CAZyme Information: KAG6612848.1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: KAG6612848.1
• CAZy Family: GH54
• CAZyme Description: Catalase/peroxidase HPI

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
400	JAFJYM010000039|CGC3	43643.34	9.4727

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: location=JAFJYM010000039:1787781-1788983(-)

Full Sequence      

MKGKGNNTFTSGFEGQWTFTPTKWGNGYFKGLTTRKWEKYDGPGGHVQWRPVPDTTPPVR
MLTADIALLHDPSYKAIATEFAANQAALDEAFSHAWYKLTSRDMGPVARCRGKDVPPAQP
FQNPLPPSPAKLADFDAVRKDIRALLNKKVDGLSGDSTGKASSYNGALFVHAAWQCASTF
RITDYAGGCNGAKIRFAPEKDWPVNKGVDKIIAALEPIKKKYSTLSSADLIVLAGQVALE
DAGSPKIDFLGGRTDATNGDGSDLLAPREYYNSTLTAVRDNIKILGVSTEEAVALAARPR
SAAQQKTLGYSGSYSNNSNKLSNEYFQVLLNEKWTAVSKKEFKAEGQNVYMMDTDLALLD
APELKASVEKFAKDQKAFQKVFASAWAKVMQADHFKAGSY

Enzyme Prediction     

No EC number prediction in KAG6612848.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	170	393	4e-33	0.8901960784313725

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
237891	PRK15061	1.21e-79	2	395	291	723	catalase/peroxidase.
223453	KatG	5.62e-78	2	395	303	727	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
272957	cat_per_HPI	7.59e-75	2	395	287	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]
173823	plant_peroxidase_like	2.25e-57	166	391	18	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.
173825	ascorbate_peroxidase	1.31e-46	129	388	7	244	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
UPT50360.1|AA0	7.47e-236	1	400	288	687
UIZ20725.1|AA0	2.23e-220	1	400	288	687
UIZ20718.1|AA0	2.09e-218	1	400	288	687
UPM44564.1|AA0	9.76e-53	2	395	280	712
UKZ91289.1|AA0	2.51e-49	3	395	320	748

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WHQ_A	1.35e-51	2	395	330	754	Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A [Neurospora crassa OR74A],5WHQ_B Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A [Neurospora crassa OR74A]
5WHS_A	1.35e-51	2	395	330	754	Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.6 A [Neurospora crassa OR74A],5WHS_B Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.6 A [Neurospora crassa OR74A]
1ITK_A	4.47e-50	4	395	298	728	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3VLM_A	4.72e-50	4	395	298	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]
3VLK_A	1.23e-49	4	395	298	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B1J7Q1|KATG_PSEPW	1.18e-58	3	395	323	749	Catalase-peroxidase OS=Pseudomonas putida (strain W619) OX=390235 GN=katG PE=3 SV=1
sp|Q9WXB9|KATG2_LEGPN	4.19e-58	3	395	307	738	Catalase-peroxidase 2 OS=Legionella pneumophila OX=446 GN=katG2 PE=2 SV=1
sp|Q5ZZ17|KATG2_LEGPH	4.19e-58	3	395	307	738	Catalase-peroxidase 2 OS=Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) OX=272624 GN=katG2 PE=3 SV=1
sp|Q88GQ0|KATG_PSEPK	5.94e-58	3	395	322	748	Catalase-peroxidase OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=katG PE=3 SV=1
sp|Q5X8J8|KATG2_LEGPA	8.02e-58	3	395	307	738	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Paris) OX=297246 GN=katG2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999983	0.000058

TMHMM  Annotations     

There is no transmembrane helices in KAG6612848.1.