CAZyme Information: mRNA_M_BR32_EuGene_00102141-p1

Basic Information

• Species: Pyricularia oryzae
• Lineage: Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae
• CAZyme ID: mRNA_M_BR32_EuGene_00102141-p1
• CAZy Family: GH32
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
603		67206.97	5.7972

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PoryzaeBR32	14781	N/A	432	14349

• Gene Location: location=BR32_scaffold00013:886132-888044(-)

Full Sequence      

MPSMLLTWLLLLLGSCLAAEFRVHDKTFKPDYVLVATAQNITINCQTRYSIVFNGTSPGP
LLTFHENQTTWVRVYNRIKDQNVTVHWHGLSQRTAPFSDGTPLVSQWPVAPDNFFDYEIR
PDIGSAGTYFYHSHVEFQAVTAHGALIVEDAVKPPYEYDEDVVVGLGEYYPKTDRQILDG
LLAKPFRWSGEPEAILFAGRSGNKSFTEASHDSCKPDLIKVQPDKTYRVRFIGGTAMSLV
VMAFEGHDMTIIEADGSYTKPVKTDRMQVGSGQRYSVLLRTKSVQEVASTNKTSYWIQYE
TRGRPTNVTGWALLQYEMPGQPEAMLPATLPSKPVATIPDDPSTWMEFTLQPLQDSVRER
FPKLSEVTRTIYIDVKQVVVDGGVVNGTVKGSIEWAQNSLVWQEDSQAAKNRPPVLVGIL
TTGMSPSIEAALANQNWDPTTQTFPAAVGETLDIVWQGNSGELGGWDVHPMHAHGTHFWD
LGSGNGTYDAPAVDAKYYADGTYVPAVRDTTMLYRYAAKGEKNHTAGWRAWRVRVTEDDI
GAWVMHCHVLQHMMMGMQTVWVLGTAAEILQKFPTSPYVNGYLTFGGDAYGNATFDPLVL
QHF

Enzyme Prediction     

No EC number prediction in mRNA_M_BR32_EuGene_00102141-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	46	558	3.2e-90	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	23	570	2	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	7.54e-90	160	316	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.
274555	ascorbase	3.56e-76	44	576	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.
259962	CuRO_3_AAO_like_2	1.54e-75	366	564	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.
177843	PLN02191	6.67e-71	44	564	38	547	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ60051.1|AA1	0.0	1	603	1	603
UPL03177.1|AA1	2.33e-248	19	603	17	597
CEF74607.1|AA1	2.35e-246	19	603	17	597
CZS77882.1|AA1	2.35e-246	19	603	17	597
QPC76805.1|AA1	4.72e-246	19	603	17	597

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	3.30e-61	44	581	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	1.03e-36	32	577	6	548	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]
5Z1X_A	2.08e-35	47	564	21	466	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
3KW7_A	6.94e-31	30	565	4	474	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
3X1B_A	2.06e-30	47	580	42	500	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF64|AURL2_GIBZE	4.17e-247	19	603	17	597	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	2.02e-155	4	603	1	631	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	1.07e-139	85	603	1	527	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P14133|ASO_CUCSA	3.46e-62	44	564	53	560	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|P24792|ASO_CUCMA	5.70e-62	44	581	48	569	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
0.000229	0.999760	CS pos: 18-19. Pr: 0.9788

TMHMM  Annotations     

There is no transmembrane helices in mRNA_M_BR32_EuGene_00102141-p1.