CAZyme Information: PGTG_18049-t26_1-p1

Basic Information

• Species: Puccinia graminis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia graminis
• CAZyme ID: PGTG_18049-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613		68648.76	9.6386

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PgraminisCRL75-36-700-3	16309	418459	509	15800

• Gene Location: location=DS178353:88200-90620(-)

Full Sequence      

MALIPRFSFILIVLFSLQLAFLFQTSQSQKNSDLNSRAYPNFGTNQFSRNVVLEVSEQVI
SADCTKRPSVVINGTFPGPELRFKPGEKVKIRVFNLLKDHTVTIHMHGLSQHFSPFSDGV
AQVSQFAIPAGGYFDYIFLLEPNSAGTFIYHAHVGFHLMTCHGALIVEDAHKPPFKYDEE
RVLLFADYYHNLEQQIVKDINSVPFKWLGEPQSMVVNGNALGSCNSTSPFGCSTDCHHHR
LVVKPGKTYRVRVIGITVLTYLYFGIEDHQQLSVIEVDSGYVRPASTKHIQLHSGQRYSF
LLKTKTRKELKKLGSKRDFWGRLETRWRPLRDQGAFVLHYEDDPTPASTGKSATTKPHDL
SRSPLPDLKKFQKIVPLPNEGNKWLTETFEPLDPKEVAPTAAEVTRRVFIQGQQLKAADG
RVNWFVNGQRYIETQPKVPFLVSAYTHKLKPDYEAAAKNNGFDAKLGAYPIKLNDVVEFV
IVNQASTAGVTEAHPWHLHGQAFFVVAHGTGPFTEAKLAAVEARSKKRHIRRDTEIIFST
KLGASYTNTTVPTGTVTGWMVLRMKAETAGAFLMHCHTQPHAAMGMGAVILIGMEHLPPL
PPAYLNKFTLPTS

Enzyme Prediction     

No EC number prediction in PGTG_18049-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	65	586	1.7e-82	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	1.55e-159	46	593	6	532	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	1.10e-89	54	605	7	536	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	2.57e-83	179	340	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.
215324	PLN02604	6.30e-74	54	601	30	555	oxidoreductase
177843	PLN02191	7.23e-73	54	601	29	555	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL03177.1|AA1	2.70e-113	47	608	26	567
CCT67688.1|AA1	1.46e-105	47	593	26	558
QKD49363.1|AA1	1.13e-104	47	593	26	558
QMW38925.1|AA1	1.22e-103	47	593	36	550
QMW26845.1|AA1	1.22e-103	47	593	36	550

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	5.50e-66	54	601	9	532	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]
1GYC_A	6.36e-29	53	589	8	466	Chain A, LACCASE 2 [Trametes versicolor]
1ZPU_A	8.70e-29	67	591	22	478	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]
3PXL_A	1.15e-28	53	590	8	467	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]
6KLG_A	1.32e-28	55	592	10	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	5.86e-112	46	593	28	594	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	2.26e-104	47	593	26	558	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	8.07e-74	104	593	1	489	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P24792|ASO_CUCMA	9.67e-66	54	601	39	562	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|P37064|ASO_CUCPM	2.83e-65	54	601	9	532	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
0.000232	0.999739	CS pos: 28-29. Pr: 0.9755

TMHMM  Annotations     

There is no transmembrane helices in PGTG_18049-t26_1-p1.