CAZyme Information: PGTG_17514-t26_1-p1

Basic Information

• Species: Puccinia graminis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia graminis
• CAZyme ID: PGTG_17514-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635		70929.98	9.7492

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=DS178350:73884-76466(-)

Full Sequence      

MNPLAFTGPFGFLLSLLLIWNTILPADASKISISQTQAPWAPTTVLVISRKNISADCTIR
PSVTINGTFPGPELRFKAGQKLWIRVINELEDETTTIHFHGLAQFGSPFADGTVKISQFP
IPPKGGYFDYEFQLPDDSAGTYIYHTHHRFQAITGYGSFVIEENGPSPPYKYAGERTLIF
SDYYHATDSKIISGLASTPIKFLGEPQSLVVNGQALGSCNSSSLFGCTKNCGPHVLHVKP
GKTYRVRTIGMSALTFLYFAIESHSKFKIIEVDGGYIKPTSTPYIEIGSGQRYSFLLKTK
TLKQLRREGGQHEFYGRVESRWREKRDMGSFILRYDLSSSASKSTNGIDKSGSALSSIQK
NYSRTLITNPTDLDKIVPLPNEDIEWVGSRFRPLSLKKDAPTAAQVNRRIFISSQQRKAA
DGSVNWFVNNSTYVENKRKLPVLVQAYTDGLRPDYEAASKNNGYDSKLDAYPVKLGEVIE
FVIVNIASTVNVSEAHPWHLHGQKFYVIGQGYGEFNEESYEKINKDDHRRNKRSIERDTQ
VVFAGKNGKYFKGPMPSGSHVGWLVIRLVAKTPGAFLIHCHLQVHAIMGMTMVMLVGIEN
LPPLPKGFLKSYTSPHGLRVKEPLSYFDTVKKIQN

Enzyme Prediction     

No EC number prediction in PGTG_17514-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	58	590	3.8e-87	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	8.07e-159	42	597	9	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	2.83e-96	54	610	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	8.22e-89	174	335	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	2.61e-82	48	605	30	555	L-ascorbate oxidase
215324	PLN02604	1.40e-76	54	605	37	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL03177.1|AA1	1.04e-104	40	630	26	600
QGI63709.1|AA1	3.02e-103	40	624	26	577
QGI80980.1|AA1	3.02e-103	40	624	26	577
QGI94591.1|AA1	3.02e-103	40	624	26	577
BCS19632.1|AA1	4.78e-103	26	625	15	573

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.02e-73	56	605	18	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]
3KW7_A	1.39e-34	42	593	4	469	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
5Z1X_A	6.52e-33	42	600	4	469	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]
1GYC_A	1.87e-31	42	608	4	484	Chain A, LACCASE 2 [Trametes versicolor]
1ZPU_A	8.82e-31	60	594	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	3.70e-100	42	632	31	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	4.42e-99	42	623	28	591	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	4.90e-74	97	597	1	489	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|Q40588|ASO_TOBAC	6.98e-73	65	606	54	560	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1
sp|P24792|ASO_CUCMA	9.96e-73	56	605	48	562	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000224	0.999743	CS pos: 28-29. Pr: 0.9597

TMHMM  Annotations     

There is no transmembrane helices in PGTG_17514-t26_1-p1.