CAZyme Information: KDQ27221.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ27221.1
• CAZy Family: GH13
• CAZyme Description: multi-copper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
537		58805.12	5.0975

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=KL198009:139479-142081(+)

Full Sequence      

MSSLSSLAWLTLPILANAAFGPIADIHVVNSDIAPDGFQRPAVLVEGTYPAPLIAGNKGD
HFQLNVINELYDTTMNTDTSIHWHGILHHSTNYADGAAMVTQCPIVPNESFLYDFHVPDQ
AGTYWYHSHLHAQYCDGLRGPFIVYDPEDPHKDLYDVDDESTILTIGDWYHTPSTEASVP
VADSTLFNGIGRYAGGPQVPLYVFNVEFGKRYRIRLINIGCDPYYNFTIAGHNFTIIEAD
GENTRPHKVDFIQILAGQRYSIILDANQEIDNYWIRANPNPDSGIPGFVDGINSAILRYQ
GAPDAEPTQGEVVPAKPLHETRLHALANPSAPGIHVPGAADINIQLDFGLDFANGVFTVN
GLPFASPDVPVLLQILSGAQTAQDILPPGSVFTLEPNKVVELTLTPLALGGPHPIHLHGH
TFSVVKSAGSNSWNWHNPVRRDTVMLGVEDGDNVVIRFVTDNPGPWFLHCHIDWHLEIGF
AAVFAEDPLGTAAANPVTPEWSDLCPLYNATQSRTPALLKTLAKSPSHRILPAHLRR

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	33	333	2.6e-147	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	1.04e-80	341	488	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.
274555	ascorbase	2.15e-75	34	486	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.
259949	CuRO_2_Tv-LCC_like	1.76e-73	162	308	1	152	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.
259925	CuRO_1_Tv-LCC_like	3.58e-72	22	146	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	6.63e-66	40	506	22	532	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAI66143.1|AA1_1	1.48e-262	16	514	17	516
AHC32223.1|AA1_1	2.99e-262	16	514	17	516
BAI66140.1|AA1_1	1.40e-260	16	514	17	516
BAI66141.1|AA1_1	4.08e-243	7	514	1	516
BAI66139.1|AA1_1	7.46e-234	18	509	19	510

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z1X_A	1.73e-220	19	510	1	489	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]
1GYC_A	1.66e-214	19	509	1	492	Chain A, LACCASE 2 [Trametes versicolor]
5A7E_A	9.90e-213	19	510	1	490	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
4A2D_A	1.99e-212	19	510	1	490	Coriolopsis gallica Laccase T2 Copper Depleted at pH 4.5 [Coriolopsis gallica],4A2E_A Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5 [Coriolopsis gallica],4A2G_A Coriolopsis gallica laccase collected at 8.98 keV [Coriolopsis gallica],4A2H_A Crystal Structure of Laccase from Coriolopsis gallica pH 7.0 [Coriolopsis gallica]
6H5Y_A	1.99e-212	19	510	1	490	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	3.45e-219	16	510	21	521	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	9.25e-216	17	510	22	519	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q01679|LAC1_PHLRA	3.62e-213	16	510	19	514	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2
sp|Q99046|LAC2_TRAVI	2.01e-212	9	509	9	512	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|Q12718|LAC2_TRAVE	2.84e-212	9	509	9	512	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000328	0.999687	CS pos: 18-19. Pr: 0.9788

TMHMM  Annotations     

There is no transmembrane helices in KDQ27221.1.