CAZyme Information: KIW16047.1

Basic Information

• Species: Exophiala spinifera
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
• CAZyme ID: KIW16047.1
• CAZy Family: GH32
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
596		66627.60	5.8195

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

• Gene Location: location=KN847495:2484634-2486735(+)

Full Sequence      

MLLFYRLLPVLFWIQAICAIPPSPEASPDYVLVATAKNLTVNCQTRYSVVLNGTSPGPTI
HMKENFTTWVRVYNRIPDENLTVHWHGLSLRTSPFSDGTPQVSQWPIAPNAFFDYSVTPA
VGDAGTYFYHSHAGFQSLTAQGLIIVEDQDDVPYDYDDDESFFIQDYFPKNDSTIVSGLI
ANPFKWSGEPEAISINGFSGNSSFSNATDATCTPYVINVEPGKTYRWRFIGATALSFVTL
GIEGHDHLTVIEADGEYTKPWSTDHLQLGSGQRFSVLFKAKTQAELDAANKTSFWLRYEN
RDRPTNVSGYALLQYNVSGSTRPSLLPATPPITLPKNVTTWAEYALEALRPQEAFPKLSE
VTRTVYITMQQQIRVGSYVNKTINGTLQWAQNNLIWQTAQRESNNSLPYLVQVYLTGQTP
NYTAAVENGGWDPYSNAFPALPGEVLDIVWQSNSGPTGGWDFHPMHAHGKHYFDLGSGNG
TYNATANEMRFANYTPARRDTTIMHRYAVSGVPETTAGWRAWRIRVTDDDVGAWMMHCHV
LQHMVMGMQTVWVFGNASSILAKFPTQPYVNGYLKFGGDAYGNSTYDPLENIYSKI

Enzyme Prediction     

No EC number prediction in KIW16047.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	44	549	8.3e-87	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	28	561	9	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.
259962	CuRO_3_AAO_like_2	1.31e-99	360	555	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.
259941	CuRO_2_AAO_like_2	3.10e-90	162	315	5	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.
274555	ascorbase	1.13e-76	42	567	16	534	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	3.19e-66	42	555	38	547	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCT67688.1|AA1	7.46e-265	8	593	9	596
QKD49363.1|AA1	2.85e-262	8	593	9	596
QBZ60051.1|AA1	5.02e-261	28	589	30	598
UPL03177.1|AA1	2.82e-257	28	593	28	596
QGI63709.1|AA1	1.97e-256	8	593	9	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	7.37e-57	42	572	18	539	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	3.75e-39	30	568	6	544	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	1.54e-37	32	565	9	479	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.56e-37	32	565	9	479	Chain A, Laccase [Coprinopsis cinerea]
1V10_A	7.44e-28	46	551	43	486	Chain A, Laccase [Rigidoporus microporus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF64|AURL2_GIBZE	1.18e-254	28	593	28	596	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	6.07e-164	28	588	31	625	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	1.69e-142	83	589	1	522	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|M4DUF2|ASO_BRARP	2.01e-56	11	567	3	553	L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1
sp|P37064|ASO_CUCPM	3.79e-56	42	572	18	539	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000217	0.999759	CS pos: 19-20. Pr: 0.9658

TMHMM  Annotations     

There is no transmembrane helices in KIW16047.1.