CAZyme Information: PSURA_51170T0-p1

Basic Information

• Species: Phytophthora ramorum
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum
• CAZyme ID: PSURA_51170T0-p1
• CAZy Family: AA17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
124		13694.45	6.6950

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PramorumPr-102	15743	N/A	251	15492

• Gene Location: location=PramPr-102_SC0588:6236-6607(+)

Full Sequence      

KSCDVIDYDLVKKDLEALMTNSQDFWPADFGHYGGLFIRLAWHCNGSYRRADGRGGCDGG
RIRFNPEHSWADNTNLDKALKLLNPIKEKYGDALSWGDLVVLSGDVAIKSMGGPVLGFCG
GRRD

Enzyme Prediction     

No EC number prediction in PSURA_51170T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	25	124	1e-22	0.3843137254901961

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
237891	PRK15061	6.38e-57	6	124	54	172	catalase/peroxidase.
173824	catalase_peroxidase_1	1.04e-56	6	124	42	160	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	7.62e-55	6	124	67	185	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
272957	cat_per_HPI	8.01e-50	6	124	52	170	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	6.81e-29	9	124	1	112	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	1.40e-76	1	124	49	172
UIZ20725.1|AA0	8.65e-74	3	124	51	172
UIZ20718.1|AA0	1.81e-72	3	124	51	172
UKZ91289.1|AA0	1.15e-48	6	124	57	175
UPM44564.1|AA0	5.56e-47	6	124	41	159

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KSG_A	1.15e-49	6	124	55	173	Crystal structure of the W153F variant of catalase-peroxidase from B. pseudomallei treated with isoniazid [Burkholderia pseudomallei 1710b],5KSG_B Crystal structure of the W153F variant of catalase-peroxidase from B. pseudomallei treated with isoniazid [Burkholderia pseudomallei 1710b]
1ITK_A	1.17e-49	6	124	59	177	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3UW8_A	1.22e-49	6	124	59	177	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	1.22e-49	6	124	59	177	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	1.22e-49	6	124	59	177	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|B2WH84|KATG_PYRTR	2.02e-49	6	124	57	175	Catalase-peroxidase OS=Pyrenophora tritici-repentis (strain Pt-1C-BFP) OX=426418 GN=katG PE=3 SV=1
sp|A1C8R3|KATG_ASPCL	5.30e-49	6	124	60	178	Catalase-peroxidase OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=katG PE=3 SV=1
sp|Q2JZT8|KATG_RHIEC	5.90e-49	6	124	60	178	Catalase-peroxidase OS=Rhizobium etli (strain CFN 42 / ATCC 51251) OX=347834 GN=katG PE=2 SV=1
sp|O59651|KATG2_HALMA	6.03e-49	6	124	59	177	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|Q1M498|KATG_RHIL3	8.04e-49	6	124	60	178	Catalase-peroxidase OS=Rhizobium leguminosarum bv. viciae (strain 3841) OX=216596 GN=katG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000074	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PSURA_51170T0-p1.