CAZyme Information: KZZ88890.1

Basic Information

• Species: Ascosphaera apis
• Lineage: Ascomycota; Eurotiomycetes; ; Ascosphaeraceae; Ascosphaera; Ascosphaera apis
• CAZyme ID: KZZ88890.1
• CAZy Family: GH16
• CAZyme Description: Ferro-O2-oxidoreductase [Source:UniProtKB/TrEMBL;Acc:A0A166NBG5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
671	AZGZ01000023|CGC1	75106.64	6.1115

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AapisARSEF7405	6442	392613	0	6442

• Gene Location: location=AZGZ01000023:255317-258063(-)

Full Sequence      

MERPISRRRHRAARVDEQQESEVDTPTLMSSTEKPLANGTDGSARGIWGYIIALLVVIGA
AFTLLAQGVQIPLLQSNNHHGASSIAVDEPTRLQDLHPEDHVYRSPKTIEFNWTVSSGMR
RPDGVVKKVYLINDLFPGPTIEARSGDRLLITVNNALENEEISMHWHGLHMRGHNDMDGV
DSVTQCPINPGGSFLYNFTIADYQSGTFWYHSHSSLQRGEGLFGALIIHKPVPLSIRGSA
PARALHSDFERYGYDKEALMLMGDWYHEPAQKTMNWYLSSASWGNEPVPDSLLINGVGHF
PCSRVAPAKPLDCIDDGYVIPHLKLDPALTYRIRAINFGTLAGISLAFQNHQVEVITVDG
GLEVEVTSKEAQSLGILYSGQRVDFILRPLDTEMQHSGFTINLDREDFRYANPAMISEQA
YPIVPSSFESPTAAGNSTGLPPLIDIPSTNHIDLSTLTSSAKITHDIPEKADETYMVYVN
VMKKAINAFKPYSYLNHTSWKPQSNPRVPLLGLPREEWDEHQLSIVIGDDQKQNDEPKKA
RWVDLVVNNLNEGSHPFHMHGHNFHVISTHQSALKFGSYNPFEPIPSNADFAGPPYDVSA
SLARDTVLIPFHGHVVLRFKADNPGLWIFHCHVMWHLSGGMAMMIDEREPEERERVKNER
WGECKGYNTPD

Enzyme Prediction     

No EC number prediction in KZZ88890.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	125	642	1.9e-93	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.56e-68	110	641	3	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.
177843	PLN02191	1.75e-66	105	644	20	543	L-ascorbate oxidase
274556	laccase	3.05e-56	127	643	22	515	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
259869	CuRO_1_LCC_like	1.02e-54	110	229	2	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
259926	CuRO_1_Diphenol_Ox	3.47e-53	110	229	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA16928.1|AA1	6.01e-192	77	646	86	668
QKX62088.1|AA1	1.58e-185	45	646	42	651
UPX44859.1|AA1	1.98e-183	29	646	15	626
QRD88142.1|AA1	1.01e-177	1	649	1	617
QMW25836.1|AA1	1.01e-177	1	649	1	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.54e-59	107	647	1	479	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	3.89e-53	108	649	67	544	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.01e-52	108	649	67	544	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	3.91e-51	111	647	6	523	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]
5EHF_A	6.91e-51	121	651	16	471	Laccase from Antrodiella faginea [Antrodiella faginea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	7.87e-70	108	670	22	520	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	2.87e-66	108	670	24	521	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|E9R598|FETC_ASPFU	1.44e-61	105	647	19	492	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|P78591|FET3_CANAX	9.68e-61	122	670	37	523	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	5.53e-60	108	659	27	516	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999869	0.000146

TMHMM  Annotations     

Start	End
47	69