YFEX_ECO57
ID YFEX_ECO57 Reviewed; 299 AA.
AC Q8XBI9; Q7ABS6;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dye-decolorizing peroxidase YfeX {ECO:0000303|PubMed:28109884};
DE EC=1.11.1.- {ECO:0000269|PubMed:28109884};
GN Name=yfeX {ECO:0000303|PubMed:28109884};
GN OrderedLocusNames=ECs3302 {ECO:0000312|EMBL:BAB36725.2};
GN ORFNames=ECpv15279_3233 {ECO:0000312|EMBL:BBC51568.1};
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 / 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Pv15-279;
RA Ogura Y., Seto K., Morimoto Y., Nakamura K., Gotoh Y., Toyoda A., Itoh T.,
RA Ohnishi M., Hayashi T.;
RT "Genomic characterization of a non-sorbitol-fermenting and b-glucuronidase-
RT positive O157:H7 strain.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:5GT2}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
RP COFACTOR, AND MUTAGENESIS OF ASP-143; HIS-215; ARG-232; SER-234 AND
RP LEU-246.
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=28109884; DOI=10.1016/j.bbrc.2017.01.081;
RA Liu X., Yuan Z., Wang J., Cui Y., Liu S., Ma Y., Gu L., Xu S.;
RT "Crystal structure and biochemical features of dye-decolorizing peroxidase
RT YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles
RT toward different substrates.";
RL Biochem. Biophys. Res. Commun. 484:40-44(2017).
CC -!- FUNCTION: Has both general peroxidase activity and dye-decolorizing
CC activity. Can catalyze the oxidation of 2,2'-azino-bis(3-
CC ethylbenzothiazoline-6-sulphonic acid) (ABTS), and the phenolic
CC compounds guaiacol and catechol. Also decolorizes the anthraquinone dye
CC reactive blue 19 (RB19). {ECO:0000269|PubMed:28109884}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:28109884};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
CC {ECO:0000269|PubMed:28109884};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P76536}.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR EMBL; BA000007; BAB36725.2; -; Genomic_DNA.
DR EMBL; AP018488; BBC51568.1; -; Genomic_DNA.
DR RefSeq; NP_311329.2; NC_002695.1.
DR RefSeq; WP_001301804.1; NZ_SWKA01000005.1.
DR PDB; 5GT2; X-ray; 2.09 A; A/B/C/D=1-299.
DR PDBsum; 5GT2; -.
DR AlphaFoldDB; Q8XBI9; -.
DR SMR; Q8XBI9; -.
DR STRING; 155864.EDL933_3594; -.
DR PeroxiBase; 5885; EcoH7DyPrx02.
DR EnsemblBacteria; BAB36725; BAB36725; ECs_3302.
DR GeneID; 915365; -.
DR KEGG; ecs:ECs_3302; -.
DR PATRIC; fig|386585.9.peg.3449; -.
DR eggNOG; COG2837; Bacteria.
DR HOGENOM; CLU_044178_2_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006314; Dyp_peroxidase.
DR Pfam; PF04261; Dyp_perox; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..299
FT /note="Dye-decolorizing peroxidase YfeX"
FT /id="PRO_0000445654"
FT BINDING 215
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:28109884"
FT MUTAGEN 143
FT /note="D->A,N: Lacks both peroxidase and dye-decolorizing
FT activities."
FT /evidence="ECO:0000269|PubMed:28109884"
FT MUTAGEN 215
FT /note="H->A: Lacks both peroxidase and dye-decolorizing
FT activities."
FT /evidence="ECO:0000269|PubMed:28109884"
FT MUTAGEN 232
FT /note="R->E,L: Lacks dye-decolorizing activity. Lacks
FT peroxidase activity towards ABTS, but retains activity
FT towards guaiacol and catechol."
FT /evidence="ECO:0000269|PubMed:28109884"
FT MUTAGEN 234
FT /note="S->Y: Lacks both peroxidase and dye-decolorizing
FT activities."
FT /evidence="ECO:0000269|PubMed:28109884"
FT MUTAGEN 246
FT /note="L->W: Lacks both peroxidase and dye-decolorizing
FT activities."
FT /evidence="ECO:0000269|PubMed:28109884"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5GT2"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:5GT2"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5GT2"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:5GT2"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 244..253
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:5GT2"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5GT2"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:5GT2"
FT TURN 293..297
FT /evidence="ECO:0007829|PDB:5GT2"
SQ SEQUENCE 299 AA; 33096 MW; 9D9A852D3BF3C6DE CRC64;
MSQVQSGILP EHCRAAIWIE ANVKGEVDAL RAASKTFADK LATFEAKFPD AHLGAVVAFG
NNIWRALSGG VGAEELKDFP GYGKGLAPTT QFDVLIHILS LRHDVNFSVA QAAMEAFGDC
IEVKEEIHGF RWVEERDLSG FVDGTENPAG EETRREVAVI KDGVDAGGSY VFVQRWEHNL
KQLNRMSVHD QEMMIGRTKE ANEEIDGDER PETSHLTRVD LKEDGKGLKI VRQSLPYGTA
SGTHGLYFCA YCARLHNIEQ QLLSMFGDTD GKRDAMLRFT KPVTGGYYFA PSLDKLMAL
