CAZyme Information: EKG14040.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG14040.1
• CAZy Family: GH125
• CAZyme Description: Multicopper oxidase type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
617	AHHD01000375|CGC3	68165.75	5.6750

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=AHHD01000375:128102-130070(+)

Full Sequence      

MKCATLWSYLASVLTVGASARSLTRSLPQHKTNGGSNWGTLDCPKLPDFLTSNPLPGGFP
WGDRSGLSNDPYTDVPNTGVTRYYDFSVARGYLAPDGYNKSGIFINGEFPGPAIEANWGD
MIEVRVHNNIVGPEEGTAFHWHGITQKGTQWFDGVPGVSQCPIAPGSSFTYRFRADVYGT
SWWHSHFSAQYTAGAFGPLIIYGPKHVPYDVDVGPVILGDYYHRDYFDVLEDAASNTTDF
NIYVPWSDNNLINGKNNYNCSMVAGNSTSFANATSSSNATCFSNAGLAQFRFEPGKVHRL
RLMNVGAAALLHFSIDGHKMQVIAHDFEPVVPYEADVITLGAAQRTDILVTADANPNETY
WIRSTISLNCSVSHNTNALAVLSYEGNDHIEEPRSRISAAAAAADEKSFLCKNDDLSQTV
PFFPKPVAEPDVTETIEVDLFTNATGHHVWIMNNRTQRTNYNEPVLLLANQGNSTFPDEW
NVYDFGRNKTIRIVLNTVYQSAHPMHLHGHSFQVLAEGPGAWDGTTITNPSNPARRDTHM
QRRYGHLVIQFEADNPGAWSYHCHIAWHASMGYNIEILERGDELAAAGAIPMVMQQTCDD
WKEWSGRNVVNQIDAGI

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	70	397	1.4e-114	0.967948717948718

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.47e-85	81	591	1	532	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	3.79e-78	81	584	24	554	oxidoreductase
177843	PLN02191	2.35e-74	78	591	20	555	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	3.49e-71	426	578	2	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.
259923	CuRO_1_MaLCC_like	1.29e-68	79	202	1	122	The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCR87931.1|AA1_3	0.0	1	617	21	627
QFF92555.1|AA1_3	3.65e-232	5	617	2	593
APA07098.1|AA1_3	2.67e-230	5	617	2	596
QFF92556.1|AA1_3	3.93e-229	5	617	2	593
ATZ46043.1|AA1_3	3.19e-228	5	617	2	593

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.72e-110	61	617	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.72e-110	61	617	49	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]
5LWX_A	7.76e-95	47	608	8	560	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.01e-94	60	608	3	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.04e-94	60	608	4	533	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|A0A067XMP2|PTAK_PESFW	1.52e-183	44	617	23	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	2.23e-114	61	617	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.94e-113	61	617	47	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	2.25e-113	7	617	5	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	2.80e-95	45	617	23	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000386	0.999578	CS pos: 20-21. Pr: 0.9701

TMHMM  Annotations     

There is no transmembrane helices in EKG14040.1.