CAZyme Information: An01g11120-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An01g11120-T-p1
• CAZy Family: AA3
• CAZyme Description: Putative multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
586	An01_A_niger_CBS_513_88|CGC10	65307.62	6.4031

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_88:2621286-2623428(-)

Full Sequence      

MQQSPSFRLRLLPWSIVLYPATICGLIFLLFLTQISQPSPLQDLIPSGVSNSQVHPVTHD
PDTSRPLIELQPENHVYRDPATQHFDWVVTANHRRPDGVLKWIYLINGLFPGPTVEARPG
DRLIVNVTNSLEDEPISIHWHGIHIENAMDGAVGVTQCPIPPGSTFTYNFTIPAHQSGTF
WYHAHSGLIRADGLYGGLIVHEPSPKPTVRGLLARADEKGTASYDRDILLLIGDWYHRSA
DQVYSWYMRAGSFGNEPVPDSLLINGMNLSYLDAKGDAAYRVRVVNTGSVAGFTLGFQNK
EFSLIQVDSIEVEQEDSNSAGVLYPGQRMDIILRPGPDKTPSSMTIDLDKEYPNPALASI
QTFNITKSSDNTSSTISPSNNTISLSEVATRKSLLSSLPEKAHQTHVVYSKIEKLSINHN
VPYGFFNRTSWKPQIDTPLIDLPRDKWDGNQLVLSTGSSTSRALPSDKDQDLWIDLIVNN
LDDSGHPFHLHGHHFYILRTYQAPVGWGAYNPFTDAYPPGLAPESVSSSRADTPYDLSRA
QLRDTVYIPSRGHAILRFRADNPGIWLFHCHIIWHQASGMAMLLQM

Enzyme Prediction     

No EC number prediction in An01g11120-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	99	581	7.3e-93	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.92e-64	82	580	1	517	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.
225043	SufI	5.86e-64	87	581	38	443	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
177843	PLN02191	4.13e-59	81	584	22	544	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.55e-58	407	585	2	165	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
215324	PLN02604	4.06e-56	82	585	24	545	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK44017.1|AA1	0.0	1	586	1	586
BCS06095.1|AA1	1.99e-286	149	585	1	458
BCR93452.1|AA1	1.99e-286	149	585	1	458
QMW37919.1|AA1	2.44e-244	2	585	9	597
QRD88142.1|AA1	8.94e-244	2	585	26	614

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.23e-58	82	584	2	477	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
3V9E_A	8.94e-53	87	582	71	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.35e-52	87	582	71	538	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]
5LM8_A	1.66e-49	62	581	8	499	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.68e-49	62	581	9	500	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|I1RMG9|FET3_GIBZE	4.72e-62	81	580	23	490	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|Q6CII3|FET3_KLULA	7.72e-62	81	584	26	503	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|K7NCS2|FETC_EPIFE	3.37e-61	81	581	21	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|P43561|FET5_YEAST	6.48e-61	89	581	30	508	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	9.15e-60	80	579	59	553	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999742	0.000288

TMHMM  Annotations     

Start	End
13	35