CAZyme Information: EKG20109.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG20109.1
• CAZy Family: GT1
• CAZyme Description: Fungal lignin peroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
312	AHHD01000096|CGC1	32870.94	5.0982

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

• Gene Location: location=AHHD01000096:70970-72048(+)

Full Sequence      

MLFSKSSIFLLSTAASVQALSLSDVSSAASVLKREASGLGNNLLSLVHRRDSCPDVWQKV
ASELKGWFLDGSVCSDDARAAIRLSFHDCFSGGCDGSIILAHEYTRSDNAGLADFAMKLA
PLADQYEVGTADLIQFAGALATATCPLGPRIAVKVGRQDSSTPSAEGQLPSSRSSASVLI
DQFAAKGFSEIDLVALVGAHSTAKQFFDQPDKAGQSLDSTPGTWDTNFYRQTTLGTAPVT
LESDKNLATDLRTAVQWTAFNAQGVWAAAYVSAMNKMTVLGNDVSSLTDCTSVISAATSK
RDIKAAPIADRI

Enzyme Prediction     

No EC number prediction in EKG20109.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	57	282	2.4e-55	0.9921568627450981

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	1.23e-76	52	307	2	300	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.
173827	secretory_peroxidase	6.24e-32	50	277	8	278	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.
173823	plant_peroxidase_like	1.44e-31	82	278	22	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.
395089	peroxidase	5.50e-31	60	260	1	184	Peroxidase.
173825	ascorbate_peroxidase	2.70e-22	51	200	7	162	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
CAE7196231.1|AA2	7.68e-83	53	312	73	333
QRC96194.1|AA2	2.24e-80	50	312	74	337
QCC62988.1|AA2	2.00e-73	6	311	4	315
CAE7013403.1|AA2	6.97e-70	52	312	24	284
QDS68272.1|AA2	2.35e-64	53	301	152	410

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LY8_A	3.87e-36	56	308	24	307	Chain A, Peroxidase [Coprinopsis cinerea],1LY8_B Chain B, Peroxidase [Coprinopsis cinerea]
5ABQ_A	6.11e-35	60	294	20	282	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]
1LYK_A	7.78e-35	56	308	24	307	Chain A, Peroxidase [Coprinopsis cinerea],1LYK_B Chain B, Peroxidase [Coprinopsis cinerea]
1LY9_A	1.09e-34	56	308	24	307	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	1.11e-34	56	308	25	308	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|Q96TS6|PEM3_PHLRA	5.76e-34	49	294	22	313	Manganese peroxidase 3 OS=Phlebia radiata OX=5308 GN=mnp3 PE=2 SV=1
sp|P28314|PER_COPCI	5.87e-34	56	308	44	327	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	8.33e-34	56	308	45	328	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|A8NK72|PER_COPC7	2.21e-33	56	308	44	327	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	1.57e-31	46	294	26	312	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.222577	0.777418	CS pos: 19-20. Pr: 0.7100

TMHMM  Annotations     

There is no transmembrane helices in EKG20109.1.