CAZyme Information: PHYSODRAFT_284779-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_284779-t26_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
449	JH159152|CGC11	48535.20	4.6489

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159152:2980469-2981818(-)

Full Sequence      

MGMNDRETVALIGGGHAFGKTHGACPTGPGPDPTQDPLNPWPGTCGEGAMKGKGNNTFTG
GFEGSWTFTPTKWGNGYFKGLTNLEWEKFDGPGGHVQWRPVPDTTPPVRMLTADIALLHD
ESYHNISLEFAANQTALDEEFSHAWYKLMSRDLGPVARCRGKDVPPAQPFQNPLPPTPAS
LADFDAVRSDIRSLLTKSVDGLTSDSSSDGTPYNGALFVHAAWQCASTFRITDYAGGCNG
ARIRFSPEKDWPVNAGVDKIISALEPVKESYPTLSTADLIVLAGQVALEDAGNVTIDFLG
GRTDADNGNGTEILAPREYYNTTLIAVRDNIKILGVSPYEAVALAGRPRSVAQQKVLGYS
GSYSNDSLTLSNEYFQVLLNETWTEVSAKEYKAEGKDVYMMDTDLALLAAPELKEAVQLF
ASEEAVFKHVFSSAWAKVMTADHFNASSY

Enzyme Prediction     

No EC number prediction in PHYSODRAFT_284779-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	220	442	1.8e-26	0.8862745098039215

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223453	KatG	6.29e-98	1	445	252	728	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	1.70e-96	1	444	240	723	catalase/peroxidase.
272957	cat_per_HPI	5.80e-87	1	445	236	712	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	1.43e-56	1	165	227	405	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	2.10e-54	185	439	1	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	0.0	1	449	239	687
UIZ20725.1|AA0	3.56e-295	1	449	239	687
UIZ20718.1|AA0	1.18e-293	1	449	239	687
UPM44564.1|AA0	8.65e-65	1	445	228	713
UKZ91289.1|AA0	1.71e-62	1	445	268	749

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WHQ_A	1.17e-61	1	445	279	755	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	1.17e-61	1	445	279	755	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	3.60e-60	1	445	244	729	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3VLK_A	3.89e-60	1	445	244	729	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	7.46e-60	1	445	244	729	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|Q5WZY1|KATG2_LEGPL	2.50e-71	1	445	255	739	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Lens) OX=297245 GN=katG2 PE=3 SV=1
sp|Q5X8J8|KATG2_LEGPA	2.50e-71	1	445	255	739	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Paris) OX=297246 GN=katG2 PE=3 SV=1
sp|Q5ZZ17|KATG2_LEGPH	4.84e-71	1	445	255	739	Catalase-peroxidase 2 OS=Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) OX=272624 GN=katG2 PE=3 SV=1
sp|Q9WXB9|KATG2_LEGPN	4.84e-71	1	445	255	739	Catalase-peroxidase 2 OS=Legionella pneumophila OX=446 GN=katG2 PE=2 SV=1
sp|A5IA67|KATG2_LEGPC	9.39e-71	1	445	255	739	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Corby) OX=400673 GN=katG2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999803	0.000234

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_284779-t26_1-p1.