CAZyme Information: PHYCI_12862T0-p1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: PHYCI_12862T0-p1
• CAZy Family: AA17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382		40819.91	6.2991

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22	26201	1048749	70	26131

• Gene Location: location=PcinCBS144-22_SC0105:40069-41216(-)

Full Sequence      

MNVRLAAFVAAIATLASGAAAGSCPFGYDKIASVKQQDRQISSELYDAKSCDVIDYDLVK
KDLEALMTNSQDFWPADFGHYGGLFIRLAWHCNGSYRRADGRGGCDGGRIRFNPEHSWAD
NTNLDKALKLLDPIKKKYGDALSWGDLIVLSGNVAIKSMGGPVLGFCGGRRDDVDGTSSL
QLGPTPEQESVAPCAVDGDCKEPLGPTTMGLIYVNPEGPMGKADPAASAPQVRDTFKRMG
MNDRETVALVGGGHAFGKTHGACKTGPGPSPLEDPANPWPGTCGEGPMKGKGNNTFTSGF
EGQWTFTPTKWGNGYFKGLTTRKWEKYDGPGGHVQWRPVPDTTPPVRMLTADIALLHDPS
YKAIATEFAANQAALDEAFSHA

Enzyme Prediction     

No EC number prediction in PHYCI_12862T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	74	188	2.4e-23	0.4392156862745098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
237891	PRK15061	9.17e-139	54	382	54	397	catalase/peroxidase.
173824	catalase_peroxidase_1	2.52e-137	54	382	42	384	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.
223453	KatG	1.26e-130	54	382	67	408	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
272957	cat_per_HPI	8.07e-117	48	382	46	391	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	3.55e-60	57	382	1	249	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPT50360.1|AA0	5.38e-243	1	382	1	382
UIZ20725.1|AA0	3.44e-234	1	382	1	382
UIZ20718.1|AA0	8.66e-230	1	382	1	382
UPM44564.1|AA0	9.25e-104	36	382	20	386
UKZ91289.1|AA0	7.33e-90	33	382	32	423

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ITK_A	1.84e-100	54	371	59	391	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3VLH_A	2.11e-100	54	371	59	391	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]
3VLK_A	5.85e-100	54	371	59	391	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]
3UW8_A	5.85e-100	54	371	59	391	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]
3VLM_A	1.63e-99	54	371	59	391	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q2RZX7|KATG_SALRD	2.74e-102	48	382	49	397	Catalase-peroxidase OS=Salinibacter ruber (strain DSM 13855 / M31) OX=309807 GN=katG PE=3 SV=1
sp|Q5V0S5|KATG1_HALMA	4.67e-100	54	371	56	390	Catalase-peroxidase 1 OS=Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) OX=272569 GN=katG1 PE=3 SV=1
sp|Q5KZ91|KATG_GEOKA	5.36e-100	31	382	38	406	Catalase-peroxidase OS=Geobacillus kaustophilus (strain HTA426) OX=235909 GN=katG PE=3 SV=1
sp|O59651|KATG2_HALMA	9.45e-100	54	371	59	391	Catalase-peroxidase 2 OS=Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) OX=272569 GN=katG2 PE=1 SV=3
sp|O73955|KATG_HALSA	5.67e-99	48	382	40	391	Catalase-peroxidase OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OX=64091 GN=katG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000214	0.999767	CS pos: 21-22. Pr: 0.9587

TMHMM  Annotations     

There is no transmembrane helices in PHYCI_12862T0-p1.