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CAZyme Information: KAG6612571.1

You are here: Home > Sequence: KAG6612571.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Phytophthora cinnamomi
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
CAZyme ID KAG6612571.1
CAZy Family GH5
CAZyme Description Catalase/peroxidase HPI
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
687 JAFJYM010000039|CGC6 73985.56 7.7416
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcinnamomiGKB4 19981 N/A 0 19981
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 457 680 1.4e-32 0.8901960784313725
AA2 74 188 7.2e-23 0.4392156862745098

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223453 KatG 0.0 54 682 67 727
Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891 PRK15061 0.0 54 682 54 723
catalase/peroxidase.
272957 cat_per_HPI 1.49e-172 48 682 46 711
catalase/peroxidase HPI. As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
173824 catalase_peroxidase_1 1.36e-152 54 403 42 405
N-terminal catalytic domain of catalase-peroxidases. This is 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. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
173823 plant_peroxidase_like 1.39e-60 57 388 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 Hit End
0.0 1 687 1 687
0.0 1 687 1 687
0.0 1 687 1 687
5.84e-144 36 682 20 712
2.48e-131 33 682 32 748

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.50e-141 54 682 59 728
Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3.15e-140 54 682 59 728
Crystal Structure Analysis of the Ser305Thr Variants of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3UW8_B Crystal Structure Analysis of the Ser305Thr Variants of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049]
3.15e-140 54 682 59 728
Crystal Structure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLK_B Crystal Structure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLL_A Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA [Haloarcula marismortui ATCC 43049],3VLL_B Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA [Haloarcula marismortui ATCC 43049]
8.81e-140 54 682 59 728
Crystal Structure Analysis of the Met244Ala Variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLM_B Crystal Structure Analysis of the Met244Ala Variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049]
1.24e-139 54 682 59 728
Crystal Structure Analysis of the Arg409Leu Variants of KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLH_B Crystal Structure Analysis of the Arg409Leu Variants of KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLI_A Crystal Structure Analysis of the Cyanide Arg409Leu Variant KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLI_B Crystal Structure Analysis of the Cyanide Arg409Leu Variant KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLJ_A Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLJ_B Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.43e-145 54 682 66 731
Catalase-peroxidase 2 OS=Escherichia coli O157:H7 OX=83334 GN=katG2 PE=3 SV=1
2.43e-145 54 682 66 731
Catalase-peroxidase OS=Escherichia coli OX=562 GN=katG PE=3 SV=1
2.76e-144 48 682 65 738
Catalase-peroxidase 2 OS=Legionella pneumophila OX=446 GN=katG2 PE=2 SV=1
2.76e-144 48 682 65 738
Catalase-peroxidase 2 OS=Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) OX=272624 GN=katG2 PE=3 SV=1
5.49e-144 48 682 65 738
Catalase-peroxidase 2 OS=Legionella pneumophila (strain Paris) OX=297246 GN=katG2 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000215 0.999769 CS pos: 21-22. Pr: 0.9550

TMHMM  Annotations      help

There is no transmembrane helices in KAG6612571.1.