CAZyme Information: KIW03356.1

Basic Information

• Species: Verruconis gallopava
• Lineage: Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
• CAZyme ID: KIW03356.1
• CAZy Family: GH28
• CAZyme Description: Peroxidase [Source:UniProtKB/TrEMBL;Acc:A0A0D1XLQ8]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
338	KN847545|CGC2	35875.46	4.7152

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_VgallopavaCBS43764	9871	N/A	53	9818

• Gene Location: location=KN847545:428868-429931(-)

Full Sequence      

MKFSIVALGASLSTTALAFPGMTGGSDDMMNFHKSLIKRAQLGGPHMRRDGTPDLPALNN
VTSTGTGQQIKDCLYGTISCEAAPQKTYVAPALGSKECDSDKCCIWDYVVKDLVTMFTLP
NGQCSELARQAIRLGFHDAGAWSINSGFGGADGSMLISDEVSRPENKGLESIVASGKSLL
AKWNVSAADLVQLMANVATVICPLGPRVLTFIGRPDSADSPTDLLPGPFSDATTLINLFQ
DKTISSDELVALVGAHSTSHQDFVDPSNAGSFQDTTPGVWDTLFYSETANNAFSVSDVTK
FPSDIALSKDARTSGVWGAMTNQRTWNAACTSYLSICF

Enzyme Prediction     

No EC number prediction in KIW03356.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	109	324	9.4e-51	0.9058823529411765

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	2.10e-84	94	329	6	262	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	8.29e-24	132	265	20	160	Peroxidase.
173823	plant_peroxidase_like	1.33e-22	132	321	22	236	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-15	132	329	37	270	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	8.25e-15	132	310	34	217	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
QDS72918.1|AA2	8.76e-101	1	327	1	325
QLI65955.1|AA2	4.14e-77	1	329	1	324
QRD06638.1|AA2	6.53e-76	54	327	50	330
UPX44932.1|AA2	4.43e-75	63	289	29	262
CAE7175176.1|AA2	2.05e-74	54	328	49	330

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FNB_A	1.07e-36	103	324	14	251	Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii],5FNB_B Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii]
5FNE_A	4.08e-36	103	324	14	251	Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37k, H39r & G330r [Pleurotus eryngii]
3FMU_A	7.95e-36	103	324	14	251	Chain A, Versatile peroxidase VPL2 [Pleurotus eryngii]
5ABN_A	7.95e-36	103	324	14	251	CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi. MUTATED RESIDUES D69S, T70D, S86E, D146T, Q202L, H232E, Q239R AND S301K. [Pleurotus eryngii]
4BLK_A	8.11e-36	103	324	15	252	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9UR19|VPL1_PLEER	2.02e-34	103	324	44	281	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|O94753|VPL2_PLEER	2.81e-34	103	324	44	281	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1
sp|Q9UVP6|VPS1_PLEER	8.95e-32	100	322	42	286	Versatile peroxidase VPS1 OS=Pleurotus eryngii OX=5323 GN=vps1 PE=1 SV=1
sp|P28314|PER_COPCI	7.61e-29	94	322	33	283	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	1.07e-28	94	322	34	284	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000364	0.999615	CS pos: 18-19. Pr: 0.9759

TMHMM  Annotations     

There is no transmembrane helices in KIW03356.1.