CAZyme Information: EKG11356.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG11356.1
• CAZy Family: AA3
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
421		47404.24	4.8094

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=AHHD01000484:42304-43617(+)

Full Sequence      

MNYDVDLGPLLISDWYHHDAFGLFHYEIASPHAPLPVTTILNGKGVFDCDPASDARCTGE
HQRHEIVFEEGKRYKIGLINTGSLLTYKFWIDGHNFTVVQTDFVPIKPYVTDVLIVGIAQ
RYEIIIEANVTFTRGSNFWIHATYCDDDDMLDSRVGIVRYDGSDGRDPHTPPKSEQHPGY
GCRDPATENLVPIVKREVGKRVNGLSPADYLRIGLQGWPNISDTDSLVHKWTLTNRTQYI
DWREPTIKALTSDVGADFADETCPIYLDYETGEWVYFVIENNYTLSDANTPRTIPRSVHP
IHLHGHDFVILAQGDGMFDPVDVVPNLHNPTRRDVVNCPIGGYVWIAFQVNNPGAWLMHC
HIAWHASAGLSLQFIEQPGLIKGLMEQAGALPELADRCEDWTEYYNTVNIPKGALQDDSG
I

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	3	370	5.5e-60	0.6675977653631285

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.78e-64	220	375	15	157	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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. It 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. 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259947	CuRO_2_MaLCC_like	8.74e-62	7	173	1	162	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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. It 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. 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.
400194	Cu-oxidase_2	8.03e-35	239	379	1	137	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259868	CuRO_2_LCC_like	6.00e-32	9	160	2	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	2.21e-30	1	398	151	561	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QED41496.1|AA1_3	3.12e-218	2	421	191	613
QLI68968.1|AA1_3	8.14e-206	2	421	183	601
QIW99253.1|AA1_3	1.41e-191	2	421	200	621
BAA08486.1|AA1_3|1.10.3.-	9.48e-181	2	421	185	605
AGO59042.1|AA1_3	1.43e-162	2	421	170	596

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.10e-74	2	421	192	580	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]
3V9E_A	4.13e-74	2	421	192	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	4.06e-62	3	404	149	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.15e-62	3	404	150	529	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	9.89e-62	3	404	177	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0CCX6|GEDJ_ASPTN	4.18e-182	2	421	185	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q4WQY8|TPCJ_ASPFU	1.44e-178	1	421	188	609	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1
sp|A0A067XMP0|PTAE_PESFW	3.98e-163	2	421	184	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	4.65e-84	2	421	198	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|D4APX3|LAC1_ARTBC	5.26e-77	3	421	217	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EKG11356.1.