CAZyme Information: AO090102000546-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090102000546-T-p1
• CAZy Family: GH76
• CAZyme Description: Ortholog(s) have hydroquinone:oxygen oxidoreductase activity and role in melanin biosynthetic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593	Chr4_A_oryzae_RIB40|CGC19	66402.30	4.5127

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr4_A_oryzae_RIB40:3034220-3036333(+)

Full Sequence      

MAPLKTLVALLSANVLTSVLAELVKFEVDLTWAKGSPDGNLRDMIFVNDQFPAPQLTLNQ
YDDVEFTVNNHMPFNATVHFHGIVQLNTPWSDGVPGLTQKPILPGGTFTYRWTATEYGTY
WYHAHARSLMADGLYGAIWINPAPEIPQPFHLISDDEKDIEAMQKAESDPKLVILSDWSH
YTSEEYQKIMEESGVDLFCVDSILINGRGRVHCPGADFINSLQTDYLKASIDNLPLTDKG
CYPKIYKTQGSFPRNDSKVPPGLESGCVATAGTHEIIEVDPEDGWVSMKFISAAWLKAVI
ASIDEHPMWIYEVDGHYIEPQLAHTMVMYNGERYSAMIKLDKTPKDYTIRIPDTNADQII
AGFATMRYKGSDQTGESEPYVDYGGLNTTADVIALNESILVPYPSIQLPTAADQLINLTF
GRRESAYQWTLEGKQLYDVMANYDDPILYNLTAKENLGDKVTVQTQNGTWVDVLLQVGIM
PNTPPIQAPHIIHKHSNKAFIVGEGDGFFNWTSVAEAATERPELFEFERPRLRDTFMVLG
LLGPRWMVIRYQVVNPGPFLIHCHIETHLANGMGVALLDGVDEWPEVPPEYAL

Enzyme Prediction     

No EC number prediction in AO090102000546-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	42	573	1.6e-76	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	3.16e-79	413	580	1	164	The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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 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.
259944	CuRO_2_Abr2_like	3.54e-69	171	369	1	138	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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.
259919	CuRO_1_Abr2_like	4.49e-60	26	141	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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.
274555	ascorbase	1.17e-55	25	590	5	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.
215324	PLN02604	4.60e-52	1	588	2	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD90476.1|AA1	0.0	1	593	1	593
QMW43549.1|AA1	0.0	1	593	1	593
QMW31491.1|AA1	0.0	1	593	1	593
UDD60426.1|AA1	0.0	1	593	1	593
QBK15064.1|AA1	7.39e-214	21	591	20	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	6.58e-44	25	588	7	532	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]
5LM8_A	1.92e-39	25	584	25	509	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.95e-39	25	584	26	510	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.67e-39	25	584	53	537	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
4JHU_A	9.90e-38	29	589	7	476	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9RBR0|ABR2_ASPFU	4.38e-203	21	587	17	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	3.19e-202	7	591	7	600	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	7.87e-195	21	592	21	593	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	3.38e-193	10	591	7	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	8.78e-183	21	593	20	607	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000247	0.999709	CS pos: 21-22. Pr: 0.9730

TMHMM  Annotations     

There is no transmembrane helices in AO090102000546-T-p1.