YFEX_ECOLI
ID YFEX_ECOLI Reviewed; 299 AA.
AC P76536; Q2MAJ5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dye-decolorizing peroxidase YfeX {ECO:0000305};
DE EC=1.11.1.- {ECO:0000269|PubMed:22068980};
DE AltName: Full=Porphyrinogen oxidase {ECO:0000303|PubMed:22068980};
GN Name=yfeX; OrderedLocusNames=b2431, JW2424;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP PRELIMINARY FUNCTION AS A DEFERROCHELATASE, COFACTOR, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF HIS-215.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19564607; DOI=10.1073/pnas.0903842106;
RA Letoffe S., Heuck G., Delepelaire P., Lange N., Wandersman C.;
RT "Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11719-11724(2009).
RN [4]
RP FUNCTION AS AN OXIDASE, AND COFACTOR.
RX PubMed=22068980; DOI=10.1128/mbio.00248-11;
RA Dailey H.A., Septer A.N., Daugherty L., Thames D., Gerdes S., Stabb E.V.,
RA Dunn A.K., Dailey T.A., Phillips J.D.;
RT "The Escherichia coli protein YfeX functions as a porphyrinogen oxidase,
RT not a heme dechelatase.";
RL MBio 2:E00248-E00248(2011).
CC -!- FUNCTION: Has both general peroxidase activity and dye-decolorizing
CC activity. Can catalyze the oxidation of both protoporphyrinogen IX and
CC coproporphyrinogen III to their corresponding porphyrins. Also
CC efficiently decolorizes the dyes alizarin red and Cibacron blue F3GA.
CC {ECO:0000269|PubMed:22068980}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000305|PubMed:19564607, ECO:0000305|PubMed:22068980};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
CC {ECO:0000250|UniProtKB:Q8XBI9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19564607}.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a deferrochelatase, which
CC promotes iron extraction from exogenous heme source, preserving the
CC tetrapyrrol ring intact (PubMed:19564607). However, Dailey et al. were
CC unable to reproduce the in vitro dechelation reaction
CC (PubMed:22068980). They suggest that YfeX is a typical dye-decolorizing
CC peroxidase and not a dechelatase, and that the protoporphyrin reported
CC by Letoffe et al. to accumulate when YfeX is overexpressed likely
CC arises from the intracellular oxidation of endogenously synthesized
CC protoporphyrinogen and not from dechelation of exogenously supplied
CC heme (PubMed:22068980). {ECO:0000269|PubMed:22068980,
CC ECO:0000305|PubMed:19564607}.
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DR EMBL; U00096; AAC75484.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76711.1; -; Genomic_DNA.
DR PIR; F65017; F65017.
DR RefSeq; NP_416926.4; NC_000913.3.
DR RefSeq; WP_001350538.1; NZ_LN832404.1.
DR AlphaFoldDB; P76536; -.
DR SMR; P76536; -.
DR BioGRID; 4260737; 17.
DR DIP; DIP-47971N; -.
DR IntAct; P76536; 5.
DR STRING; 511145.b2431; -.
DR PeroxiBase; 5875; EcoDyPrx02_K12.
DR jPOST; P76536; -.
DR PaxDb; P76536; -.
DR PRIDE; P76536; -.
DR DNASU; 946913; -.
DR EnsemblBacteria; AAC75484; AAC75484; b2431.
DR EnsemblBacteria; BAE76711; BAE76711; BAE76711.
DR GeneID; 946913; -.
DR KEGG; ecj:JW2424; -.
DR KEGG; eco:b2431; -.
DR PATRIC; fig|1411691.4.peg.4300; -.
DR EchoBASE; EB3917; -.
DR eggNOG; COG2837; Bacteria.
DR HOGENOM; CLU_044178_2_0_6; -.
DR InParanoid; P76536; -.
DR OMA; CAEPNLH; -.
DR PhylomeDB; P76536; -.
DR BioCyc; EcoCyc:G7266-MON; -.
DR BioCyc; MetaCyc:G7266-MON; -.
DR PRO; PR:P76536; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:EcoCyc.
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 Cytoplasm; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..299
FT /note="Dye-decolorizing peroxidase YfeX"
FT /id="PRO_0000201328"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q47KB1"
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:0000250|UniProtKB:Q8XBI9"
FT MUTAGEN 215
FT /note="H->A: Strong decrease in affinity for heme and
FT protoporphyrin."
FT /evidence="ECO:0000269|PubMed:19564607"
SQ SEQUENCE 299 AA; 33052 MW; B64D99408BB9126F CRC64;
MSQVQSGILP EHCRAAIWIE ANVKGEVDAL RAASKTFADK LATFEAKFPD AHLGAVVAFG
NNTWRALSGG VGAEELKDFP GYGKGLAPTT QFDVLIHILS LRHDVNFSVA QAAMEAFGDC
IEVKEEIHGF RWVEERDLSG FVDGTENPAG EETRREVAVI KDGVDAGGSY VFVQRWEHNL
KQLNRMSVHD QEMVIGRTKE ANEEIDGDER PETSHLTRVD LKEDGKGLKI VRQSLPYGTA
SGTHGLYFCA YCARLHNIEQ QLLSMFGDTD GKRDAMLRFT KPVTGGYYFA PSLDKLMAL
