CAZyme Information: EHY56454.1

Basic Information

• Species: Exophiala dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala dermatitidis
• CAZyme ID: EHY56454.1
• CAZy Family: GH31
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
751	JH226133|CGC3	82527.95	4.7316

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EdermatitidisNIHUT8656	9356	858893	71	9285

• Gene Location: location=JH226133:564279-566613(-)

Full Sequence      

MAIMSSSRLLLQRLGIFLCLISSVISNTTPRPVPVPVQHDSNFVPDIVLRVDVATIQLNC
QPRLSTLINGTYPAPPIYLEPERTTWIRVYNDAYFNTTMHWHGLSLSTAPYADGTPQASQ
WPIPPGHFFDYELHPSAAEAGTSFYHSHVGFQAITASGPLIVKDASPLPYAYDDEIILKI
GDLYPQDDKTIETELTSIPFRWIGDPSALLVNGQSGTTISQPQTQSTTTNSNSVNSTEAG
SDTSCQPWVMNVLPEKIYRVRLIGATTISLVLFGFEDHDNLTIIETDSAYVSPVQTDHMQ
VDTGQRFSFLLPTKSREELAATNKSTFWIQFETRQDDRVVSAWALLNYTLDASASDPSDS
DSDQYSPPAAPATPSSIPSSSVVSLPNNVTSWMEYTFINPPFAGYDSPPLSSEVTRRVII
STLQLLNTTTQNTLMVSNNASWFDGPPLGPSVHVPYLVEILQNETINGGVPDFDGAIGSN
SNSNSTSSTFPFEGSGFDPLTNTYPARIGEVIEIVWQNAASSPARVFGAHPMHAHGGHYW
DMGSGQGVYSPAVHAEMLRANSVVVDAPDDGENSSTPWSSQQIIVPYPGSRRDTTLLYKY
ASLGTYPGELNGWRVWRVRVTERNVGVWMMHCHILQHIIMGQQTVWLFGTPEEIRQHVEP
VQGSLDGYFNFGGDVVGRTGTGYDGQQEGGEEWHRGNDTVWGNGPRPNGEEAVKGKKMNK
PNGKGRVKNKGEAGWKQGSKDEAIEVMQFFE

Enzyme Prediction     

No EC number prediction in EHY56454.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	62	641	2.9e-75	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	37	655	1	538	L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized.
259941	CuRO_2_AAO_like_2	3.62e-84	174	348	1	161	The second cupredoxin domain of plant Ascorbate oxidase homologs. This family includes plant laccases similar to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couples oxidation of substrates with reduction of dioxygen to water. 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 2 of 3-domain MCOs has lost the ability to bind copper.
259962	CuRO_3_AAO_like_2	1.77e-83	413	649	1	188	The third cupredoxin domain of Ascorbate oxidase homologs. This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which 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 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	1.28e-58	59	641	16	516	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	5.14e-49	59	649	38	547	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL03177.1|AA1	7.65e-159	39	677	22	585
QPC67932.1|AA1	2.04e-156	39	677	22	585
QPC76805.1|AA1	2.28e-155	39	677	22	585
CEI66209.1|AA1	2.28e-155	39	677	22	585
QBZ60051.1|AA1	6.63e-155	39	677	24	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.25e-44	59	650	18	525	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
6KLG_A	5.82e-28	60	647	19	529	Crystal Structure of the Zea Mays laccase 3 [Zea mays],6KLI_A Crystal Structure of the Zea Mays laccase 3 complexed with sinapyl [Zea mays],6KLJ_A Crystal Structure of the Zea Mays laccase 3 complexed with coniferyl [Zea mays]
1HFU_A	1.69e-20	47	322	2	272	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.70e-20	47	322	2	272	Chain A, Laccase [Coprinopsis cinerea]
3FPX_A	2.09e-18	63	311	22	248	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF64|AURL2_GIBZE	6.41e-155	39	677	22	585	Multicopper oxidase aurL2 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=aurL2 PE=2 SV=1
sp|G2QFD0|LMCO1_MYCTT	6.54e-136	39	677	25	619	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|Q0D1P3|TERE_ASPTN	3.83e-116	99	677	1	515	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P37064|ASO_CUCPM	6.45e-44	59	650	18	525	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1
sp|P24792|ASO_CUCMA	3.27e-43	59	650	48	555	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999765	CS pos: 26-27. Pr: 0.9806

TMHMM  Annotations     

There is no transmembrane helices in EHY56454.1.