CAZyme Information: KIS67600.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS67600.1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
630	CM003151|CGC1	69997.95	5.8634

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=CM003151:23340-25553(-)

Full Sequence      

MQRYISPLFTALLVLSSTWMVFAKTVQHDWTISPLYEAPEDGHYRMTFGINGHTPGPVLE
LDQGDDVEISIHNSLPVDITIHWHGILQIGSPEMDGVPGVTQWAIPPLGDYTYKFTPTNQ
TGLHWYHAHLRGYLDDGVKGLLYIRPSAQRPRPFQLIDPSGDQVAAMQQAEDSPRNLALY
DWKHVQEDEALAMFFASGRPTTCVDSVLFNGKGSIYCASAETLNQAAGGRFDAMPFFESK
LDARGCLVIPGSGIYSAHTITSPMGCSNSTGQLEIVPTHSEWTLINLANVGGEWTWVFSI
DAHDLWVISADGDYIVPEKVQALPVSIGQRYGVMVRTDKPDGGDYYIRANSAGFAQVMGG
VGILRYQDAPHQKRRTTEQTSVSVADPWRDMSRSHVKYNATPAEGTSTYDPIKSMPFIAD
APPSKVDRTLIFHANQSEPTVFSIASRPLRMVEELNLPVLFSNSSQYTGTRDPDWLIRIA
KGDVVDVILQNAQNALFPAPAEPPHPIHLHGHKFWVLGSNEYDDWQFQSAAEAMAHGVQL
NLDNPPKRDTFLLPTAGWLVLRFVADNPGAWMLHCHRMGVVFLEGEDEIAAIPDRFQKRP
TAHVAHQGWQTDARTKRSLDDSARHPALFV

Enzyme Prediction     

No EC number prediction in KIS67600.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	44	577	4.8e-84	0.952513966480447

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.42e-74	25	594	1	533	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.
177843	PLN02191	1.32e-69	12	594	10	556	L-ascorbate oxidase
215324	PLN02604	9.92e-61	23	593	22	555	oxidoreductase
259919	CuRO_1_Abr2_like	9.28e-58	41	145	13	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259944	CuRO_2_Abr2_like	2.74e-54	175	367	1	138	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains 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
QOD95012.1|AA1	5.52e-111	10	592	11	642
CZS81623.1|AA1	4.49e-106	27	599	27	575
QLI72976.1|AA1	5.94e-105	10	592	16	654
CEI62063.1|AA1	7.07e-105	27	599	27	576
CEF78328.1|AA1	1.36e-104	27	599	27	575

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	5.21e-57	28	595	6	534	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]
3V9E_A	2.47e-44	41	590	82	548	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	6.30e-44	41	590	82	548	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
5LWX_A	7.60e-39	41	576	66	517	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.00e-38	41	576	38	489	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	2.27e-98	4	599	2	577	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|A0A443HK79|VDTB1_BYSSP	5.75e-87	12	596	6	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	2.00e-83	10	603	7	599	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	2.27e-80	20	596	19	600	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	3.00e-75	16	615	16	621	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000386	0.999566	CS pos: 23-24. Pr: 0.9765

TMHMM  Annotations     

There is no transmembrane helices in KIS67600.1.