CAZyme Information: EPrPVT00000024114-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000024114-p1
• CAZy Family: GT71
• CAZyme Description: Multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
511		56646.12	5.1261

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

• Gene Location: location=PvexDAOMBR484_SC1769:693-2245(+)

Full Sequence      

MFRPSHPCSALALLLLLQSASVCIARVVTYDWEISQMQAAFDGLTTTVYSINGRPGHEAL
IEATLGDRVEVRVVNALSETTCLHWHGLKQLGTQEMDGVSGIMQTAVYRFTPDKPGSFWW
HSHDSTQYAFELCGPLVVHSPPNQLAVWERQVTAEYTLQLTDWYHALPNGVPMWDSVLIN
YRGRFDCSVASANNLTCSEDQPLSRIRFEQGKTYRLRLINEGALAPLLFSIDGHEFSVVA
VDAEPVKPSKLINSLLINVGQRYDIIVKAKKSHNPAQVLCRHAKGLPGNFWIRATSQYSR
PWTGWPVDTAAPDGFNQYGLAILDYDVHARSEPTTATWDTISILDELAFAPVVPSTLPVT
PDQRVVVEFDLMQVVPNSPPLGYVSINNGNFSTLKIPDEPSLFSIANGLHTSDLLASANA
FKLDYGKYIEVVLVNDMNEQHPFHMHTRAPWVVASGQVSRDAIFANTITDYNLDGPVLRD
VYTVPPCNTDADGNCVDIGYLVLRFDTDNAG

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	45	511	9.9e-67	0.9301675977653632

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	5.09e-52	27	511	1	501	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.
215324	PLN02604	1.74e-49	22	511	19	524	oxidoreductase
177843	PLN02191	2.41e-47	25	511	21	524	L-ascorbate oxidase
259868	CuRO_2_LCC_like	4.63e-37	156	325	1	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) 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 compounds 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 2 of 3-domain MCOs has lost the ability to bind copper.
259926	CuRO_1_Diphenol_Ox	5.65e-36	30	139	3	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26495.1|AA1	2.24e-174	15	511	11	517
AFY09915.1|AA1	1.65e-169	9	511	5	521
AFY09916.1|AA1	6.34e-164	9	511	7	501
UIZ26488.1|AA1	5.09e-156	25	511	14	493
AIG56347.1|AA1_2	4.64e-66	26	511	40	514

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	2.29e-47	31	511	7	450	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
5LDU_A	1.42e-44	31	511	7	447	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
3FPX_A	1.96e-44	31	511	7	447	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]
1HFU_A	2.10e-44	42	511	19	446	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.13e-44	42	511	19	446	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q99056|LAC5_TRAVI	4.39e-44	31	511	30	475	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|Q12729|LAC1_PLEOS	2.26e-43	60	511	67	476	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q99044|LAC1_TRAVI	2.70e-43	31	511	28	468	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1
sp|Q12717|LAC5_TRAVE	3.02e-43	31	511	30	475	Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1
sp|Q12739|LAC2_PLEOS	8.64e-43	60	511	69	478	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000308	0.999654	CS pos: 25-26. Pr: 0.9391

TMHMM  Annotations     

There is no transmembrane helices in EPrPVT00000024114-p1.