CAZyme Information: PWY65599.1

Basic Information

• Species: Aspergillus heteromorphus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
• CAZyme ID: PWY65599.1
• CAZy Family: AA1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
544	MSFL01000051|CGC1	61585.50	4.6653

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55	11436	1448321	306	11130

• Gene Location: location=MSFL01000051:120990-122697(+)

Full Sequence      

MIRTLLTLALYGLVQDTLAKDVYLDWNITWVTAAPDGYARPVIGINGQWPCPQIDVSVGD
NLVVDVYNALGNQSTGIHWHGLHQNYNGYMDGAPGVTQCELRPHQRMRYVVPMNQTGTYW
YHSHETGQYPDGLRGPIVVHDTVPLPFEYDEEITLTLTDWYHVQMPQLVSEFEAPSEYAS
VGGQEPLPDAVLFNDAFGTKIKVKPSTTYLIHVVCMGNWAGHALIIDDHDMTIVGADGIG
IEPHFLTPQYIRMTVGQRLDILLTTKDDTSRNYPIWDGLDIDEMFKQENRSIPDGYNPNG
TAWLTYDDSLPFPPMPDIHIGNASLDFLDDVTLQPRDRLPLIEPVDLQIILDTDATTLDG
KPAYTINNMTYKTPNEPTLYTAIAADPETAMDPSIYGEVNPFVVNYGDVVEIVLNNHHTN
LHPWHLHGHDFQIVQRTYPYGGFFNGYGNVSSHPMRRDTIMVEPKGHFVIRFRAMNPDNL
QRSSTDQYIRIWMLHCHVEWHVEVRLMAIIIEAPDRLQNLTVPTDHQEICGGAPSHWAPL
PPLY

Enzyme Prediction     

No EC number prediction in PWY65599.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	385	4.8e-117	0.9851632047477745

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	1.57e-63	22	514	36	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	2.54e-62	24	520	4	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.
259920	CuRO_1_Fet3p	1.61e-56	22	140	1	121	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.
259966	CuRO_3_Fet3p	1.90e-56	344	514	3	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	5.61e-55	26	517	28	551	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK42098.1|AA1_2	0.0	1	542	1	545
BCS11789.1|AA1_2	0.0	1	542	1	531
BCR99488.1|AA1_2	3.24e-300	1	478	1	478
ACJ13061.1|AA1_2	3.48e-227	8	541	3	535
AHA42447.1|AA1	5.83e-227	8	541	7	539

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.89e-101	25	530	6	500	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	2.92e-49	25	530	7	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5ANH_A	1.04e-47	25	530	7	485	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]
2HRG_A	1.44e-47	25	530	7	485	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
6H5Y_A	5.25e-47	25	530	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|Q4WZB4|ABR1_ASPFU	2.08e-227	8	541	7	539	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2
sp|E9R598|FETC_ASPFU	3.60e-133	14	530	15	511	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	4.43e-133	6	530	7	514	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	3.81e-125	25	533	28	518	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|W3X7K0|PFMAD_PESFW	7.32e-115	7	530	8	507	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000233	0.999746	CS pos: 19-20. Pr: 0.9765

TMHMM  Annotations     

There is no transmembrane helices in PWY65599.1.