CAZyme Information: EPrPRT00000021480-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000021480-p1
• CAZy Family: GH6
• CAZyme Description: Catalase-peroxidase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
448		48532.96	8.2952

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531	13857	1223556	52	13805

• Gene Location: location=ParrATCC12531_SC01703:5796-7213(-)

Full Sequence      

MGKPDPAGSAIEIRDTFKRMGFGDRETVALVGGGHGFGKMHGACATGPGPDPIESPDAPW
PGTCTNNAGHPKGKGNNTYTNGFEHAWTFHPTNWTNEYFQGITGVPLFEKEVSPGGRIQW
RGIPDTDPPLRMLTADLALVNDAKYKPVSLEFAANITALADTFGSAWYKLLTLDMGPVTR
CRGNLRIVALLHQGVKGLTGDTVTGGKTYNGALFVHLAYQCASTFRITDYSGGCNGAKIR
FAPQKDWEGNAGLGDVLAALETIRKEFPTLSMADLIVLAGQVALQQGGSGAIRFVGGRVD
ALDGANIEKLAPRTYYKSPLAFVRDDAKVRGLTAYEYVALAGRPRSLVQQKRLGYSGTFT
DQIDTVSNMFFKVLVSNTWAKSGTRQYKAKGKENLYVLDTDVALLWDSSYKSIVQEFASD
EALFKSVFASAWGTLMTADHFSTKEGYY

Enzyme Prediction     

No EC number prediction in EPrPRT00000021480-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	214	439	1.1e-22	0.8941176470588236

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
237891	PRK15061	7.14e-90	2	441	222	723	catalase/peroxidase.
223453	KatG	3.03e-88	2	441	234	727	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
272957	cat_per_HPI	1.28e-81	2	441	218	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	2.78e-53	1	183	208	401	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	6.29e-48	211	436	18	254	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	1.05e-178	1	442	220	683
UIZ20718.1|AA0	1.26e-174	1	442	220	683
UIZ20725.1|AA0	7.16e-174	1	442	220	683
UPM44564.1|AA0	4.44e-51	2	441	210	712
UKZ65891.1|AA0	2.06e-50	2	441	54	553

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KQH_A	9.83e-54	2	441	226	725	Crystal structure of the V293D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5KQH_B Crystal structure of the V293D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
3VLH_A	1.08e-53	2	441	226	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]
5TXQ_A	1.35e-53	2	441	226	725	Crystal structure of the A143D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5TXQ_B Crystal structure of the A143D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
5SYU_A	1.35e-53	2	441	226	725	Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b],5SYU_B Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b]
5V4O_A	1.35e-53	2	441	226	725	Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5V4O_B Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q5WZY1|KATG2_LEGPL	6.76e-66	2	444	237	741	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Lens) OX=297245 GN=katG2 PE=3 SV=1
sp|Q9WXB9|KATG2_LEGPN	3.49e-65	2	444	237	741	Catalase-peroxidase 2 OS=Legionella pneumophila OX=446 GN=katG2 PE=2 SV=1
sp|Q5ZZ17|KATG2_LEGPH	3.49e-65	2	444	237	741	Catalase-peroxidase 2 OS=Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) OX=272624 GN=katG2 PE=3 SV=1
sp|A5IA67|KATG2_LEGPC	6.73e-65	2	444	237	741	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Corby) OX=400673 GN=katG2 PE=3 SV=1
sp|Q5X8J8|KATG2_LEGPA	9.34e-65	2	444	237	741	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
1.000046	0.000004

TMHMM  Annotations     

There is no transmembrane helices in EPrPRT00000021480-p1.