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CAZyme Information: EPrPAT00000019449-p1

You are here: Home > Sequence: EPrPAT00000019449-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Pythium aphanidermatum
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
CAZyme ID EPrPAT00000019449-p1
CAZy Family GH5
CAZyme Description Multicopper oxidase type 2.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
693 PaphDAOMBR444_SC0269|CGC1 78868.17 6.3738
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444 12363 1223555 58 12305
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.10.3.2:4 1.10.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 124 683 4.1e-34 0.9720670391061452

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259922 CuRO_1_Tth-MCO_like 1.80e-59 104 228 1 138
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
400195 Cu-oxidase_3 2.21e-26 127 233 19 119
Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259869 CuRO_1_LCC_like 9.45e-25 106 228 2 119
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
225043 SufI 1.65e-24 88 688 16 448
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
259924 CuRO_1_McoC_like 4.23e-19 127 228 25 120
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins. This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.93e-38 159 688 5 468
6.96e-19 135 448 20 280
7.62e-10 129 232 107 205
4.00e-09 129 265 50 178
4.20e-09 129 247 50 159

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.02e-22 127 688 39 438
Crystal structure of Laccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],2XUW_A Crystal Structure of Apolaccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],2XVB_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Hg, crystal of the apoenzyme soaked for 5 min. in 5 mM HgCl2 at 278 K. [Thermus thermophilus HB27],2YAE_A X-ray induced reduction of laccase from Thermus thermophilus HB27(0.0- 12.5 percent dose) [Thermus thermophilus HB27],2YAF_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (12. 5-25.0 percent dose) [Thermus thermophilus HB27],2YAH_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (25. 0-37.5 percent dose) [Thermus thermophilus HB27],2YAM_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (37. 5-50.0 percent dose) [Thermus thermophilus HB27],2YAO_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (50. 0-62.5 percent dose) [Thermus thermophilus HB27],2YAP_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (62. 5-75.0 percent dose) [Thermus thermophilus HB27],2YAQ_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (75. 0-87.5 percent dose) [Thermus thermophilus HB27],2YAR_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (87. 5-100.0 percent dose) [Thermus thermophilus HB27],4AI7_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Hg, crystal of the apoenzyme soaked for 2 h in 5 mM HgCl2 at 278 K. [Thermus thermophilus HB27],5AFA_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Ag, crystal of the holoenzyme soaked for 30 m in 5 mM AgNO3 at 278 K. [Thermus thermophilus HB27],5G3B_A Preserving metallic sites affected by radiation damage: the CuT2 case in Thermus thermophilus multicopper oxidase [Thermus thermophilus],5G3C_A Preserving Metallic sites affected by radiation damage the CuT2 case in thermus termophilus multicopper oxidase [Thermus thermophilus],5G3D_A preserving Metallic Sites Affected by Radiation Damage the CuT2 cCase in Thermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3E_A Preserving Metallic Sites Affected by Radiation DAmage the CuT2 CAse in THermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3F_A Preserving Metallic Sites Affected by Radiation Damage the CuT2 CAse in Thermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3G_A Preserving MEtallic Sites Affected by Radiation Damage the CuT2 case in Thermus Thermophilus multicopper Oxidase [Thermus thermophilus],5G3H_A Preserving Metallic Sites Affected by Radiation Damage the CuT2 Case in Thermus Thermophilus Multicopper oxidase [Thermus thermophilus],5JRR_A Crystal structure of native laccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],5JX9_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu(II)-cyclophanes, 5 min) [Thermus thermophilus HB27],5K0D_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu(II)-cyclophanes, 3 min) [Thermus thermophilus HB27],5K15_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu2PO, 8 min) [Thermus thermophilus HB27],5K3K_A Crystal structure of laccase from Thermus thermophilus HB27 (CuSO4, 20 min) [Thermus thermophilus HB27],5K5K_A Crystal structure of laccasse from Thermus thermophilus HB27 (ascorbic acid 10 min) [Thermus thermophilus HB27],5K7A_A Crystal structure of laccase fron Thermus thermophilus HB27 (sodium nitrate 1.5 min) [Thermus thermophilus HB27],5K84_A Crystal structure of laccase from Thermus thermophilus HB27 (sodium nitrate 10 min) [Thermus thermophilus HB27],6Q29_A Chain A, Laccase [Thermus thermophilus HB27],6TYR_A Chain A, Laccase [Thermus thermophilus HB27]
5.07e-22 127 688 40 439
Chain A, Laccase [Thermus thermophilus HB27],6W2K_B Chain B, Laccase [Thermus thermophilus HB27],6W9X_A Chain A, Laccase [Thermus thermophilus HB27],6WCG_A Chain A, Laccase [Thermus thermophilus HB27],6WCH_A Chain A, Laccase [Thermus thermophilus HB27],6WCL_A Chain A, Laccase [Thermus thermophilus HB27],6WCM_A Chain A, Laccase [Thermus thermophilus HB27]
6.14e-22 127 688 62 461
Chain A, Laccase [Thermus thermophilus HB27],6WCP_A Chain A, Laccase [Thermus thermophilus HB27]
8.17e-15 127 688 74 479
Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
4.71e-09 127 240 26 136
Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.38e-10 124 256 71 197
Multicopper oxidase mco OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=mco PE=3 SV=2
1.24e-09 124 256 71 197
Multicopper oxidase mco OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=mco PE=3 SV=2
2.25e-09 129 248 48 158
Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
3.91e-09 129 249 50 162
Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
6.67e-09 124 256 71 197
Multicopper oxidase mco OS=Staphylococcus aureus OX=1280 GN=mco PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.828523 0.171473

TMHMM  Annotations      help

There is no transmembrane helices in EPrPAT00000019449-p1.