CAZyme Information: QRD04919.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRD04919.1
• CAZy Family: GH72
• CAZyme Description: L-ascorbate oxidase [Source:UniProtKB/TrEMBL;Acc:A0A7U2FGM8]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
722		79542.97	6.0809

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069039:1185351-1187566(-)

Full Sequence      

MRSGGCVKQPLEIISKANVSRQLHRRQLGRTAESTAESLRGTTEADPDIGDTNSQNAQHG
QSDDLGLQQFEPFAKTAFSFPGHPNGDWSQYSQAVLPALAISVSFRICCASDRIQGSGTM
RNFFAAGLLLTAAHLVAGHNAPNPPAPQSPSPSQARQNGEPQRPHGKDFVPDHYLSVTFE
NHTVACQHHMSALVNHTSPGPAIRIPAGKTSWIRVCNDMEEYNTTMHWHGLTQRTAPFSD
GSPVSQWPIAPHRCFDYEIHPEPEDAGTYFYHSHVGFQAISAAGALIVEDVGPPPFHYDE
ERIVLIQDYFNKSDETIEKGLRSVPFVWSGETNAVLLNGVGVAIGEKAGQGNCKLPVIDV
EPGKTYRMRFVGATALSLVALGIEGHSRMDVIVADGSYTQPHTVDHMQLSSGQRFDAIMC
TKTVEELGNQTDYIIQFETKDRPAVYTGFGVLRYPSTSPKITTAPAVKPLTLSNATYDFL
EYALEPLVPNDFPTASEVTRRVHVTNAQIRQSATIWQLDGLNWTEDTAANSPPYLVDIYK
NGPVAMPNYTAALANGGWDPYSLTWPAKLGEVIEIILENTGSLVDNNGGYDYHPFHLHGA
HFYDCGSGNGTYDPIENEKKLANYHPVKRDTTNLYRYQTKGTAGKAMGWRAWRIRVQNPG
CWMLHCHVLQHMIMGMQSVWIMGDYEEIATIPYSGAEGYLEFGGTAYGGQDITPVVNHNW
ND

Enzyme Prediction     

No EC number prediction in QRD04919.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	190	677	1.8e-83	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	165	688	3	537	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	7.59e-96	497	683	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.
259941	CuRO_2_AAO_like_2	2.05e-80	300	454	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	6.43e-79	186	692	17	532	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	3.08e-65	177	694	31	557	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD04919.1|AA1	0.0	1	722	1	722
CAE7187842.1|AA1	2.31e-315	122	720	5	599
SMR54647.1|AA1	4.01e-255	124	722	9	614
SMR56477.1|AA1	4.01e-255	124	722	9	614
SMY25673.1|AA1	4.01e-255	124	722	9	614

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	8.17e-56	186	706	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]
1HFU_A	1.08e-33	200	679	33	465	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.09e-33	200	679	33	465	Chain A, Laccase [Coprinopsis cinerea]
5Z1X_A	7.87e-33	191	692	24	475	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]
6KLG_A	8.08e-33	173	682	5	530	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	2.34e-200	165	722	25	633	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	1.08e-177	165	722	22	599	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	1.94e-142	226	721	1	528	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P14133|ASO_CUCSA	3.32e-56	194	692	62	568	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|P37064|ASO_CUCPM	4.20e-55	186	706	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000058	0.000000

TMHMM  Annotations     

There is no transmembrane helices in QRD04919.1.