CAZyme Information: KID67100.1

Basic Information

• Species: Metarhizium anisopliae
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
• CAZyme ID: KID67100.1
• CAZy Family: GH36
• CAZyme Description: L-ascorbate oxidase, fungi

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
601	AZNF01000004|CGC4	67531.74	4.9476

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549	10891	1276135	0	10891

• Gene Location: location=AZNF01000004:398483-400351(+)

Full Sequence      

MLWLRRTVTTLALAAVPVLSLQAHSHDDSFTPDIVLSVTRQNISIGGMYRETTLVNNSLP
GPTLRIPERKTIWIRVYNDIENDNVTIHWHGLAQAAYPFSDGAPLASQWPIPPKHFFDYE
LKAESGTAGTYYYHSHVGFQASTATGALIVEDPAGAPYTTDGERLVFLQEYWSQSDTQIK
NGLESIPLRWSGEPKGWLINGKSISNYRAVDPSTRALSVIDVEPGKTYRFRFVGATALSL
ALLGFEKHGNLEIIEADGEYTQPYPVDLLQIGSGQRYSALFHAKSCQDLREDGQLDYYIQ
LESRDRNRVVTNYAVLRYENACNMTSQPVATNKNPETPPLNLPPTIDGYLDYALQPLEPN
NFPTAEEVTRRVILNVQVVMNQYFIWTINNYTWSEDADSLPATVPQTPYLVSLYQNQSAY
LPNYEDAVANGGIDPKTGTYPAKIGEVLEIVFQQFGGKSVSGLGGGMLDTHPWHGHGIHH
YDVGGGRGAWDPDTVEEKLEGKQPVLRDTTMLYRYERFVEADEKMGWRVWRIRVEQPGVW
MVHCHTLQHMIQGMQTVWVNGDAEDILKVGKPDVEGYLLYGGNVYGNESHTPQVVHFDEM
D

Enzyme Prediction     

No EC number prediction in KID67100.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	555	6.5e-90	0.9888268156424581

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	26	567	3	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.
274555	ascorbase	7.58e-89	55	571	25	530	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	6.67e-87	367	561	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	9.62e-76	55	573	47	556	L-ascorbate oxidase
259941	CuRO_2_AAO_like_2	3.02e-70	162	318	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
QLI66568.1|AA1	0.0	1	601	1	601
QPG97523.1|AA1	0.0	22	599	19	602
UNI15593.1|AA1	1.96e-278	20	601	20	650
UKZ68153.1|AA1	4.65e-270	80	601	1	526
QLI74016.1|AA1	4.85e-270	15	601	14	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	3.16e-63	55	571	27	530	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]
1HFU_A	6.68e-41	36	575	9	482	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	6.78e-41	36	575	9	482	Chain A, Laccase [Coprinopsis cinerea]
6KLG_A	4.67e-36	55	572	27	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]
1KYA_A	5.25e-33	36	574	8	474	Chain A, Laccase [Trametes versicolor],1KYA_B Chain B, Laccase [Trametes versicolor],1KYA_C Chain C, Laccase [Trametes versicolor],1KYA_D Chain D, Laccase [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	9.41e-173	26	597	25	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	7.07e-163	26	594	22	593	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	4.01e-139	87	596	1	525	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|Q8LPL3|ASO_ARATH	3.48e-63	55	579	47	558	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1
sp|P37064|ASO_CUCPM	1.62e-62	55	571	27	530	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
0.002012	0.997953	CS pos: 25-26. Pr: 0.6615

TMHMM  Annotations     

There is no transmembrane helices in KID67100.1.