CAZyme Information: EJT71865.1

Basic Information

• Species: Gaeumannomyces tritici
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
• CAZyme ID: EJT71865.1
• CAZy Family: CE1
• CAZyme Description: galactose oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
809		85565.03	6.2395

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1	14749	644352	291	14458

• Gene Location: location=GL385400:2187218-2189647(+)

Full Sequence      

MPAPAVLRAVGLGAALLSHMRPVAAQNIVANLTSCLESETIWTTAEQISFSICDGTTYQA
GGKSLQIIEDVCGTRECVGYCHENPKCVLAFYDKEARTCHIKDSESGEDHIWAQDSNCDA
IRKLPPDAGSGGGNSGDNTSPTSSALPTAAPTAAPTTSSSAASSAAPTTTSSTAPIASPP
TSVPGTPGKEPVIPPVNGNDLQDGAFLASCPGQQTEFKGANAKYLICPGSDYDGKTERVF
NGVASAQACAEACANAKDCKKAAYDSQTKDCHVKGAEPRYSLFLVKAQHYTTIRVEAALD
ASKVGRWSDLIRFPVIPVAAYVVPSFPEPSKLMFFSSWGVDAFGGPSGLTQFGSFDLKTG
AVSQREISNTKHDMFCPGISALADGRILVQGGSDAAAVSVYDPATDSFSRVQDLKMARGY
QSSVTLSDGRVFTVGGAYSGARAGKNGEVYDADANTWSALSDADVKPMLTKDHEGIWRED
NHAWLFSWRQGSVFQAGPSKKQHWYGTKGYGAIVEAGTRDDVDAMCGTFVMYDATAGKIL
TAGGAQDYDKSDGNTHAHITTIGEPGTRSNVERVGDMAFPRAFANTVVLPDGRVIVTGGQ
RKALVFTNTDGILIPEVFDPASKTWSQMAPMAVPRNYHSVSILLPDATVFVGGGGLCYVN
KIKGSSARCDKTVDHADGEIFEPPYLFKADGSRADRPAIANLERERVNAGETLVFSVGGA
ENVKDCKFSLVRVGTVTHSVNTDQRRVPLTDINVRADGKVEAKLPADYGVLTPGFWYLFA
MSPSGVPSVARTVQVTLTAKAKAKVALWG

Enzyme Prediction     

EC	1.1.3.9:34	1.1.3.13:3	1.1.3.-:1	1.1.3.7:1	1.1.3.47:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA5	244	795	1.6e-219	0.9047619047619048

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
199882	E_set_GO_C	6.92e-26	691	795	1	103	C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
401164	DUF1929	3.22e-23	707	795	6	91	Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase.
276965	Kelch	6.59e-12	380	462	6	90	Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.
276965	Kelch	3.24e-11	380	462	53	137	Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.
276965	Kelch	5.83e-09	572	654	39	112	Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGI66562.1|AA5_2	4.28e-295	30	797	20	710
QGI97452.1|AA5_2	4.28e-295	30	797	20	710
QGI83803.1|AA5_2	6.07e-295	30	797	20	710
QKD57968.1|AA5_2	2.45e-294	30	797	20	710
CCT70837.1|AA5_2	2.45e-294	30	797	20	710

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RYV_A	2.11e-287	32	797	4	691	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001],6STX_C Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
6RYW_A	8.53e-287	32	797	4	691	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
6RYX_A	1.21e-286	32	797	4	691	Copper oxidase from Colletotrichum graminicola [Colletotrichum graminicola M1.001]
2EIC_A	3.10e-151	265	796	108	638	Chain A, Galactose oxidase [Fusarium graminearum]
1GOF_A	4.37e-151	265	796	108	638	NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],1GOG_A NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],1GOH_A NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],2EIE_A Chain A, Galactose oxidase [Fusarium graminearum],2JKX_A Chain A, GALACTOSE OXIDASE [Fusarium graminearum],2VZ1_A Chain A, GALACTOSE OXIDASE [Fusarium graminearum],2VZ3_A Chain A, Galactose Oxidase [Fusarium graminearum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0CS93|GAOA_GIBZA	7.88e-150	265	796	149	679	Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA PE=1 SV=1
sp|I1S2N3|GAOA_GIBZE	1.57e-149	265	796	149	679	Galactose oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GAOA PE=3 SV=1
sp|Q9FYG4|GLOX1_ARATH	4.87e-15	577	795	392	614	Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
sp|Q3HRQ2|GLOX_VITPS	6.68e-15	356	795	80	521	Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
sp|A0A2H4HHY6|GLOX_ARTAN	2.69e-06	576	795	374	593	Putative aldehyde oxidase Art an 7 OS=Artemisia annua OX=35608 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.855116	0.144901

TMHMM  Annotations     

There is no transmembrane helices in EJT71865.1.