Entry
Name
dye decolorizing peroxidase;
DyP;
DyP-type peroxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
BRITE hierarchy
Sysname
Reactive-Blue-5:hydrogen-peroxide oxidoreductase
Reaction(IUBMB)
Reactive Blue 5 + 2 H2O2 = phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O [RN:
R10915 ]
Reaction(KEGG)
Substrate
Product
phthalate [CPD:
C01606 ];
2,2'-disulfonyl azobenzene [CPD:
C20938 ];
3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate [CPD:
C20939 ];
H2O [CPD:
C00001 ]
Comment
Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC
1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
History
EC 1.11.1.19 created 2011, modified 2015
Orthology
K15733 dye decolorizing peroxidase
Genes
MTHN : 4412656_02086(efeN)
CDIP : ERS451417_01405(ycdC)
CLW : CLAC_05825 CLAC_10930
CCYS : SAMEA4530656_0964(efeN)
CAMC : I6I65_02045 I6I65_06310
NFR : ERS450000_00996(efeN_1)
NAD : NCTC11293_01410(efeN)
RPSK : JWS13_02890 JWS13_26885
DIT : C3V38_03990 C3V38_17115 C3V38_17140
DPC : A6048_07925 A6048_15295
DKN : NHB83_00330 NHB83_10650 NHB83_14795
SVL : Strvi_0331 Strvi_9152
SHO : SHJGH_0730 SHJGH_4878
SRC : M271_24200 M271_24735 M271_25560
SMAL : SMALA_3813 SMALA_3981
SSOI : I1A49_23030(efeB) I1A49_23850
STRE : GZL_02164 GZL_04573
SCW : TU94_04855 TU94_16845
SLC : SL103_17035 SL103_35165
STRC : AA958_12605 AA958_15715
SLE : sle_36660(sle_36660) sle_58700(sle_58700)
STRT : A8713_15370 A8713_31500
SNR : SNOUR_09695 SNOUR_20485
SALU : DC74_1116 DC74_4308
SALL : SAZ_06075 SAZ_22930
SPLU : LK06_016190 LK06_029355
SAUO : BV401_00530 BV401_22685 BV401_23510
SLX : SLAV_06610 SLAV_18840
STRO : STRMOE7_02310 STRMOE7_20350
SQZ : FQU76_16095(efeB) FQU76_24320
SVN : CP980_17325(efeB) CP980_30320
SVR : CP971_15905(efeB) CP971_27750
SGF : HEP81_02157 HEP81_03961(efeB_1)
SBY : H7H31_16880(efeB) H7H31_23975
STSU : B7R87_15745 B7R87_24040
SNF : JYK04_04317 JYK04_07613(efeN_4)
SPLA : CP981_01865 CP981_20125(efeB)
SBRO : GQF42_22475(efeB) GQF42_35365
SATA : C5746_21235 C5746_31790
SHUN : DWB77_03828 DWB77_04059
SAUH : SU9_017685(efeB) SU9_033360
SROI : IAG44_08095 IAG44_21070(efeB)
SANU : K7396_07100 K7396_17280(efeB)
SMAO : CAG99_13165 CAG99_18685
SGOB : test1122_05790(efeB) test1122_12690(efeB)
SINE : KI385_23760(efeB) KI385_42090
SNIG : HEK616_33370 HEK616_68670
STUD : STRTU_001626 STRTU_003411(efeB)
SANT : QR300_21500 QR300_22355(efeB)
SYUN : MOV08_09610 MOV08_20710(efeB)
SCOA : QU709_21395(efeB) QU709_28655
STRZ : OYE22_16615(efeB) OYE22_23215
SCY : SCATT_02060 SCATT_30100
KAU : B6264_10925 B6264_22405
ABRY : NYE86_01060 NYE86_34770 NYE86_35660(efeB)
MIO : AOA12_07890 AOA12_16190
MIX : AB663_000903 AB663_002984
MAUR : BOH66_03250 BOH66_15520
MBIN : LXM64_09135 LXM64_12935
LALL : MUN78_01695 MUN78_05285
PSEV : USB125703_01202(efeN_2)
AAI : AARI_25720 AARI_30420
GAR : AOZ07_13285 AOZ07_16710
KVR : CIB50_0000332(efeN_1)
BLIN : BLSMQ_1107 BLSMQ_3650
DCO : SAMEA4475696_1082(efeN)
NEX : NE857_15650 NE857_19390
NCG : KGD84_06800 KGD84_12815
SNAH : OUQ99_06115 OUQ99_12840
MHAI : OHB01_25660 OHB01_25755 OHB01_27475
FRA : Francci3_2498 Francci3_2591
MTUA : CSH63_06790 CSH63_21850
MICH : FJK98_19285 FJK98_22120
» show all
Taxonomy
Reference
Authors
Kim SJ, Shoda M
Title
Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes.
Journal
Reference
Authors
Sugano Y, Ishii Y, Shoda M
Title
Role of H164 in a unique dye-decolorizing heme peroxidase DyP.
Journal
Reference
Authors
Zubieta C, Joseph R, Krishna SS, McMullan D, Kapoor M, Axelrod HL, Miller MD, Abdubek P, Acosta C, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Kumar A, Marciano D, Morse AT, Murphy KD, Nigoghossian E, Okach L, Oommachen S, Reyes R, Rife CL, Schimmel P, Trout CV, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA
Title
Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA.
Journal
Sequence
Reference
Authors
Sugano Y, Matsushima Y, Tsuchiya K, Aoki H, Hirai M, Shoda M
Title
Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1.
Journal
Reference
Authors
Sugano Y
Title
DyP-type peroxidases comprise a novel heme peroxidase family.
Journal
Reference
Authors
Ogola HJ, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, Shibata H, Sawa Y
Title
Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120.
Journal
Reference
Authors
van Bloois E, Torres Pazmino DE, Winter RT, Fraaije MW
Title
A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily.
Journal
Sequence
Reference
Authors
Liers C, Bobeth C, Pecyna M, Ullrich R, Hofrichter M
Title
DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes.
Journal
Reference
Authors
Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T
Title
New and classic families of secreted fungal heme peroxidases.
Journal
Other DBs
ExPASy - ENZYME nomenclature database: 1.11.1.19