CAZyme Information: AN7389-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN7389-T-p1
• CAZy Family: GH76
• CAZyme Description: Putative laccase related protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
580	ChrIV_A_nidulans_FGSC_A4|CGC11	64825.20	5.0598

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnidulansFGSCA4	10988	227321	276	10712

• Gene Location: location=ChrIV_A_nidulans_FGSC_A4:107863-109659(+)

Full Sequence      

MHAIYGSLALLLGLAVSSRASTVRHDHSFQPDHILRVTADIYNEACSERYSVLVNGSSPG
PELRLREGEVSWIRVYNDMTDANTTIHWHGLTAFTAPFSDGSPAASQWPIPPGHFFDYEV
KPEPGSAGSYFYHSHVDFQSVTAKGPLIVDSSEPAPYHYDEERTVMISDYFSEPDDEIVD
GLVSTNFTWSGETEAILVNGQSRPATNATGACKLAAISVEAGKTYRLRFIGATALSFVSL
AIESHHMHIIEADGHYTKPLETDFLQIGSGQRYSVLLTAKGEDELKALDRRQFYLQITTL
ERPAVLTSFAVLDYTSDAAPDLTTVPSPPPLPVATTVQGWLDYELEPAHPNEDFPTLDEV
TRRIVIDVHQNVSDRTIWLQNGYDWVESFPKSPYLVDIYQDRLDLDASYHRALTRGNGFD
NITRTFPARVGEVLEIVWQNRGTVENGGVDAHPFHAHGRHFYDIGGGDGLYNATANEIRL
RGTHPIQRDTSVLYRYRSKTSQLVPSGWRAWRIRVTNPGVWMYHCHVLQHMIMGMQTVFT
FGDREDILAKTGQVDDGYLTYGGSAYGNGTWDPMVQDFDV

Enzyme Prediction     

No EC number prediction in AN7389-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	47	536	2.6e-91	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	23	548	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.
259962	CuRO_3_AAO_like_2	6.14e-95	359	542	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	1.06e-89	46	542	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.
177843	PLN02191	2.06e-77	46	562	39	562	L-ascorbate oxidase
215324	PLN02604	4.06e-76	46	542	40	547	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS19632.1|AA1	0.0	1	579	1	577
QMW38925.1|AA1	1.88e-305	1	578	8	586
QMW26845.1|AA1	1.88e-305	1	578	8	586
UDD54641.1|AA1	1.88e-305	1	578	8	586
QRD81157.1|AA1	1.95e-305	1	578	9	587

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.05e-62	46	565	19	542	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	6.50e-40	37	539	10	528	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	6.26e-35	49	539	23	466	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	6.34e-35	49	539	23	466	Chain A, Laccase [Coprinopsis cinerea]
1ZPU_A	6.66e-35	44	538	17	476	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	4.99e-175	7	578	7	630	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|I1RF64|AURL2_GIBZE	1.22e-163	11	578	8	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|Q0D1P3|TERE_ASPTN	1.85e-128	86	576	1	524	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P24792|ASO_CUCMA	9.35e-63	10	565	20	572	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|P37064|ASO_CUCPM	5.41e-62	46	565	19	542	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
0.000218	0.999733	CS pos: 20-21. Pr: 0.9565

TMHMM  Annotations     

There is no transmembrane helices in AN7389-T-p1.