CAZyme Information: EKG20708.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG20708.1
• CAZy Family: GT2
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553		62161.58	6.0821

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

• Gene Location: location=AHHD01000080:41978-43837(-)

Full Sequence      

MAQDGNPRGVLTINGQTPGPLIWGYEGDTLRVTVTNKMFIEATMHWHGVYQVDKYWNDGV
PGVTQWPIESRDSYTYEFTLTNQTGSYFYHGHFGPAFADGQRGPLWIAPAPWRPRPYELA
SDDPAEVAAMRAAEDNPRHLMVSDWNYEGMEVLIVGFRDAGIAPACSASLVTNGKGRTTC
LGPDDIKKYDPEGRRNSLGCLPPPVGAEFTNKRECRETTTDFEIIQAEEGEKYIYMNFIH
PGAHHELRIAVDEHDMIIVAADGDFVMPKKVQAINLNMGDRISVLVPLDKKPGEYAIRLS
SISEEQLITGLSILRYPGVQERRKDGIMLAPETKPHIDLLGRMVTEGGVMMDEMTDLAPF
PPRSPPATSDHTFRFLSNRTGPSTWMLSSEPHQGFRQQMPPIMWNEESRGPTTIQGMKNG
STVDIIFESRAYAMHPFHKHNHKAWIIGRGKGYFRWPDVATAISEAPENFNLINPPLRDG
ARLEAEEGSWTVIRYTITFPAMSMLHCHRIQHFAAGQQIVLLEGQDVMQSPPEYIKKMTH
ASFVPPLRYGPLD

Enzyme Prediction     

No EC number prediction in EKG20708.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	8	516	1e-71	0.9692737430167597

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.09e-57	4	533	16	534	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.
259944	CuRO_2_Abr2_like	3.67e-56	138	317	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.
177843	PLN02191	2.28e-52	10	533	44	556	L-ascorbate oxidase
259919	CuRO_1_Abr2_like	3.70e-52	3	107	12	116	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.
215324	PLN02604	4.55e-52	10	535	45	558	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SMR53097.1|AA1	1.11e-301	4	553	37	586
SMQ51194.1|AA1	1.11e-301	4	553	37	586
SMR54717.1|AA1	1.11e-301	4	553	37	586
SMY24839.1|AA1	1.58e-301	4	553	37	586
CEI62063.1|AA1	2.80e-229	2	553	38	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.04e-38	6	524	20	524	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	2.19e-33	4	525	82	544	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	4.00e-33	4	525	82	544	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]
2XYB_A	5.97e-33	1	523	15	467	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
5NQ7_A	8.05e-30	1	523	36	488	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	1.70e-228	4	553	37	592	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.70e-85	3	527	29	575	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	2.87e-83	2	534	37	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|A0A443HK79|VDTB1_BYSSP	1.31e-82	2	534	32	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	5.25e-78	2	539	36	597	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000072	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EKG20708.1.