CAZyme Information: An05g02540-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An05g02540-T-p1
• CAZy Family: GH131
• CAZyme Description: Putative multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
588	An05_A_niger_CBS_513_88|CGC4	65795.45	4.5240

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=An05_A_niger_CBS_513_88:578611-580513(+)

Full Sequence      

MWLPHGKLVLASFFIFIQWALCRVVEYNLTLTWEDLEVAGITRKAVLINGQFPGPPLRLK
QGDNVEVMVTNNMPFSTTIHFHGIRQQGTPWSDGVPGLTQLPIGPGSQFLYAWKADDYGT
YIYHSHEAARIDDGLYGAIYIEPADNIEKPFSIITTDEVELEFLKKAEQNTQPVILSDWR
RFTSDEIWYIEEQSGVESYCASSILVNGKGSTYCPPQEQINELTRPELKSLLKGGNMSDM
GCLPPIPSRLGFFSFNISNIPQGYYQGCTPAVGETQVFSIDPAWRYVSYDLINIAGSSSL
VFSVDEHPLYIYAVDGRYVEPVLVDALTIHIGARYSVMAKLDQAAGNYTVRIANSYANQI
INGTAVLSYEAPIEQDFVSQPYITEIGTAVSRQTSILDESNLVPFPAIPPASDVDRTYIL
NIHMYNASYRWVLGNDSFPLSLEHLSTPVLYNISSIPVQYTLPTLNDTWVDIIFNVTVDE
PQHPLHKHSNKFFVIGEGTGPWTYSSVAEAVEHIPEKFNFVNPQIRDTYPTPNSREGGAW
LAIRYYVENPGPFLLHCHVLMHQVGGLDIALLDGIDAWPTVPENVNLP

Enzyme Prediction     

No EC number prediction in An05g02540-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	567	1.1e-80	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.16e-74	415	574	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	7.61e-60	172	370	1	138	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	3.12e-58	43	585	19	535	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	1.06e-56	15	585	15	558	oxidoreductase
259919	CuRO_1_Abr2_like	1.79e-55	27	141	1	116	The first 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 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
CAK44915.1|AA1	0.0	1	588	1	588
BCS12208.1|AA1	3.04e-261	2	588	3	595
BCS00432.1|AA1	3.04e-261	2	588	3	595
CAK47814.1|AA1	1.57e-260	2	588	3	592
CAK37372.1|AA1	4.73e-260	16	588	15	592

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	3.67e-54	26	573	69	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]
3V9E_A	7.00e-54	26	573	69	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	5.05e-46	24	566	23	497	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.13e-46	24	566	24	498	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	5.60e-46	24	566	51	525	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|E9RBR0|ABR2_ASPFU	5.02e-172	20	588	15	586	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	1.05e-147	23	582	22	589	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	1.13e-146	26	583	43	612	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	9.18e-146	24	582	47	621	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	3.82e-140	25	584	23	604	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.863533	0.136486

TMHMM  Annotations     

There is no transmembrane helices in An05g02540-T-p1.