CAZyme Information: SPBR_02574-t41_1-p1

Basic Information

• Species: Sporothrix brasiliensis
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix brasiliensis
• CAZyme ID: SPBR_02574-t41_1-p1
• CAZy Family: GH11
• CAZyme Description: ferrooxidoreductase Fet3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
618	AWTV01000006|CGC25	68035.39	4.3335

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=AWTV01000006:1154882-1156738(+)

Full Sequence      

MVRAFVAGLLALAAGAVAETINLDFNVSWVMANPDGLADRKVIGINGEFPLPLINVTKGD
RLVVNMYNGLGDKSTSIHWHGMFQNGTNSMDGASMFTQCPIPPGSSFTYNFTVEQTGTYW
YHCHTDYCYPDGYRQALIVHDPEAPFYNDYEEEFVMTLSDWYHDLMEDLSTQFLSLYNPT
GAEPVPNSFLMNDGQNQTFHVKPNTTYLLRIINSGNFIAQYFYIEGHNFTIVEVDGVYTE
PQEASTLYVAIAQRYSVLLTTANSTEVNYKIVTVADSDLMDTIPSNLQLNQTNWLVLNEN
APLEQAVVTAATSDDIVAFDDFTLVPSDRMALLPEPDIQINVTVYMVNLINGFNYAELNN
ITYTIPKVPSLYTALSAGDLRTSEVVYGEYTHPIVLGHNQVVEIVLNNGDTGSHPFHLHG
HTFQVINREPPIGPDFNSYRDGDPVAYDANNHTDFPPIPIRRDTVVLPPQGFVVMRFVAD
NPGVWAFHCHIDWHMASGLAMTFVEAPELIPTHVEVPDDHYAACAAAAVPTVGNAAANAQ
NFLDLTGQNAQPKDIPDGFTPRGIVAMTFTVLSAVLGIISIIYYGLADLKHAPKSAPAAR
DSSEGENAVTTTSMPKHG

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	379	6.3e-144	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.41e-83	23	510	4	528	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	1.79e-79	23	508	38	451	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].
259966	CuRO_3_Fet3p	1.69e-76	337	507	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.
259945	CuRO_2_Fet3p_like	9.53e-72	152	299	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.
177843	PLN02191	2.19e-71	42	519	44	557	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX63715.1|AA1_2	3.34e-297	18	603	23	618
UKZ96021.1|AA1_2	1.76e-296	10	609	7	605
AYD59708.1|AA1_2	4.25e-290	10	612	7	608
QYT00246.1|AA1_2	4.02e-288	10	612	7	608
CAK97337.1|AA1_2	3.33e-286	9	608	9	609

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	7.12e-183	19	558	1	534	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]
1V10_A	9.81e-72	10	511	13	495	Chain A, Laccase [Rigidoporus microporus]
3KW7_A	6.40e-71	24	505	7	472	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]
5Z1X_A	4.39e-67	34	505	17	465	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
1GYC_A	6.90e-66	28	505	7	469	Chain A, LACCASE 2 [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	2.29e-223	18	604	20	591	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|K7NCS2|FETC_EPIFE	3.18e-213	16	587	18	577	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	4.11e-206	10	605	14	592	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|P38993|FET3_YEAST	5.04e-195	16	592	19	589	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|P78591|FET3_CANAX	1.25e-192	18	591	21	584	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000268	0.999711	CS pos: 18-19. Pr: 0.9801

TMHMM  Annotations     

Start	End
564	586