CAZyme Information: QYA_200248.P249

Basic Information

• Species: Mucor lusitanicus
• Lineage: Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor lusitanicus
• CAZyme ID: QYA_200248.P249
• CAZy Family: GT35
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
591	McirCBS277-49_SC03|CGC3	66018.19	4.5058

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MlusitanicusCBS277-49	11852	747725	0	11852

• Gene Location: location=McirCBS277-49_SC03:1901639-1903922(-)

Full Sequence      

MKCFATLSCALAAAAALSLSSVVAERVVYDWHLGYKHVNPDGLHQRRVISINDQWPPAPV
KLNINDTLVIHVHNKLNEPTVIHAHGINQNNRTNIYDGAGMVTQCPIPPNYDFTYEFPVT
QAGTFWIHSHFKVQYMDGLRVPLVVYDSNEPFEYDQDEIITVSDWYHEDSYTNLEQYMNE
DNLDGVEPIPQSGLINDHVNATFHFKPGKTYRLRIINVSGIATFGVSIDDHDMQVIEVDG
VRTQAKPVRSVYMAAGQRVSVLVKTKNTTDRNYRLHANMAPVMFDYIPDDLQMDIEAPIY
YDESKPFAPRDDPSLKKGDYDDAFTPPLIEAPALKVDRQVNFTIDFMENTDGLNHGVING
IPYLTPLVPSLHTLLSVGEYANNSAVYGPQSITHMFELNEVVELVINNLDDGPHPFHLHG
HAFQVIARGSGVYSNQTIDIPSNPTYRDTIGVPSEGYIVIRFRADNPGVWFFHCHVDWHL
PAGLAATFITAPELAQETMTLPQEWIDMCIAAGQPGTGNAAGKEGLDLDGAPDGVRPIQS
TLMMSALIATLVGMSTVIWHVWVDPGADDDEDEDDEQIKMDKKPLLQDQQD

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	45	379	7e-119	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.76e-74	29	488	4	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.
225043	SufI	4.26e-73	51	493	57	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	2.21e-70	337	492	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.
215324	PLN02604	1.15e-63	29	488	27	544	oxidoreductase
259945	CuRO_2_Fet3p_like	7.71e-61	156	303	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS03778.1|AA1_2	2.58e-207	24	565	17	567
CDS09935.1|AA1_2	5.14e-204	24	565	25	572
CDS12866.1|AA1_2	5.61e-155	17	535	13	542
AHZ58332.1|AA1_2	7.85e-141	11	574	9	598
AHZ58331.1|AA1_2	1.11e-140	11	574	9	598

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.33e-110	25	521	1	512	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	8.76e-67	17	509	13	508	Chain A, Laccase [Rigidoporus microporus]
1HFU_A	1.15e-65	37	509	15	487	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.18e-65	37	509	15	487	Chain A, Laccase [Coprinopsis cinerea]
1KYA_A	1.47e-65	38	509	15	488	Chain A, Laccase [Trametes versicolor],1KYA_B Chain B, Laccase [Trametes versicolor],1KYA_C Chain C, Laccase [Trametes versicolor],1KYA_D Chain D, Laccase [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	5.92e-136	17	560	13	571	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	2.92e-135	29	560	27	575	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|K7NCS2|FETC_EPIFE	1.27e-130	11	560	7	574	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|P43561|FET5_YEAST	3.98e-129	17	562	11	587	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|Q4PIF8|FER1_USTMA	1.94e-128	24	562	29	615	Iron multicopper oxidase fer1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=fer1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000253	0.999734	CS pos: 24-25. Pr: 0.9709

TMHMM  Annotations     

There is no transmembrane helices in QYA_200248.P249.