CAZyme Information: An01g00860-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An01g00860-T-p1
• CAZy Family: AA1
• CAZyme Description: Putative multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
508		56135.73	6.4147

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

• Gene Location: location=An01_A_niger_CBS_513_88:202613-204197(-)

Full Sequence      

MVYWQSWFLLLGTVASFNPLESLLPDGLSPYGLLPTYHLDPFLKSGSNNNQYQHSNLEHP
PWKDISPSGGPPDTGVTRHYNFTITRDITAPDGYQKSGILINGQFPGPLIEANWGDMISV
TVNNMITTETAEGLTLHWHGLTQAKSPWEDGVPGITQCPIAPGGSFTYTFQADQYGTSWY
HSHYSAQYTDGAYGPMIIHGPVQPEASYDYDLGPVIISDYSHLSYFEVLENIFSIPPVFP
NVDNNLINGRGAYNCNSSSTTTCSPASSLARFNFHSGKTHRLRLMNTGSNANQKFTIDGH
NMTVIANDFVPVQPYTTDVVTLGVGQRTDIIVTXTGNPTESYWMRASIDMTCLNATASIP
TVKAAIYYEDADTATWPTTTTTTTWSSNNCANDPLNLTIPYYLQTPPSTPATTQTMEITX
GENATXHTLFYVNNXHLPLRLQHPAPPPRQSRQLLRPGPRPERLQLRLELLRPSHHLQSL
LHAAPASSPRSQLLGASPGKRDLGWSRH

Enzyme Prediction     

EC	1.10.3.2:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	72	384	4.8e-122	0.9583333333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	3.18e-70	75	199	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.
274555	ascorbase	3.32e-60	77	348	1	281	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.
259926	CuRO_1_Diphenol_Ox	6.77e-58	78	199	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.
215324	PLN02604	2.80e-54	77	348	24	302	oxidoreductase
259947	CuRO_2_MaLCC_like	1.34e-50	212	372	1	153	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS07898.1|AA1_3	3.40e-288	1	434	2	435
BCR95349.1|AA1_3	1.71e-282	1	434	2	459
CAK43464.1|AA1_3	2.26e-278	1	373	1	373
QGA18227.1|AA1_3	4.33e-167	13	434	11	416
QKX63435.1|AA1_3	1.09e-164	61	434	44	415

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	2.96e-76	62	352	58	334	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.96e-76	62	352	58	334	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	1.10e-67	35	401	2	362	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.17e-67	72	401	18	334	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.19e-67	72	401	19	335	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	1.53e-106	61	445	44	433	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	5.72e-89	54	401	41	388	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.72e-79	62	401	58	380	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q0CCX6|GEDJ_ASPTN	7.70e-74	62	405	45	381	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	8.59e-74	75	377	55	353	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000253	0.999729	CS pos: 16-17. Pr: 0.9634

TMHMM  Annotations     

There is no transmembrane helices in An01g00860-T-p1.