CAZyme Information: AEO59029.1

Basic Information

• Species: Thermothelomyces thermophilus
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Thermothelomyces; Thermothelomyces thermophilus
• CAZyme ID: AEO59029.1
• CAZy Family: GH43
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362	CP003005|CGC31	38179.17	5.1608

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TthermophilusATCC42464	9292	573729	195	9097

• Gene Location: location=CP003005:2662397-2663581(+)

Full Sequence      

MKIRYVFLLFLGLASPGVSRTLLGMNKSLAGEISPAAAKRQTGELLADLSTLPDAALSPA
GWTIKNILLGNRAAVSPQDLTTVYTAPGPLDSSECRRETCCVWKYIADAMATSFRDGAGR
CNELARQAVRLGFHDAGTWSKSAGGGGADGSVLLAPSELARDDNRALEVVAAQMAAWYAE
WRPRGARMADLIQMGAVVAAASCPLGPRARAFVGRNDSATPAPPDRLPSAANSDAAALAA
LFADKTLSLGELVALVGAHTTSVQRFFDPLAAGSPQDSTPGVWDTLYYNQTASSDPPQGV
FRFPSDLALSQYPPARELWQTFANAQAVWNDDFAAAYVHLSVLGVEHINDLTECTGVLPL
SG

Enzyme Prediction     

No EC number prediction in AEO59029.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	105	345	2.9e-52	0.984313725490196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	2.87e-74	100	359	14	288	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	6.00e-20	108	341	1	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	1.92e-12	129	347	34	252	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.
173827	secretory_peroxidase	1.77e-09	245	345	153	283	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.
178467	PLN02879	5.94e-09	129	344	38	246	L-ascorbate peroxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO59029.1|AA2	1.52e-261	1	362	1	362
UNI21317.1|AA2	1.66e-99	44	360	35	350
UQC76336.1|AA2	2.33e-98	13	359	11	361
QLI65955.1|AA2	4.14e-98	33	360	26	352
QDS77259.1|AA2	7.91e-98	13	359	17	359

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LY8_A	9.23e-33	85	359	10	297	Chain A, Peroxidase [Coprinopsis cinerea],1LY8_B Chain B, Peroxidase [Coprinopsis cinerea]
3Q3U_A	5.96e-31	96	359	11	289	Trametes cervina lignin peroxidase [Trametopsis cervina]
1LYK_A	1.26e-30	85	359	10	297	Chain A, Peroxidase [Coprinopsis cinerea],1LYK_B Chain B, Peroxidase [Coprinopsis cinerea]
1LY9_A	1.74e-30	85	359	10	297	Chain A, Peroxidase [Coprinopsis cinerea],1LY9_B Chain B, Peroxidase [Coprinopsis cinerea],1LYC_A Chain A, Peroxidase [Coprinopsis cinerea],1LYC_B Chain B, Peroxidase [Coprinopsis cinerea]
1ARP_A	1.77e-30	85	359	11	298	Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 angstroms resolution: structural comparisons with the lignin and cytochrome C peroxidases [Penicillium janthinellum],1ARU_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARV_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARW_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARX_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARY_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1C8I_A BINDING MODE OF HYDROXYLAMINE TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1CK6_A BINDING MODE OF SALICYLHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1GZA_A PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1GZB_A PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1HSR_A BINDING MODE OF BENZHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],2E39_A Crystal structure of the CN-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus'],2E3A_A Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus'],2E3B_A Crystal structure of the HA-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus']

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28314|PER_COPCI	9.15e-30	85	359	30	317	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	1.29e-29	85	359	31	318	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|A8NK72|PER_COPC7	3.35e-29	85	359	30	317	Peroxidase OS=Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) OX=240176 GN=CIP1 PE=3 SV=1
sp|Q9UR19|VPL1_PLEER	1.02e-25	100	359	44	313	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|O94753|VPL2_PLEER	1.94e-25	100	359	44	313	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.082693	0.917274	CS pos: 20-21. Pr: 0.7058

TMHMM  Annotations     

There is no transmembrane helices in AEO59029.1.