CAZyme Information: sr16230-t26_1-p1

Basic Information

• Species: Sporisorium reilianum
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Sporisorium; Sporisorium reilianum
• CAZyme ID: sr16230-t26_1-p1
• CAZy Family: GT21
• CAZyme Description: related to L-ascorbate oxidase precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
767		83988.53	6.3433

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SreilianumSRZ2	6791	999809	118	6673

• Gene Location: location=FQ311439:304097-306400(+)

Full Sequence      

MPNTPPFSLFSAFLLLTLSLTSLTLTAARPSEITFSPRSPPPRHITVRHYTLNITSTILW
QSCDPFGATTVVNATLPGPTLRARAGEILQIRVYNSLSPDAEDANGGNVTMHFHGLAMRM
HPVMDGTMMVSQWPVRPGRWFDYRIPLTAEDKGTYFYHSHVGVQAMTAYGALVVEDPVGV
YVDPSDADAEAATEGRVKFVHVDGDAGLARKGKSGKESPYAYDEDRVLAVGDWFSYSSTA
LVQNQLRADPFVWPGSATKLLLNGQSSPSTTTPPPCNQTRADPIGIQCSTAPAHCDTPPA
YPTIHLDYDKTYRLRLIGATSLMYVSLAILQPTATPYTSANASDSKARQPVGMENMTLIE
ADGTYLDALEVDRVELTTGQRYSVLYKSRTRAQVSGDGTGGVYWMRVESRWRAGPSMWVK
LVYPSSSSTASTASPPLKLFPGQKDVQLLPAETFGWVTSQLAPLSRASGPEWWYAAPMPS
DEQVTRTVVIDTQQVKFYPSGKGVKWDEDGTVFDEPAPPTAQPYLVRTFLGDIQFPTPSQ
FQSALYNPTTYSYAGSSTSSNAAPQEIIDLGDKAEVAAAKKRKWAQGYDSALNMYFAQAD
EVIDIVLVNKPSAISSNVEIHPWHMHSHKHFTRTTQPGTFSFRHLDALYSSASSSFAHPI
QRDTTVAYANPGAAFLNQTVPNPTTDDGGWTVLRYKVDKENAGVFLLHCHIQFHLEMGMA
TVWTVAPDVLANRTGMYWPTEGRGGTKTIEGLDDGYLEYGKSVSAVL

Enzyme Prediction     

No EC number prediction in sr16230-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	69	329	6.4e-43	0.5223463687150838
AA1	353	720	2e-20	0.441340782122905

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	1.84e-106	50	725	11	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.
259916	CuRO_1_AAO_like_2	5.12e-52	55	176	1	117	The first cupredoxin domain of Ascorbate oxidase homologs. This family includes fungal proteins with similarity 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 couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555	ascorbase	3.24e-49	47	723	1	521	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	1.01e-48	224	423	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	1.11e-42	47	723	23	544	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBQ69957.1|AA1	0.0	1	767	1	767
SJX65603.1|AA1	0.0	1	767	1	767
CDU22462.1|AA1	0.0	9	766	10	760
SAM86019.1|AA1	1.64e-309	9	766	6	762
CDI56015.1|AA1	2.23e-127	166	487	1	329

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	4.32e-37	47	723	3	521	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]
6KLG_A	3.39e-17	49	725	5	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]
6RHH_A	3.95e-13	62	408	17	265	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	3.96e-13	62	408	17	265	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]
5MEJ_A	3.96e-13	62	408	17	265	Structural study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. First structure of the series with 3 min total X-ray exposition time. [Steccherinum murashkinskyi],5MHU_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The third structure of the series with total exposition time 63 min. [Steccherinum murashkinskyi],5MHV_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fourth structure of the series with total exposition time 93 min. [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF64|AURL2_GIBZE	1.59e-60	71	723	50	555	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|G2QFD0|LMCO1_MYCTT	2.72e-56	71	730	53	600	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|Q0D1P3|TERE_ASPTN	7.58e-55	111	723	1	486	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P24792|ASO_CUCMA	1.56e-37	47	723	33	551	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|P37064|ASO_CUCPM	2.22e-36	47	723	3	521	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
0.000213	0.999767	CS pos: 28-29. Pr: 0.9682

TMHMM  Annotations     

Start	End
7	29