CAZyme Information: POW01892.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW01892.1
• CAZy Family: GH10
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
637	PKSL01000151|CGC1	71260.52	9.3059

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93-210	15090	N/A	0	15090

• Gene Location: location=PKSL01000151:92976-95551(+)

Full Sequence      

MVVTAMISLTFTRLFGFFLFLALRHINLADASKVSSSQAPWAPTTVLVVSRTNISADCTI
RPSVTINGTFPAPELRFKAGQKLWIRVINELEDETTTIHFHGLAQFGSPFADGTVKLSQF
PIAPRGGYFDYEFQLPDDSAGTYIYHAHHRFQAITAYGSFIIEEKDVPPPYKYDEELTLM
FGDYYHATDKQIVTGLASTPIKFLGEPQSLAVNGQALGSCNSTSLFGCTKNCHPHVVHVK
PGKTYRVRTIGITALTFLYFSIESHSKLTLIEVDGGYIKPTSTPYMELGSGQRYSFLLKT
KTLEQLQGKHGQLDFYGRVESRWREKRDMGSFILRYDLGSSASNPTHSAQKSATVPSPTR
QSYLSTLITDPTELDKIVPLPNEDQEWVSCRFRPLRIKKEAPTAAQVNRRIFISSQQKKA
PDGSVNWFVNNLTYVEQKPKVPLLVRAYTDGLRPDYEAAFANNGYDAKLDAYPIKLGEVI
EFIIVNVASTVNVAEVHPWHLHGQKFFVIGQGYGEFTEDSYKKINKDNHLKNKRSIERDT
QVVFAGKNNKLFKGPMPSGSHVGWLVIRLVANTPGAFLVHCHLQVHAIMGMSLVMLVAIE
NLPPLPQNFLKSYTSPGGSRLKEPISYFDSVKKLQSS

Enzyme Prediction     

No EC number prediction in POW01892.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	59	591	7.4e-87	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	2.95e-157	43	597	9	531	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	1.09e-94	55	611	14	537	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.
259941	CuRO_2_AAO_like_2	1.31e-87	175	336	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.
177843	PLN02191	4.46e-80	55	610	36	559	L-ascorbate oxidase
215324	PLN02604	5.25e-76	55	606	37	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDS68174.1|AA1	4.34e-107	32	590	24	547
UPL03177.1|AA1	2.01e-105	41	631	26	600
QBZ60051.1|AA1	1.53e-101	41	618	28	587
QGI63709.1|AA1	2.67e-101	31	625	16	577
QGI80980.1|AA1	2.67e-101	31	625	16	577

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.15e-71	66	610	27	536	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]
1ZPU_A	2.97e-36	61	595	22	477	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
1GYC_A	2.18e-35	43	594	4	466	Chain A, LACCASE 2 [Trametes versicolor]
6KLG_A	1.82e-34	48	611	9	549	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]
3PXL_A	4.57e-34	43	607	4	482	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	5.11e-101	41	633	29	636	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	1.82e-98	18	619	3	582	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|Q40588|ASO_TOBAC	1.04e-71	66	610	54	563	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1
sp|P24792|ASO_CUCMA	2.89e-71	57	610	48	566	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|P37064|ASO_CUCPM	5.89e-71	66	610	27	536	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
0.000378	0.999612	CS pos: 31-32. Pr: 0.9553

TMHMM  Annotations     

There is no transmembrane helices in POW01892.1.