CAZyme Information: KNZ59038.1

Basic Information

• Species: Puccinia sorghi
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi
• CAZyme ID: KNZ59038.1
• CAZy Family: GH71
• CAZyme Description: L-ascorbate oxidase [Source:UniProtKB/TrEMBL;Acc:A0A0L6VE52]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
628		70210.97	9.2262

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsorghiRO10H11247	21769	N/A	691	21078

• Gene Location: location=LAVV01006628:14979-17500(+)

Full Sequence      

MNPLDLISLLVAFQFIPVQHFILAAVSKIPSPPAPWAPTTVLVISRTNVSVGCTIRPSVT
INGTFPGPELRFKSGQKLWIRVINELDDEATTIHFHGLSQFGSPFADGTVKVSQSPIAPR
GGTFDYEFQLPPDSEGTYIYHTHHKFQSVTGYGSFIIEANDGPLPYSYDEERTLMFSDYY
HATDNQIISGLASTPIKFLGEPQSLAVNGRALGFCNSSSLFGCTKNCHPYVMHVEPGKTY
RVRAIGMTALTFLYFAIESHLKLTVIEVEGGFIKRTSSSFMQLGSGQRYSFLLKTKTLKQ
LQDQGGQRDFYGRVESRWREKRDMGSFILRYDLSSSASGRSNGNKESAPVPSPKPRNYFN
QIITNPTDLDKIVPLPTEEQEWIESRFRPLLRKKDAPTAAQVSRRIFISSQQRKTPDGTV
NWFVNNMTYFENKHRVPLLVQAYTHGLKPDYEAASRNNGYDAKLDAYPVKLGEVIEFVIV
NTASTVNVSEAHPWHLHGQKFYVIGQGYGEFNEESYQKVNKDNHLKNKRSIERDTQIVLA
GKNGKYFKGPMPSGSHVGWLVIRLVAKTPGAFLVHCHLQVHAIMGMTLVMLVGIENLPPL
PQGFLEEYTNPGGSRVKQPVSHVASVEA

Enzyme Prediction     

No EC number prediction in KNZ59038.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	54	586	5.1e-84	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	3.10e-159	38	593	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	5.77e-97	53	601	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.
259941	CuRO_2_AAO_like_2	1.06e-83	170	331	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	3.86e-82	59	601	46	555	oxidoreductase
177843	PLN02191	2.22e-80	59	601	45	555	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL03177.1|AA1	3.64e-103	36	622	26	590
CCT67688.1|AA1	9.39e-100	13	620	3	592
QGI63709.1|AA1	1.24e-99	13	620	3	577
QGI80980.1|AA1	1.24e-99	13	620	3	577
QGI94591.1|AA1	1.24e-99	13	620	3	577

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	3.46e-72	61	601	27	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	1.29e-37	52	590	18	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]
5EHF_A	1.03e-33	38	598	4	470	Laccase from Antrodiella faginea [Antrodiella faginea]
6RHH_A	5.31e-32	38	604	5	484	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]
5MEW_A	5.37e-32	38	604	5	484	The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. Second structure of the series with total exposition time 33 min. [Steccherinum murashkinskyi],6RGH_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RGP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	1.44e-101	38	614	31	616	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	3.24e-96	13	619	3	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|P37064|ASO_CUCPM	1.78e-71	61	601	27	532	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1
sp|P24792|ASO_CUCMA	1.73e-70	61	601	57	562	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|Q0D1P3|TERE_ASPTN	9.28e-70	93	613	1	511	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 OTHER

Other	SP_Sec_SPI	CS Position
0.640984	0.359019

TMHMM  Annotations     

There is no transmembrane helices in KNZ59038.1.