CAZyme Information: PTTG_02125-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_02125-t43_1-p1
• CAZy Family: GH10
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
611		68329.51	8.2483

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02000022.1:710448-712849(+)

Full Sequence      

MAPLRSFSFLSVILFSLQLFLLLQSSYSRATSQLSSGPRPSFGPHEFSRKVVLEVTEKVI
AADCTKRPSAVVNGTFPGPELRFKAGDKIKVTVINLLKEDNITIHFHGLSTVGAPFSDGT
EKIAQYAIPPAGGKFDYIFLLDSPGTYIYHAHVGFKLMTCHGAFIVEDAHKPPFKYDEER
VLLFADYYHNLEKQIELGVTSVPFQWLGEPQSMVVNGNALGKCNANSPFGCTTDCRHHRL
VVKPGMTYRVRVIGITVLTYLYIGIEDHEDLSVIEVDSGYVRPASTKHIQLHSGQRYSFL
LKTKSREELKKLGSKRDFWGRIETRWRPIRDQGAFVLHYEDEASTSIGPSVTNKPLDLSL
SPLPEPKEFKKIVDLPNEGNTWLADTFEPLDPKEVAPTAAEVTRRILIQGQQLKMPDGHI
YWFVNGEKYVETQPKVPFLVRAYTSKLKPDYKAAEENNGFDKKLGAYPIKFNDVVEIVIV
NQASSAGTSEIHPWHLHGQEFYVVAHGTGEFTKAKLAEAEAHPKRHIRRDTEIIFASQRG
ASYTGTTVTPGMVTGWMVLRMKARTPGAFLMHCHTQPHVFMGMGVVIVVGIEDLPPLPPG
VLKDYVKPTEP

Enzyme Prediction     

No EC number prediction in PTTG_02125-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	65	583	1.5e-81	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	5.49e-161	45	593	5	535	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	1.63e-104	54	603	7	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.
215324	PLN02604	5.86e-87	49	602	25	559	oxidoreductase
177843	PLN02191	6.25e-87	54	598	29	555	L-ascorbate oxidase
259941	CuRO_2_AAO_like_2	2.79e-84	178	339	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
UPL03177.1|AA1	6.79e-106	52	590	31	558
BCS19632.1|AA1	6.20e-104	47	590	29	540
QMW38925.1|AA1	3.79e-101	52	590	41	550
QMW26845.1|AA1	3.79e-101	52	590	41	550
UDD54641.1|AA1	3.79e-101	52	590	41	550

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	4.28e-74	54	598	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]
1ZPU_A	1.72e-36	67	593	22	486	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]
5LM8_A	4.35e-32	49	588	24	503	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.39e-32	49	588	25	504	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	7.43e-32	49	588	52	531	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	5.53e-108	52	605	34	610	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	1.62e-99	47	590	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|P24792|ASO_CUCMA	7.23e-76	54	598	39	562	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|P37064|ASO_CUCPM	2.20e-73	54	598	9	532	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1
sp|Q0D1P3|TERE_ASPTN	2.94e-73	104	590	1	489	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000816	0.999152	CS pos: 28-29. Pr: 0.9686

TMHMM  Annotations     

There is no transmembrane helices in PTTG_02125-t43_1-p1.