CAZyme Information: ASPCADRAFT_207607-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_207607-t33_1-p1
• CAZy Family: GH28
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
451		50097.32	4.2035

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907500:140161-141516(+)

Full Sequence      

MTDWYHELTQEIAPTFITVDNPTGAEPIPDSFLFNDTLNTKIPVEAGKTYLLRLINIGAF
VAQYFYIEDHTMRIVEIDGIYTDAAEADILYISAAQRYSVLVTMKNSTEKNYPIVTVADS
VLLDTIPSDLKLNQTNWLEYNSSASFPQAVMTVSDCSDLNPYDDMSLVPYDKMPLLEDPD
VSLELTVTMQVLDNGADYAFLNDISYTKPKVPALYTVMSAGSLATDATVYGDYTHSVVLD
EDQVVEIILNNGDTGTHPFHLHGHAFQMIDRFPSYGAHFYDYADGDPVTYNASNHSTFPA
YPARRDTFVLPPQGYFVIRFKADNPGVWFFHCHIDWHLAQGLAMVFIEAPLAIQERVTIP
QQHYDVCEAAGIAYEGNAAANTEDYTDLSGQNKQIAWLPGGFTARGIVALVFSCVSAFLG
MGMIAFYGLSDIKKGAQGPIALREEVREHAD

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	221	4e-81	0.6409495548961425

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	3.09e-78	180	350	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	2.35e-70	1	142	7	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.
400194	Cu-oxidase_2	1.95e-47	206	350	1	136	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259977	CuRO_3_MCO_like_4	1.87e-45	185	348	3	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.
225043	SufI	5.07e-44	1	350	166	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK37140.1|AA1_2	2.52e-301	1	451	163	613
BCS08533.1|AA1_2	1.23e-299	1	451	164	614
QKX63715.1|AA1_2	9.30e-234	1	433	162	596
QSS50310.1|AA1_2	1.67e-227	1	433	159	592
QQK44081.1|AA1_2	4.50e-225	1	432	163	594

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	7.07e-144	1	401	139	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]
1GYC_A	1.88e-35	1	381	148	498	Chain A, LACCASE 2 [Trametes versicolor]
1V10_A	7.73e-34	1	348	169	489	Chain A, Laccase [Rigidoporus microporus]
3KW7_A	4.12e-33	1	367	148	491	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]
5E9N_A	1.86e-32	1	383	149	504	Steccherinum murashkinskyi laccase at 0.95 resolution [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	3.97e-167	1	432	160	576	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	2.78e-159	1	432	160	582	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|I1RMG9|FET3_GIBZE	5.44e-156	1	430	162	578	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	9.56e-155	1	437	160	591	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|K7NCS2|FETC_EPIFE	3.99e-153	1	441	160	588	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000001

TMHMM  Annotations     

Start	End
407	429