dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: XP_001912809.1

You are here: Home > Sequence: XP_001912809.1

Basic Information help

Species

Podospora anserina

Lineage

Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina

CAZyme ID

XP_001912809.1

CAZy Family

GT3

CAZyme Description

Peroxidase [Source:UniProtKB/TrEMBL;Acc:B2AB29]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
423	CU633438\|CGC15	46811.94	9.9056

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in XP_001912809.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA2	162	402	6.5e-49	0.9764705882352941

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	4.35e-100	143	418	3	289	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.
173823	plant_peroxidase_like	2.24e-25	172	399	9	254	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.
173825	ascorbate_peroxidase	1.94e-18	185	403	34	250	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.
395089	peroxidase	3.66e-18	179	379	14	185	Peroxidase.
178467	PLN02879	4.33e-13	165	402	8	246	L-ascorbate peroxidase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
8.11e-317	1	423	1	423
1.24e-265	60	423	1	364
3.48e-119	73	420	3	367
2.75e-115	104	419	99	419
1.92e-106	75	417	8	349

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.63e-31	147	417	6	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]
5.79e-30	155	417	20	297	Chain A, Ligninase H8 [Phanerochaete chrysosporium RP-78]
2.09e-29	155	417	20	297	Chain A, PROTEIN (RECOMBINANT LIGNIN PEROXIDASE H8) [Phanerodontia chrysosporium],1B80_B Chain B, PROTEIN (RECOMBINANT LIGNIN PEROXIDASE H8) [Phanerodontia chrysosporium]
2.88e-29	155	417	20	297	Chain A, Ligninase H8 [Phanerodontia chrysosporium],1B85_B Chain B, Ligninase H8 [Phanerodontia chrysosporium]
3.83e-29	152	417	10	283	CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-br. MUTATED RESIDUES T2K, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R, A309K AND A314R. [Pleurotus eryngii]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.24e-29	156	417	41	319	Ligninase C OS=Trametes versicolor OX=5325 PE=1 SV=2
4.18e-29	155	417	40	316	Ligninase LG5 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG5 PE=2 SV=1
1.52e-28	155	417	41	318	Ligninase H8 OS=Phanerodontia chrysosporium OX=2822231 GN=LPOA PE=1 SV=1
1.01e-27	155	417	41	318	Ligninase LG2 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG2 PE=1 SV=1
1.19e-27	147	417	23	313	Ligninase-3 OS=Phlebia radiata OX=5308 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000047	0.000000

TMHMM Annotations help

There is no transmembrane helices in XP_001912809.1.