CAZyme Information: SPBR_02475-t41_1-p1

Basic Information

• Species: Sporothrix brasiliensis
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix brasiliensis
• CAZyme ID: SPBR_02475-t41_1-p1
• CAZy Family: CE9
• CAZyme Description: iron transport multicopper oxidase fet3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
678		74245.93	6.3601

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sbrasiliensis5110	9231	1398154	140	9091

• Gene Location: location=AWTV01000006:2792896-2794994(-)

Full Sequence      

MPDDTSEQGDRLLRPPLDHVHEWRAGEDGPGAQETGSDSDEEHAQWPPESRRPPSRWQRL
CRALATVRQIVMPALAILTALAVVMALFLLLTGGSLSMPAYDTDTNAPKARPTAKDPVIV
LHPEDHIHREPQTIHLSWNITKSRIAPDGVFRDVVLINGEFPGPTIEARTGDTLVVTVTN
SLVDEGLSLHWHGLHMRGANHMDGPVGVTQCAIPANGGSFVYQVPTGDQAGTFWYHSHSE
MQRADGLYGGLVVHAPTDTPAAAAVDKEILLLVGDWYQFSGKTVFAEFQDPTSNGNEPVP
GSVLINGRGAFDCGRATKAAPVDCHAVELPPLRLDTRLRYRVRLVNVGVLTGISTTVPDA
RIDVLTVDGGLPVVLPDDAKAVAANSIGVVYPAQRVDYVLSWPDAGATGDGTQLVVTVDG
EYYVGNWQDPPSQTFAIGAAPSTQRRATRPVQRAASPPPPSSQATRAVDLRTVRGTALGT
PLPPPDRLYMIFAVVEILSHNRFIPKGYINHTMWVPQERPLLSLDRSAWDSHQLVPWTGA
APAWVELTINNIDTQGHPFHLHGFDFYVVGSHEGLGGWDYYNPFFVPWKPPRGGPMNTLD
PVLRDTVYVPPYGYVILRFRADNEGIWVLHCHILWHQASGMNMAFQVLGHSEHGLGGTPQ
SFRAAEYCRTRKEKHPHL

Enzyme Prediction     

No EC number prediction in SPBR_02475-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	150	642	3.7e-82	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.12e-62	135	645	3	521	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.
259977	CuRO_3_MCO_like_4	2.44e-59	489	647	1	166	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.
177843	PLN02191	3.48e-58	137	645	27	544	L-ascorbate oxidase
259869	CuRO_1_LCC_like	8.81e-53	135	254	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.
215324	PLN02604	2.96e-52	130	646	21	545	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI63946.1|AA1	6.43e-143	103	647	63	625
UPX44859.1|AA1	2.38e-139	113	668	72	648
UPK99837.1|AA1	1.61e-138	119	647	84	600
UNI19384.1|AA1	1.90e-135	93	647	146	710
UKZ91860.1|AA1	4.53e-135	119	669	84	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.54e-52	139	645	73	540	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	4.00e-52	139	645	73	540	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]
6F5K_A	6.70e-51	146	645	48	517	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
1AOZ_A	5.47e-50	132	645	2	521	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]
3KW7_A	3.57e-48	140	645	10	470	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	3.00e-62	133	645	22	493	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q55P57|LAC1_CRYNB	1.57e-61	99	662	27	574	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	1.05e-59	99	640	27	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
sp|J9VQZ4|LAC2_CRYNH	1.32e-55	98	640	26	553	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|I1RMG9|FET3_GIBZE	7.66e-55	144	645	35	494	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999863	0.000133

TMHMM  Annotations     

Start	End
70	92