CAZyme Information: An04g10400-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An04g10400-T-p1
• CAZy Family: GH13
• CAZyme Description: Putative multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
605		67115.66	4.7434

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=An04_A_niger_CBS_513_88:2522937-2524882(+)

Full Sequence      

MAFPSPLFAFFMLLGLLDSVRAIGNWSCPDLITSSVPVKFALILTEQNISPDGFQRKGIL
VNGQFPGPILEVCQGVEVEVQVWNELPYPVTVHFHGIEQRETPWSDGVPGVSQKGIQPGL
SFTYKWRATDSRSYFYHSYERGHLEDGLYGAIYIHPRNSVERPFAQITDDPSQLEAMHIA
EQNTKPIILSDWRHLASEQVWEAEEATGLDAYCANALLINGKGSVTCLSQETIDEFTSED
LKPLLNGSHLTDIGCLPPTIPAAQGPYRHNFSAVPQSLFSGCNASHGATETLLVDPGLQY
SSWDLINAGGLATLSFSIDEHPMYVYAVDGRYIVPKLVEAVKLVPGRRFSVLVKLDKPPR
DYTVRSNIVGNQILNTTTIMSYDAAVRFQNDPSTPYIDITGRNATPDAVLLDETQVVPFP
VEVPAQTADQTFVLHIDRFNSSYQWTLGNGSFPLSLEEAAPLLFYPDSEVAHSDLTIRTT
NGSWVDLIFYVRSAPQPEHPIHKHSNKFFYIGSGQGEWEYPSVAEAMRDIPHNFNLHNPP
LFDTIATPAAMSDPVWTAVRYHVVNPGAFVVHCHIQVHINGGMSLAVLDGIDAWPQIPDE
YQITN

Enzyme Prediction     

No EC number prediction in An04g10400-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	54	583	1.2e-74	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	2.26e-73	429	590	1	164	The third 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 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.
259944	CuRO_2_Abr2_like	7.38e-57	185	382	1	137	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.
274555	ascorbase	5.29e-56	50	600	14	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.
177843	PLN02191	3.27e-54	50	600	36	557	L-ascorbate oxidase
215324	PLN02604	5.78e-53	50	598	37	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK44820.1|AA1	0.0	1	605	1	605
BCR93194.1|AA1	1.34e-248	14	605	8	601
CAK37405.1|AA1	2.19e-247	14	605	8	601
QRD91048.1|AA1	1.72e-233	24	603	18	596
QMW31975.1|AA1	1.72e-233	24	603	18	596

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	5.09e-38	25	589	57	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.27e-37	25	589	57	542	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]
1AOZ_A	2.34e-37	61	598	27	532	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]
6KLG_A	3.10e-32	40	584	6	525	Crystal Structure of the Zea Mays laccase 3 [Zea mays],6KLI_A Crystal Structure of the Zea Mays laccase 3 complexed with sinapyl [Zea mays],6KLJ_A Crystal Structure of the Zea Mays laccase 3 complexed with coniferyl [Zea mays]
5LM8_A	7.54e-32	52	589	38	504	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9RBR0|ABR2_ASPFU	3.53e-163	32	597	14	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	1.04e-143	29	601	16	592	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	6.07e-141	26	601	14	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	1.53e-140	27	601	9	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	2.89e-135	14	605	7	609	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000219	0.999767	CS pos: 22-23. Pr: 0.9761

TMHMM  Annotations     

There is no transmembrane helices in An04g10400-T-p1.