CAZyme Information: KDQ22995.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ22995.1
• CAZy Family: AA3
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
516		55681.49	5.0465

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=KL198014:1054528-1057041(+)

Full Sequence      

MSPAVCLPFLLPFLLYTAHLASAANGPTADLHIVNKVIAPDGFSRSTVLAGLSSSSGQFP
GPLITGNKGDHFQINVIDELVDNSMLLDTSIHWHGFYQKGSNWADGPAFVTQCPIVPGDS
FLYSFSAPDQAGTFWYHSHLSTQYCDGLRGVFVVYDPEDPHRSLYDVDDEDTVITLADWY
HVPAPSAGLVPVSQSTLINGLGLYQDGPESPLAVIHVKRGSRYRFRLVSISCDPNHVFAI
DGHNMTIIEVDSVNTQPLVVDSIQIFPGQRYSFVLNANQQVDNYWIRASPNLGPQGFAGG
LNSAILRYVGAPEAHPNSSETQSSHPMLQTDLVPLENPGAPGPHELGAADVSINLGIAFD
EEKFKFSINGVSYVNPTAPVLLQILSGAMDATSLLPAGSVYVLPPNKVIEVSIPGLATGG
PHPFHLHGHSFDVIRSAGSSTYNFANPVRRDVVSTGVTGDNVTIRFTTDNAGPWFLHCHI
DWHLELGLAIVFAEDTKSVHDQATPASWDQLCPKSS

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	342	6.1e-153	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	8.50e-88	350	495	1	146	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.
259949	CuRO_2_Tv-LCC_like	3.78e-79	172	324	1	159	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.
274555	ascorbase	1.45e-77	39	494	14	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.
259925	CuRO_1_Tv-LCC_like	6.74e-77	27	156	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.
177843	PLN02191	5.23e-71	56	494	48	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFD97050.1|AA1_1	5.21e-264	9	513	4	507
ARD69908.1|AA1_1	1.72e-263	13	513	8	509
AFE48786.2|AA1_1	9.80e-260	21	513	16	507
BAI66142.1|AA1_1	7.41e-258	21	513	21	513
AAD30965.1|AA1_1	1.27e-257	10	513	12	508

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z1X_A	2.76e-233	24	512	1	484	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
2HRG_A	3.62e-229	24	513	1	486	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]
5A7E_A	5.14e-229	24	513	1	486	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
4JHU_A	1.03e-228	26	513	3	486	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5ANH_A	1.03e-228	26	513	3	486	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	1.27e-254	1	513	1	517	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	4.89e-251	1	513	1	515	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q12719|LAC4_TRAVE	1.06e-233	22	513	21	510	Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1
sp|Q99055|LAC4_TRAVI	4.28e-233	22	513	21	510	Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1
sp|Q01679|LAC1_PHLRA	7.03e-232	21	513	19	510	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000208	0.999799	CS pos: 23-24. Pr: 0.9808

TMHMM  Annotations     

There is no transmembrane helices in KDQ22995.1.