CAZyme Information: OAG23014.1

Basic Information

• Species: Alternaria alternata
• Lineage: Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
• CAZyme ID: OAG23014.1
• CAZy Family: GH64
• CAZyme Description: ligninase LG6 precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
294	KV441473|CGC3	30846.47	7.5125

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f	13577	N/A	111	13466

• Gene Location: location=KV441473:252898-253839(-)

Full Sequence      

MRSFAIILIALAASSTSAFDIWPRSSSKCPSVWSDVASELQSDFAGCGADAHGAIRAPFH
DCINNGCDGSLILTDECSRSENAGLSAICKKLKGWSDKYNVAAADMIQFAAATAISACPL
GPRVQALVGRKDSSKAAAVGSVPSSRGTLSSILGAFSAKGFSADDVVALMGTHSVALQFN
DDPSQAGKSLDSTPSTYDNTFYKETKDGTAPYSLQSDVLLSNSSQTAKTWSSFADDADAW
SSAFTGAWNRFAVIGSDASKLQDCSSLIPSSSASKKRQAFNARFTKMMSAKFRV

Enzyme Prediction     

No EC number prediction in OAG23014.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	33	256	2.2e-54	0.9764705882352941

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	6.50e-72	32	264	16	283	Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.
395089	peroxidase	4.11e-30	32	236	1	187	Peroxidase.
173823	plant_peroxidase_like	2.66e-25	34	251	1	253	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
173827	secretory_peroxidase	1.78e-23	26	247	8	274	Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.
173825	ascorbate_peroxidase	1.79e-14	55	247	34	241	Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7013403.1|AA2	1.69e-126	1	293	1	289
QRC96194.1|AA2	3.67e-62	29	281	77	332
CAE7196231.1|AA2	4.56e-59	28	282	72	327
QCC62988.1|AA2	7.83e-56	24	282	52	310
QDS75494.1|AA2	1.78e-50	23	283	109	374

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5ABQ_A	7.25e-36	35	269	22	283	CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-SS. MUTATED RESIDUES T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K AND A314R. [Pleurotus eryngii]
4BLK_A	5.52e-35	35	269	23	284	CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BLL_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM II [Pleurotus ostreatus],4BLN_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM III [Pleurotus ostreatus],4BLX_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM IV [Pleurotus ostreatus],4BLY_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form V [Pleurotus ostreatus],4BLZ_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vi [Pleurotus ostreatus],4BLZ_B Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vi [Pleurotus ostreatus],4BM0_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vii [Pleurotus ostreatus]
4BM1_A	6.23e-35	32	269	17	290	CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BM1_B CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BM2_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Ii [Pleurotus ostreatus],4BM3_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Iii [Pleurotus ostreatus],4BM4_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Iv [Pleurotus ostreatus]
2VKA_A	7.91e-35	35	269	22	283	Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii]
3FM6_A	2.06e-34	35	269	22	283	Chain A, Versatile peroxidase VPL2 [Pleurotus eryngii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9UR19|VPL1_PLEER	1.89e-33	35	269	52	313	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|O94753|VPL2_PLEER	7.13e-33	35	269	52	313	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1
sp|P28314|PER_COPCI	2.84e-29	25	270	38	318	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	2.89e-29	25	270	39	319	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|Q9UVP6|VPS1_PLEER	3.18e-29	32	269	51	320	Versatile peroxidase VPS1 OS=Pleurotus eryngii OX=5323 GN=vps1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000227	0.999780	CS pos: 18-19. Pr: 0.9763

TMHMM  Annotations     

There is no transmembrane helices in OAG23014.1.