CAZyme Information: VDB93858.1

Basic Information

• Species: Blumeria graminis
• Lineage: Ascomycota; Leotiomycetes; ; Erysiphaceae; Blumeria; Blumeria graminis
• CAZyme ID: VDB93858.1
• CAZy Family: GT39
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
591		65711.42	4.9891

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BgraminisTritici96224	8470	1268274	123	8347

• Gene Location: location=LR026992:17355119-17357157(+)

Full Sequence      

MSLLLLVLLSSIISIQAETQVYNFNITWVRANPDGAFERPTIGINNKWPPPIIQTVKGDQ
VIVNVENQLGNQTTTLHFHGLHHNGTANMDGAAQVTQCGIAPGARFTYNFTANQAGTYWY
HSHDKGQYPDGLRAPFIITDPESPYQADEEVILSVSDWYHEEMTTIIPRFLEKTNPTGAE
PVPQAALINDTQNLMISIQPEKTYLFHLINMGAFAGQYIWFEGHNMTVVEVDGVATIPVE
VNRLYISAGQRYSFLLRTKAESSTNYAFVASMDTDLFDILPDNLIWNSTGYLVYDKEKPI
PQPATVQTLDFFDDLNLIPLDKMPLLPPPDKSIVLDVIMGNLENGRSYSFFNNITYTHPK
VPTLYTLMSSGSLATDSRIYGQFTHSYIIDRMQTIEIVINNLDDGKHPFHLHGHNFQTLV
RSGDGSGKFDPTSVTQAEYPTIPMRRDTVLLHPHGHMVIRFRADNPGVWMFHCHIEWHMA
QGLSATLIEAPLDVQKQLTISENHFDNCRHRGIPIAGNAAANTVDLLNLDGANVAPGPLP
AGFTDRGIVAMSFSCLAAILGLIVISWYGLADMGEVSMHEDQSPCVGEEGT

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	371	3.3e-147	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	1.11e-78	330	491	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	2.23e-76	22	490	4	524	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	2.10e-74	16	491	32	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].
259945	CuRO_2_Fet3p_like	8.41e-73	149	296	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	1.44e-69	17	489	21	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VDB93858.1|AA1_2	0.0	1	591	1	591
ATZ46936.1|AA1_2	1.03e-295	16	587	23	596
QSZ34526.1|AA1_2	1.73e-290	16	589	23	598
APA05965.1|AA1_2	7.70e-286	16	587	23	584
QLI66871.1|AA1_2	2.01e-262	17	575	20	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.51e-182	18	542	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]
3KW7_A	9.07e-72	21	508	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]
1GYC_A	4.69e-70	32	508	16	488	Chain A, LACCASE 2 [Trametes versicolor]
2QT6_A	8.95e-70	17	489	6	468	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
2XYB_A	1.31e-67	21	508	5	486	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	1.94e-259	7	571	10	577	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	3.19e-253	3	571	6	574	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	6.14e-251	16	577	21	585	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	2.60e-198	7	588	10	607	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	1.97e-192	12	575	12	588	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999772	CS pos: 17-18. Pr: 0.9800

TMHMM  Annotations     

Start	End
548	570