dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: I308_04698-t35_1-p1

You are here: Home > Sequence: I308_04698-t35_1-p1

Basic Information help

Species

Cryptococcus gattii VGIV

Lineage

Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGIV

CAZyme ID

I308_04698-t35_1-p1

CAZy Family

GT1

CAZyme Description

cytochrome c peroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315	KN848867\|CGC4	33728.06	6.0347

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiIND107	6843	1296105	147	6696

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in I308_04698-t35_1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA2	12	251	3.2e-49	0.9803921568627451

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173825	ascorbate_peroxidase	5.31e-122	8	251	12	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.
178218	PLN02608	7.22e-80	29	276	29	266	L-ascorbate peroxidase
166005	PLN02364	9.33e-69	8	250	11	246	L-ascorbate peroxidase 1
178467	PLN02879	5.53e-68	9	250	6	246	L-ascorbate peroxidase
173823	plant_peroxidase_like	1.98e-53	14	248	1	255	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
4.33e-226	1	315	1	334
3.76e-216	1	315	1	355
1.46e-109	8	278	6	293
1.51e-109	8	278	6	293
2.53e-106	7	257	5	272

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.25e-64	8	250	10	245	The structure of ascorbate peroxidase Compound I [Glycine max],2XIF_A The structure of ascorbate peroxidase Compound II [Glycine max],2XIH_A The structure of ascorbate peroxidase Compound III [Glycine max],2XJ6_A The structure of ferrous ascorbate peroxidase [Glycine max],5JQR_A The Structure of Ascorbate Peroxidase Compound II formed by reaction with m-CPBA [Glycine max]
1.81e-64	8	250	22	257	Ascobate peroxidase from soybean cytosol in complex with ascorbate [Glycine max],1OAG_A Ascorbate peroxidase from soybean cytosol [Glycine max],1V0H_X ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID [Glycine max],2GHH_X Conformational mobility in the active site of a heme peroxidase [Glycine max],2GHK_X Conformational mobility in the active site of a heme peroxidase [Glycine max],5JPR_A Neutron Structure of Compound II of Ascorbate Peroxidase [Glycine max],6TAE_A Neutron structure of ferric ascorbate peroxidase [Glycine max],6XV4_A Neutron structure of ferric ascorbate peroxidase-ascorbate complex [Glycine max],7BI1_A Chain A, Ascorbate peroxidase [Glycine max]
1.99e-64	8	250	22	257	Structure of isoniazid (INH) bound to cytosolic soybean ascorbate peroxidase [Glycine max]
3.54e-64	8	250	10	245	Ascorbate Peroxidase R38K mutant [Glycine max]
1.00e-63	8	250	10	245	Ascorbate Peroxidase R38A mutant [Glycine max]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.32e-227	1	315	1	315	Putative heme-binding peroxidase OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CNE03890 PE=3 SV=1
1.32e-227	1	315	1	315	Putative heme-binding peroxidase OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CNBE3880 PE=3 SV=1
3.62e-114	7	293	5	304	Putative heme-binding peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP2 PE=3 SV=1
1.99e-109	5	257	3	275	Putative heme-binding peroxidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN5440 PE=3 SV=1
8.51e-106	5	255	3	273	Putative heme-binding peroxidase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=AFUA_6G13570 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000070	0.000000

TMHMM Annotations help

There is no transmembrane helices in I308_04698-t35_1-p1.