"
FT /id="PRO_0000185874"
FT DOMAIN 1..78
FT /note="GST N-terminal"
FT DOMAIN 83..202
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 49
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 62..63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT CONFLICT 195
FT /note="A -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3R2Q"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3R2Q"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3R2Q"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3R2Q"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 84..112
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 153..168
FT /evidence="ECO:0007829|PDB:3R2Q"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3R2Q"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3R2Q"
SQ SEQUENCE 202 AA; 22545 MW; BFEA058143049D67 CRC64;
MKLVGSYTSP FVRKLSILLL EKGITFEFIN ELPYNADNGV AQFNPLGKVP VLVTEEGECW
FDSPIIAEYI ELMNVAPAML PRDPLESLRV RKIEALADGI MDAGLVSVRE QARPAAQQSE
DELLRQREKI NRSLDVLEGY LVDGTLKTDT VNLATIAIAC AVGYLNFRRV APGWCVDRPH
LVKLVENLFS RESFARTEPP KA
//
