CAZyme Information: KDQ27218.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ27218.1
• CAZy Family: GH13
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
522		57357.40	4.8579

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PostreatusPC15	12460	1137138	164	12296

• Gene Location: location=KL198009:142804-144923(-)

Full Sequence      

MIAPVLSFGLTVLSLLSPTNAAIGPVAELDIVNRHIAPDGYSRQAILANGIFPGPLIVGQ
KGDTFRLNVKDSLNDPTMKTSTSIHWHGLYQEKTTWADGPAFVTQCPIVPGHSFEYNFHV
PEQAGTFWYHAHYGTQYCDGLRGPFVIYDDCDPHKDLYDVDDESTVLTIGDWYHPTAEEL
VARGGPPQPDLTVFNGIGRSVDGPPVPLYVLNVEQGKRYRIRLINIACEPNYNFTIDGHQ
MTIIETDGENTVPLDVDAIDIFASQRYSFVLHANQPIGNYWIRGNPSAGPTGFQNGINSA
ILRYKGAPLVEPSTPYINATNPMREVDLHALENPAAPGLPFPGGADILLNFAFSFDPMTS
RFATNGVSFQSPTVPVLLQILSGAQSAQSMLTEGGVYTLPPNKVIEISMPGGVNGGPHPF
HLHGHTFSVVRSAGSSVYNYENPVRRDVVSIGDRGDNVTIRFVTDNNGPWFLHCHVDWHL
DLGLAVVLAENPRDVPYDEPIPQAWYDLCPIYDDYNRTHPST

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	36	338	1.8e-150	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.45e-83	30	490	7	523	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
259970	CuRO_3_Tv-LCC_like	1.25e-82	346	492	1	147	The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259925	CuRO_1_Tv-LCC_like	1.47e-78	25	149	1	125	The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. 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.
274556	laccase	3.81e-73	42	487	21	516	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
259949	CuRO_2_Tv-LCC_like	9.93e-73	165	315	1	154	The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAR48257.1|AA1_1	0.0	1	522	1	522
CAR48260.1|AA1_1	0.0	1	522	1	522
BAI66145.1|AA1_1	5.14e-316	1	522	1	523
AQX45445.1|AA1_1	2.01e-238	20	521	19	515
AKE48164.1|AA1_1	2.01e-238	20	521	19	515

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NQ8_A	6.10e-230	14	513	14	511	Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]
2HRG_A	8.63e-227	22	513	1	489	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
6H5Y_A	7.04e-226	22	513	1	489	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]
5ANH_A	2.32e-224	22	513	1	489	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]
1GYC_A	5.21e-224	22	513	1	492	Chain A, LACCASE 2 [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12718|LAC2_TRAVE	1.92e-223	13	513	12	512	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q02497|LAC1_TRAHI	1.99e-223	12	513	12	513	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	1.56e-222	13	513	12	512	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|O59896|LAC1_PYCCI	4.31e-222	14	513	14	511	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1
sp|Q99044|LAC1_TRAVI	4.62e-222	12	513	12	513	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000355	0.999619	CS pos: 21-22. Pr: 0.9779

TMHMM  Annotations     

There is no transmembrane helices in KDQ27218.1.