CAZyme Information: HMPREF1541_08833-t46_1-p1

Basic Information

• Species: Cyphellophora europaea
• Lineage: Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
• CAZyme ID: HMPREF1541_08833-t46_1-p1
• CAZy Family: GT15
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
577		63435.28	4.6974

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466	11153	1220924	59	11094

• Gene Location: location=KB822725:999205-1000988(+)

Full Sequence      

MACRSRTSAVINGTSPGPPLRITPDQTTWVRVYNDMENENLTMHWHGLSQSIAPFSDGTP
LVSQWPIPPQHFFDYELHPNKTESGTYFYHSHVGFQTVSAIGPLIIEDVDGCPYEYDEER
IIQITEYFNKSDDAIVEGLLVSPFVWSGEAMAILVNGNSAEAKSEATEDDAGLEGQCGPE
LIRVEPGKTYRFRNIAAAALSAMTYGIEDHDNLTIIEADGRYTKPATTDHLELGSGMRFD
YLLTTKTESELTTLNKHNFWIQIEIRDRPVNYTSYACLSYDGQGCGAVPSQNSPIITLPH
GTSWLEYTLEPLSPNNFPTLSDVTRQVTIVTEQVNISGALVWHFNGQRLDVDHPRPTPYL
VDIYRQGAAAIPSPALTATNNSFSSAFNAYAASLGDVIDIVWLQRPNIPAGGFDSHPLHA
HGGHFYDLGSGPGSYDAEANERRFQHYTPVLRDTTFLYRYTTDADTAEGVDQGWRAWRVR
VEDPGVWLLHCHTLQHMIMGMQTVWVMGDAEEITRGDGLELQGYLDYGGSAYGSDGDGGG
GGGSGGGEGSSGKKAPVVKHHWDGVGKSQNEHGKVKL

Enzyme Prediction     

No EC number prediction in HMPREF1541_08833-t46_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	5	502	3.8e-89	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	2	513	23	537	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.
274555	ascorbase	2.01e-80	3	508	17	524	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.
259962	CuRO_3_AAO_like_2	5.86e-80	323	508	2	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.
177843	PLN02191	2.71e-74	3	508	39	547	L-ascorbate oxidase
259941	CuRO_2_AAO_like_2	2.01e-73	118	280	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX59572.1|AA1	8.77e-193	1	534	45	613
QGA14799.1|AA1	7.33e-191	2	534	47	610
SMR54647.1|AA1	7.33e-190	1	537	73	604
SMR56477.1|AA1	7.33e-190	1	537	73	604
SMY25673.1|AA1	7.33e-190	1	537	73	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.93e-59	3	508	19	524	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	3.35e-40	3	507	19	530	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]
3X1B_A	1.35e-32	5	504	42	488	Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus],3X1B_B Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus]
1HFU_A	2.30e-31	5	504	22	465	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.33e-31	5	504	22	465	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF64|AURL2_GIBZE	4.12e-169	3	537	43	589	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|Q0D1P3|TERE_ASPTN	2.14e-168	43	563	1	528	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|G2QFD0|LMCO1_MYCTT	1.98e-165	2	567	45	636	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|P14133|ASO_CUCSA	3.82e-63	11	508	62	560	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|P37064|ASO_CUCPM	9.91e-59	3	508	19	524	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000033	0.000017

TMHMM  Annotations     

There is no transmembrane helices in HMPREF1541_08833-t46_1-p1.