CAZyme Information: EPrPRT00000025912-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000025912-p1
• CAZy Family: GT71
• CAZyme Description: Catalase-peroxidase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
308		33521.13	8.1164

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_SC06697:25-1114(+)

Full Sequence      

MLTADLALINDDKYKPVAHEFAANITXXXXIEAPNAPWPGTCTNVTAHPKGAGNNTYTSG
FEHAWAFNPTNWTNEYFQGLKNVPLFEQEVSPAWYKLLTLDMGPVTRCRGNLVPPAQPFQ
NPLPPAPAPSQLPDFTAVWKRVKALLHQEVEGLTSDTVTGGKTYNGALFVHLAYQCASTF
RITDYSGGCNGAKIRFAPQKDWEGNAGLGDVLAALETIRKEFPTLSIADLIVLAGQVALQ
QGGSGAIRFVGGRVDALDGANIEKLAPRTYYKSPLAFVRDDAKVRGLTAYEYVALAGRPR
SLVQQKRL

Enzyme Prediction     

No EC number prediction in EPrPRT00000025912-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	167	297	4.3e-16	0.5019607843137255

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223453	KatG	3.79e-40	47	302	300	623	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	1.35e-39	50	302	291	619	catalase/peroxidase.
272957	cat_per_HPI	1.60e-37	50	302	287	607	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]
173828	catalase_peroxidase_2	6.38e-31	169	302	33	194	C-terminal non-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 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	5.43e-30	166	302	18	161	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	1.10e-95	34	308	275	595
UIZ20725.1|AA0	1.54e-95	32	308	273	595
UIZ20718.1|AA0	2.17e-95	32	308	273	595
UKZ91289.1|AA0	2.63e-22	50	302	319	644
UKZ65891.1|AA0	2.68e-20	45	256	118	389

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VLH_A	6.03e-22	86	302	395	624	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]
1ITK_A	3.64e-21	86	302	395	624	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3VLK_A	3.65e-21	86	302	395	624	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]
3VLM_A	3.65e-21	86	302	395	624	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]
3UW8_A	3.65e-21	86	302	395	624	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B1J7Q1|KATG_PSEPW	8.17e-26	51	302	323	645	Catalase-peroxidase OS=Pseudomonas putida (strain W619) OX=390235 GN=katG PE=3 SV=1
sp|Q2J2I9|KATG_RHOP2	3.66e-25	80	302	387	623	Catalase-peroxidase OS=Rhodopseudomonas palustris (strain HaA2) OX=316058 GN=katG PE=3 SV=1
sp|Q5KZ91|KATG_GEOKA	9.09e-25	31	302	287	621	Catalase-peroxidase OS=Geobacillus kaustophilus (strain HTA426) OX=235909 GN=katG PE=3 SV=1
sp|A5W241|KATG_PSEP1	1.24e-24	50	302	321	644	Catalase-peroxidase OS=Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) OX=351746 GN=katG PE=3 SV=1
sp|Q7UUW9|KATG_RHOBA	1.31e-24	45	302	403	735	Catalase-peroxidase OS=Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1) OX=243090 GN=katG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998310	0.001706

TMHMM  Annotations     

There is no transmembrane helices in EPrPRT00000025912-p1.