CAZyme Information: EDK39262.2

Basic Information

• Species: Meyerozyma guilliermondii
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Meyerozyma; Meyerozyma guilliermondii
• CAZyme ID: EDK39262.2
• CAZy Family: GT15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663		75749.76	5.5234

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MguilliermondiiATCC6260	6062	294746	142	5920

• Gene Location: location=CH408158:168603-170594(-)

Full Sequence      

MPNRALMVRYRNISIIKIKIQVQDPRKRIPNKKKMQVLLLIAFLVSVVTAKTHVYNFNIT
YVTKNPDGLHERRVIGINNEWPIPTIRVKPHDRVVINVDNQLDRNTSLHFHGLFQEKQNF
MDGAEQVTQCPIPPGHKFVYNFTIGDQSGTYWYHSHSGAQYSDGLRGFFIIEDDTLPSHD
EEVSISVSDWYHNEASVIMGKFLNKYNPTGAEPIPQNALVNDTKNMTWTVQPDKTYLVRF
VNMGMFVSQYIYLEGHKMTIVEVDGVRVKPQEVDSLYITVAQRYTVLLHTKDTKENFRFV
NIIDQEMLDVLPEDLEVISTNYLVYDKSSKLPERLTNGPDKFEAAIGKLNPFDDFYLKPL
SKTPLLDDYDYQIELNFTMNNLGDGVNYAFFNNITYVLPKVPTLMSVLSAGKFANNAGIY
GSNTHTYVLQKDEVVEIVLNNMDPGKHPFHLHGHIFQLISRSPEGEDDDNPLVYDETNPE
HNNFPNHPMMRDTVMVNPNGFIVLRFKADNPGVWFFHCHVDWHLEQGLAITLVESPMDIL
AQNSSIPQSHWDACKLSNTISYGNAAGNFGPDESDWLNLSGELVQAKPLPEGFTTKGYVA
FFICTILALFGVYSIYRYGIEDVDTKENEETMRKLYAILSAHQDSDQYSLATREGETEPL
QGH

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	71	412	6.5e-148	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	1.73e-88	42	537	25	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	1.42e-84	370	536	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.
274555	ascorbase	7.42e-77	55	534	4	523	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.
259945	CuRO_2_Fet3p_like	1.32e-74	181	327	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	2.13e-68	37	534	8	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAG88101.1|AA1_2	2.82e-301	33	642	2	612
CCE85919.1|AA1_2	2.41e-293	48	642	16	609
QRG36491.1|AA1_2	1.61e-286	50	646	20	624
QEL59042.1|AA1_2	5.31e-285	50	646	20	624
QEO20037.1|AA1_2	5.31e-285	50	646	20	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	9.54e-195	51	592	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]
5NQ7_A	4.45e-73	54	560	26	513	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
3KW7_A	1.17e-71	54	554	5	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]
5LDU_A	4.11e-71	54	554	5	488	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
1HFU_A	8.82e-71	59	551	11	483	Chain A, LACCASE 1 [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	2.30e-220	38	629	9	588	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	2.27e-209	46	635	21	602	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|P43561|FET5_YEAST	2.42e-201	46	637	14	613	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|P38993|FET3_YEAST	3.87e-201	35	636	6	598	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|K7NCS2|FETC_EPIFE	3.91e-200	41	619	11	575	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
0.658593	0.341409

TMHMM  Annotations     

Start	End
37	59
597	616