DYP_THEFY
ID DYP_THEFY Reviewed; 430 AA.
AC Q47KB1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Dye-decolorizing peroxidase Tfu_3078;
DE Short=DyP;
DE EC=1.11.1.19;
DE AltName: Full=Peroxidase Tfu_3078;
DE Flags: Precursor;
GN OrderedLocusNames=Tfu_3078;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [2]
RP FUNCTION AS A PEROXIDASE, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, EXPORT VIA THE TAT-SYSTEM, SUBCELLULAR
RP LOCATION, SUBUNIT, ACTIVE SITES, AND MUTAGENESIS OF ASP-242 AND HIS-338.
RX PubMed=19967355; DOI=10.1007/s00253-009-2369-x;
RA van Bloois E., Torres Pazmino D.E., Winter R.T., Fraaije M.W.;
RT "A robust and extracellular heme-containing peroxidase from Thermobifida
RT fusca as prototype of a bacterial peroxidase superfamily.";
RL Appl. Microbiol. Biotechnol. 86:1419-1430(2010).
CC -!- FUNCTION: Peroxidase that is able to convert a large number of
CC compounds, but its physiological substrate is not known. Shows high
CC reactivity towards anthraquinone dyes (e.g. Reactive Blue 19) and a
CC modest activity towards standard peroxidase substrates (such as
CC guaiacol and 2,6-dimethoxyphenol) and azo dyes (e.g. Reactive Blue 5).
CC Is also able to oxidize aromatic sulfides enantioselectively, resulting
CC in the corresponding (R)-sulfoxides, but with a poor efficiency. Does
CC not display catalase activity. {ECO:0000269|PubMed:19967355}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-
CC amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2
CC H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563,
CC ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278;
CC EC=1.11.1.19;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:19967355};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
CC {ECO:0000269|PubMed:19967355};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for Reactive Blue 19 {ECO:0000269|PubMed:19967355};
CC KM=27 uM for H(2)O(2) {ECO:0000269|PubMed:19967355};
CC Note=kcat is 10 sec(-1) with Reactive Blue 19 as substrate.;
CC pH dependence:
CC Optimum pH is 3.5 with Reactive Blue 19 as substrate.
CC {ECO:0000269|PubMed:19967355};
CC Temperature dependence:
CC Optimum temperature is about 25 degrees Celsius. Thermostable.
CC Retains 50% of its activity after heating 2 hours at 60 degrees
CC Celsius, while no decrease in activity is observed within the same
CC time at 30 or 40 degrees Celsius. {ECO:0000269|PubMed:19967355};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19967355}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19967355}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR EMBL; CP000088; AAZ57111.1; -; Genomic_DNA.
DR RefSeq; WP_011293495.1; NC_007333.1.
DR PDB; 5FW4; X-ray; 1.80 A; A/B=1-430.
DR PDBsum; 5FW4; -.
DR AlphaFoldDB; Q47KB1; -.
DR SMR; Q47KB1; -.
DR STRING; 269800.Tfu_3078; -.
DR EnsemblBacteria; AAZ57111; AAZ57111; Tfu_3078.
DR KEGG; tfu:Tfu_3078; -.
DR eggNOG; COG2837; Bacteria.
DR HOGENOM; CLU_039488_1_2_11; -.
DR OMA; FVCWQAD; -.
DR OrthoDB; 837319at2; -.
DR BioCyc; MetaCyc:MON-15995; -.
DR BRENDA; 1.11.1.19; 12263.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006314; Dyp_peroxidase.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04261; Dyp_perox; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Secreted; Signal.
FT SIGNAL 1..39
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 40..430
FT /note="Dye-decolorizing peroxidase Tfu_3078"
FT /id="PRO_5000099631"
FT REGION 42..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:19967355"
FT BINDING 338
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:0000305"
FT MUTAGEN 242
FT /note="D->A: 0.7% of wild-type catalytic activity. Still
FT able to bind heme."
FT /evidence="ECO:0000269|PubMed:19967355"
FT MUTAGEN 338
FT /note="H->A: Lacks the heme cofactor. 3% of wild-type
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:19967355"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 97..120
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:5FW4"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:5FW4"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:5FW4"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 275..284
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:5FW4"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 369..380
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5FW4"
FT STRAND 404..414
FT /evidence="ECO:0007829|PDB:5FW4"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:5FW4"
SQ SEQUENCE 430 AA; 45928 MW; 6975FA82686601C0 CRC64;
MTEPDTERKG SSRRGFLAGL GAAALTGAGI GMAAGEVLRP LLPDSDPAAS PEAEQRLRMA
AQRADATAAP QPGISGPAPA FVHVIALDLA EEARKNPDTA RDSAAAALRS WTELAARLHE
ESPHDIAEGA ASAGLLPASL MVTVGIGGSL LSAIDAEDRR PDALADLPEF STDDLHPRWC
GGDFMLQVGA EDPMVLTAAV EELVAAAADA TAVRWSLRGF RRTAAAARDP DATPRNLMGQ
IDGTANPAQD HPLFDRTITA RPADNPAHAW MDGGSYLVVR RIRMLLTEWR KLDVAARERV
IGRRLDTGAP LGSRNETDPV VLSARDEEGE PLIPENAHVR LASPENNLGA RMFRRGYSYD
QGWRDDGVRD AGLLFMAWQG DPATGFIPVQ RSLADQGDAL NRYIRHEGSA LFAVPAAREG
RYLGQDLIEG
