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YIBF_ECOLI
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   03-AUG-2022, entry version 115.
DE   RecName: Full=Uncharacterized GST-like protein YibF;
GN   Name=yibF; OrderedLocusNames=b3592, JW3565;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; 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; P0ACA1; -.
DR   PRIDE; P0ACA1; -.
DR   EnsemblBacteria; AAC76616; AAC76616; b3592.
DR   EnsemblBacteria; BAE77701; BAE77701; BAE77701.
DR   GeneID; 66672515; -.
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; VDIGTIA; -.
DR   PhylomeDB; P0ACA1; -.
DR   BioCyc; EcoCyc:EG11762-MON; -.
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   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   InterPro; IPR034343; YibF.
DR   PANTHER; PTHR42673:SF12; PTHR42673:SF12; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 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
 
 
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