CAZyme Information: KIS66557.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS66557.1
• CAZy Family: CE4
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
767		85088.54	9.0761

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003157:336886-339189(+)

Full Sequence      

MILSKLGFALVRLISVLILCTCSHALPSSSSIPATRRLAPRRVTVRHYTLNVTTATLFSA
CDPFGPTTLIDSSFPGRVLRARAGEILSVRVYNHLDANGESGGNLTMHFHGLSMRMHPVM
DGTMLVSQWPITPGKFFDYRIPLTAEDKGTYYYHSHVGVQSMTAYGALVVEDPEEQELWD
PSQATLLKSKHAESVEFVHVYGEEALHKNGKSGQNSPYSYDQDRVLAIGDWFSYSSVKQV
QKQLLADPFVWPGSATKLLVNGKSSPVNISALSAPACNQTKADAIGVKCTSAPAQCARPV
YPTIELDYDKTYRFRLVGATSLMYVSLGILKPTKTAYTSINATSSVVAQPVQFDKMTLIE
ADGSYLDRLDVDHIELTSGQRYSVLYKSLSRKQVKQDGTGGVYWMRLESRWRAGPSMWLK
IVYPSHNTSAVQPPIRLASGQKDLQLLPAETFGWKTSQLSPLSKPYGPHWWYSDRMPSDS
EVTRTVLIDTQQVKFFASGKGVKWDQNGVALNETSPGTRTPYLVRTFLGDIQLPTATQIE
SAMYNPVSYKYRDSNGNDTGTSRMMIDMNNATEVEAASRRHWGQAYSSKLNMYFGGAGEV
IDIVLVNQASQLSSSVEIHPWHMHSHKHFTRTIQAGTFSFSRLASLYASSSSSKAFSNPI
QRDTTVAYASPGAAFLNQTIPNPQVDHGGWTVLRYKVDPKNAGVFLLHCHIAFHLEMGMA
TVWTMAPDQLARTARFNWPTLHSDHPNIQGLNADRYLHYANNVNAVL

Enzyme Prediction     

No EC number prediction in KIS66557.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	66	329	1.6e-41	0.5251396648044693
AA1	351	720	2.7e-20	0.44692737430167595

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	8.65e-102	45	724	1	530	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	5.74e-63	53	172	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	1.80e-55	45	732	1	530	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-51	222	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	1.20e-43	45	732	23	553	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBQ69957.1|AA1	0.0	40	767	42	767
SJX65603.1|AA1	0.0	40	767	42	767
CDU22462.1|AA1	0.0	25	766	29	760
SAM86019.1|AA1	6.28e-302	40	731	51	723
CDI56015.1|AA1	7.94e-128	162	485	1	329

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	3.70e-35	70	732	27	530	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	1.48e-13	70	723	27	528	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]
6VOX_A	8.68e-12	64	174	25	122	Chain A, Copper oxidase [Pseudomonas parafulva]
3KW7_A	4.60e-11	74	723	31	470	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]
5LWW_A	1.16e-10	40	177	19	149	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF64|AURL2_GIBZE	2.45e-57	69	732	50	564	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	7.75e-54	50	725	35	593	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	2.57e-50	107	725	1	488	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P14133|ASO_CUCSA	8.02e-36	70	723	62	557	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|P24792|ASO_CUCMA	7.81e-35	70	732	57	560	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
0.000654	0.999310	CS pos: 25-26. Pr: 0.9436

TMHMM  Annotations     

There is no transmembrane helices in KIS66557.1.