CAZyme Information: KDQ27220.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ27220.1
• CAZy Family: GH13
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
518		56515.32	6.9080

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=KL198009:857493-859637(+)

Full Sequence      

MLQTTRLASLLALLPLAYAALGPRTEIVLTNEVVAPDGFPRSAVLINGGGKGVQPGPLIQ
GRVGDTFKINVVNKLQDKTMPTSTSIHWHGLLQRGTNWADGPAFVTQCPIVPNEAFEYAF
KASHPGTFWYHSHLSTQYCDGARGPMVVYNPRDPYARFYDVDDSSTIITLEDWYHVPSLQ
VQGVPTPDSTLINGHGRSKDGPKMPLSVINVEHGKRYRIRLVSMVCDPNYRFSIDSHTMF
IIEADADYTQMVEVDSLQIFAGQRYSFILHATQNVGNYWIRANPNVGAQGFDGGINSAIL
RYKGAPCEEPTSIQTNSTRPLLETDLHPLYDPKAPGRPVPGGADVVIDLATAFNLTSALY
TVNNKTFVPPTLPVLLQILSGAHSAQELLPTGSVYTLPRNKVVELTLPGGAIGGPHPIHL
HGHLFSVVRSAGNSTYNFDNPVRRDVVSNGVAGDLVTIRFVTDNPGPWLLHCHIDWHFEL
GFAAVFAEDPQGTKIANPVPGNGVVEAMPCVRKVCFKT

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	34	336	5.5e-146	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	7.11e-89	344	490	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	5.79e-78	35	488	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.
177843	PLN02191	3.09e-69	55	488	52	546	L-ascorbate oxidase
274556	laccase	1.05e-67	41	486	22	517	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	1.34e-67	166	315	1	156	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
AAD30965.1|AA1_1	2.41e-227	1	500	2	501
DAA04507.1|AA1_1|1.10.3.2	2.41e-227	1	500	2	501
AYR00610.1|AA1_1	7.31e-222	8	500	11	500
AIW01083.1|AA1_1	9.31e-222	3	498	5	496
AAD30966.1|AA1_1|1.10.3.2	1.94e-221	7	489	4	488

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GYC_A	1.16e-214	20	500	1	481	Chain A, LACCASE 2 [Trametes versicolor]
5Z1X_A	1.91e-212	20	502	1	479	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]
5NQ8_A	8.68e-212	10	500	12	500	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]
6RHH_A	2.45e-211	19	500	1	481	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]
5MEJ_A	2.54e-211	19	500	1	481	Structural study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. First structure of the series with 3 min total X-ray exposition time. [Steccherinum murashkinskyi],5MHU_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The third structure of the series with total exposition time 63 min. [Steccherinum murashkinskyi],5MHV_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fourth structure of the series with total exposition time 93 min. [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	1.12e-217	17	498	21	508	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	1.73e-213	11	500	12	501	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|Q12718|LAC2_TRAVE	2.45e-213	11	500	12	501	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	1.32e-210	18	489	22	499	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q99044|LAC1_TRAVI	9.05e-209	5	500	2	502	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
0.000247	0.999711	CS pos: 19-20. Pr: 0.9837

TMHMM  Annotations     

There is no transmembrane helices in KDQ27220.1.