CAZyme Information: EEU36078.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU36078.1
• CAZy Family: CBM21
• CAZyme Description: Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:C7ZIS7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
582		64912.32	6.5046

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698931:202039-204007(+)

Full Sequence      

MVAHDEEHDGLLDEFELQDEDPKTRPNSSHRTVRRWARFVRRRVWCLIAVVVAIALLCIL
GAAFSSRGTLKALKGPEEGGRLGIRLHPEEHASRPPATLSFNWTITAGLRSPDGVQKRVY
LVNDEFPGPTIEARSGDRLVLQIRNSLEEEGVSLHWHGLRMKHQNLMDADGLWGGLIVHS
PREENPPPEDYLVMVSDWFHRNQTEILAWYADASSRGNEPVPDSLLVNGRGRFNCSMAVP
ARPVVCSQIAAHELAPLLNPSREKAMRLRFVNTGSVAGFSVQIDGATMHPVRVDGGFSVH
AEASESIGIIYPGERVDVDVKWIKDYPGDHWLSIDLDSENFGYPNPALNPTQIFPIIGET
SRESKHREQHAPSNTRALDLQNVTAATRVSDIPPRAKETFVFYAKTEKLAHLDYQPVGFI
NHTSWKPQSRPLLSQNRTAWDENQLVPFIGLSSTEPTRVDIVINNLDDGAHPFHLHGHSF
YVLSSYRDEGRGGWGSYNPYSGDQPPNGLNLDFPLRKDTVSVPRRGHVVLALVADNPGIW
ILHCHMLVHMARGMAMALHVGDVQDVEHVISADLMAGELCGR

Enzyme Prediction     

No EC number prediction in EEU36078.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	163	555	1.4e-44	0.7374301675977654

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259977	CuRO_3_MCO_like_4	1.30e-63	400	560	1	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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	4.98e-49	101	554	4	517	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	1.45e-45	101	561	27	547	oxidoreductase
177843	PLN02191	1.87e-42	97	565	22	556	L-ascorbate oxidase
259868	CuRO_2_LCC_like	1.40e-40	191	354	1	150	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to 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 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
UPK99837.1|AA1	0.0	1	582	1	622
QKD61545.1|AA1	1.36e-277	1	580	1	616
AVI02163.1|AA1	1.11e-276	1	580	1	616
QPC62885.1|AA1	1.67e-264	1	562	1	602
QPC80252.1|AA1	3.06e-262	1	562	1	602

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	6.08e-35	101	577	6	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]
3V9E_A	7.31e-33	102	556	76	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.80e-32	102	556	76	538	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
6F5K_A	2.43e-30	102	571	45	529	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
5LM8_A	2.01e-27	113	555	38	499	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	2.25e-51	96	553	59	553	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.40e-49	96	553	59	553	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|Q55P57|LAC1_CRYNB	6.49e-48	96	553	59	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	2.83e-41	75	558	47	549	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q8LPL3|ASO_ARATH	3.43e-37	93	561	18	544	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999983	0.000023

TMHMM  Annotations     

Start	End
44	66