CAZyme Information: EKG13968.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG13968.1
• CAZy Family: GH106
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
690		77127.08	5.4252

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=AHHD01000376:17607-19679(-)

Full Sequence      

MIDTKSTGSGADGGRYAALRQDESELYEQKEHTQCTQPSGAAYLGGNGREEALGLIDENV
VARTKRRCGPTRRYSVFLEFAILGLVLIIALLGALAWSRGSHHHTDPVSGSSQPSSKGRR
GKYVLDPAWDFAAPPQVRKYHWTIRDIELRPDGVKRPLITINNEFPGPTIECNQGDTVRV
EVHNEAVNSTSFHWHGIYQNGTTYMDGTVGISQCPITSGSSMTYEFKVDRESGTYWYHAH
MAMQGSDGLFGPLIVHSKNERKLQQLEYASDQVIMVHDYYHDLTSALIPHYLAPDNENTE
PVPDGGLINGMNKRNCELLRGRDCDATDAQLATFGLEPNKNHRLRIINTGAFAEFQVKID
EHTFAVTEVDGTEVAPAYYHRLNINPGQRYSIVINTNVTDRDSFWLRAKMIEACFAEENP
NLDPEVRAIIQYTRKDEDTQPKEPSSRDWDDIVDMQCLDMNVTELQPVEKATPPPADTTL
YLRSNFEIGNWRLSRGFFNSSSWRPTLSSPSLHRMIDGLHSQNASFLPDRAYPFQINSAG
FDTGPELVYQTSGIRTIDILVSNFDDGNHPLHLHGYKYFVLASGHGYPPADLYAHLDISN
PLRRDTASIEAFGWILLRLVADNPGVWAFHCHIGWHTEAGMLMQFATRVDVLASSQIPDT
HLALCAADGLDRGASPPDSTWFGDFGDLDP

Enzyme Prediction     

No EC number prediction in EKG13968.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	154	641	2.3e-111	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.48e-87	137	663	1	537	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.
215324	PLN02604	1.22e-78	132	655	19	557	oxidoreductase
177843	PLN02191	4.53e-76	132	662	18	559	L-ascorbate oxidase
259926	CuRO_1_Diphenol_Ox	6.62e-71	138	256	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259953	CuRO_2_MCO_like_1	3.13e-70	272	433	1	163	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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
QIW97242.1|AA1	2.30e-236	21	685	5	658
QGI88009.1|AA1	3.35e-236	40	685	18	680
QGI70665.1|AA1	3.35e-236	40	685	18	680
CCT75372.1|AA1	3.35e-236	40	685	18	680
QGJ01555.1|AA1	3.35e-236	40	685	18	680

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	2.38e-67	137	648	23	505	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.43e-67	137	648	24	506	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
1AOZ_A	3.54e-67	136	663	2	537	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]
5LWX_A	8.47e-67	137	648	51	533	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	1.20e-63	111	653	40	548	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	1.57e-94	123	666	47	579	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	6.37e-93	123	666	47	579	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.36e-91	101	666	31	579	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|I1RMG9|FET3_GIBZE	1.10e-76	120	670	2	520	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|A0A067XMP2|PTAK_PESFW	2.59e-74	137	665	64	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000004

TMHMM  Annotations     

Start	End
75	97