CAZyme Information: SAPIO_CDS8659-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS8659-t41_1-p1
• CAZy Family: GT2
• CAZyme Description: Iron transport multicopper oxidase FET3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
566		63159.14	5.4994

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462	10920	N/A	2544	8376

• Gene Location: location=JOWA01000121:2207752-2209786(-)

Full Sequence      

MRGPAFGLLLPGILAGVASAATVEYDWDITWLNAAPDGFQRPVIGVNNQWPCPEIRATKG
DTIRVKMNNKLGNQTTSLHFHGINQVSTNWMDGPSLATQCPVPPGESIVYEFLADEAGTF
WWHSHNMAQYPDGLRAPLIIEDPNDPYKDEYDEEYILTISDWFLEEALILGKRLLSSNNT
FGAPPAPNSILLNDGQGADYPFEVGKNYRFRIINMGASNNAMIHFDSHDMNVIMNDAAYV
QQEIAYQLHVTPAQRYDVIIKGIERDNRNFGILVSLDRNRDYTAVTPKPVWPLNATAYLV
LDPEGERRPDVVDVWRPFDDAHFKPLQGDILPPADKTLVFNFQTCKDKYGIVRHCVNGSP
YVPAKVPTLYTAATTGNFNTNETVYGAVHPFIVSYGDIVDIVVNNHDGSIHPFHLHGHHF
QVLSRPQTNGGDWPGPDHAGGYNPKPPRRDTVNVFPKSHAVLRFEANNPGVYLFHCHIEW
HVEMGLTATIIEAPDMLRDITIPKDHIEACKKAGVPFEGNAGGNVEDPLDTSNIDYEPPL
EYVGAQWTPTSPPACRVKRSRIGRLL

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	377	2.8e-110	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	6.70e-72	37	494	48	450	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].
274555	ascorbase	2.19e-69	22	500	1	531	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.
259966	CuRO_3_Fet3p	1.08e-67	333	494	1	160	The third 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 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	2.29e-63	8	500	9	554	L-ascorbate oxidase
259920	CuRO_1_Fet3p	1.26e-61	23	140	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
URF33722.1|AA1_2	1.81e-247	9	551	5	548
UQC85338.1|AA1_2	4.41e-245	15	556	11	553
VBB75073.1|AA1_2	9.09e-230	20	565	20	566
AUS45867.1|AA1_2	1.47e-229	14	562	14	554
CDP25016.1|AA1_2	1.83e-229	15	565	15	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.29e-105	22	530	2	520	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]
4JHU_A	4.40e-63	35	510	16	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5EHF_A	2.37e-62	26	520	7	496	Laccase from Antrodiella faginea [Antrodiella faginea]
5NQ7_A	2.72e-62	14	510	15	507	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
6H5Y_A	3.24e-62	28	510	7	485	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X7K0|PFMAD_PESFW	3.46e-207	20	547	20	544	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	2.19e-154	17	538	17	542	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	8.90e-149	8	538	6	539	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	1.46e-137	14	530	16	535	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|Q4WZB4|ABR1_ASPFU	1.33e-127	9	553	7	550	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000272	0.999685	CS pos: 20-21. Pr: 0.9744

TMHMM  Annotations     

There is no transmembrane helices in SAPIO_CDS8659-t41_1-p1.