CAZyme Information: EAW19334.1

Basic Information

• Species: Aspergillus fischeri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
• CAZyme ID: EAW19334.1
• CAZy Family: GH17
• CAZyme Description: conidial pigment biosynthesis oxidase Abr1/brown 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
699	DS027696|CGC18	76128.08	4.5280

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

• Gene Location: location=DS027696:6089692-6091960(+)

Full Sequence      

MFHSRALLLSWLVGFTAAKDIHLDWNITWVWAAPDGFGRPMIGINNEWPCPIVNADLGDR
LIVDVHNGLGNQSTGIHWHGFHQYMTGTMDGSNQVTQCAMPPGSSMRYEFDVNQTGTYWY
HSHEMGQYPDGLRGPFIVRDPSPPFAYDDEFTLTLTDHYHEQMSVLLQEYEAQSVGAQAG
VNEPLPAAALINEGLDSTTLRVEPNKTYLIHLVCVGNWPGHVIVFDDHEISVVEVDGTWV
DAYPARDKKIRLATGQRMSILLKTKDNTDRNYAIWDSMDVNMMFFYENRAIPEGFNPNTT
AWLVYDEAKELPPAPDVHELDPNNDFVDDLVFVPANHEPLLEKVDRQIIFDTSVTQRDGR
SVYTINGQTYVDPEEPTMYTALAASPENASNASIYGQVNPFVVQYGEVVEIIINNHHGNL
HPWHIHGHQFQVLQRTVPEGGYFDGYFANISSTPVKRDTIMVQNHGHAGLTGTLIEAPAQ
MHDISVPLDHQRICPSYGTPPGGNTPPYDAPPAEDTTPPASPQDPQPGGNPPPNGTPPAE
NTTPPSPPPQDAPQPGGAPGSPQYPPQPWDKPGASPPQDAPQPGGAPGSPPQYSPQPWGK
PGASPPQQPPQPWSQPSNAQPPANNYAQGYPGTPSKPQPPANNYGQGYPSGYAPVAPGPV
IIDSEFHYGGKSSHVGSSGVNAGHRDGMTAESEGDASAS

Enzyme Prediction     

No EC number prediction in EAW19334.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	384	8.1e-120	0.9851632047477745

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.03e-57	22	466	3	489	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.
259945	CuRO_2_Fet3p_like	6.52e-55	149	307	1	148	The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.
259920	CuRO_1_Fet3p	8.94e-55	22	138	2	120	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.
225043	SufI	1.91e-50	18	446	32	404	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	8.57e-49	25	466	28	512	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHA42447.1|AA1	0.0	1	699	1	664
AHA42448.1|AA1	0.0	1	699	1	664
ACJ13061.1|AA1_2	0.0	5	684	1	645
BCS26736.1|AA1_2	2.19e-243	4	468	2	466
BCR85366.1|AA1_2	5.66e-237	9	468	10	466

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.70e-83	24	463	6	442	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]
5LDU_A	9.65e-50	24	497	7	491	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
5NQ7_A	9.24e-49	5	497	5	510	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
3FPX_A	1.22e-48	24	497	7	491	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]
3PXL_A	1.68e-48	24	497	7	491	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WZB4|ABR1_ASPFU	0.0	1	699	1	664	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2
sp|E9R598|FETC_ASPFU	4.59e-124	16	504	18	521	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.13e-111	5	504	9	525	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|K7NCS2|FETC_EPIFE	1.59e-111	13	504	15	524	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|W3X7K0|PFMAD_PESFW	2.86e-103	4	504	7	517	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000232	0.999732	CS pos: 18-19. Pr: 0.9677

TMHMM  Annotations     

There is no transmembrane helices in EAW19334.1.