CAZyme Information: PPTG_04280-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_04280-t26_1-p1
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
690	KI669566|CGC1	74585.81	4.8976

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669566:1822630-1824702(+)

Full Sequence      

MNVRLAAFVAALASLSAGIDAGRSGSCPFGFDKVASVKEQDRQISSELYDPKSCEVINYD
LVKADLEKLMTDSQAFWPADFGHYGGLFIRLAWHCNGSYRRADGRGGCDGGRIRFNPEHS
WADNTNLDKALKLLNPIKEKYGDALSWGDLIVLSGDVAIKSMGGPVLGFCGGRRDDADGT
SSLQLGPSAEQEAVAPCEVDGQCKEPLGPTTMGLIYVNPEGPMGKPDPVGSVADVRDTFK
RMGMDDRETVALIGGGHAFGKTHGACPTGPGPSPLEDPENPWPGTCGEGEMKGKGNNTFT
SGFEGQWTFTPTKWGNGYFKGLTSFEWEKFDGPGGHVQWRPVPDTNPPVRMLTADIALLH
DESYLKISKEFAADQAALDEAFSHAWYKLMSRDMGPVARCRGNDIPPVQPFQNPLPPTPE
NLPDFDAVRKDIKELLTKSVDGLPSDATSDGKAYNGALFVHAAWQCASTFRITDYAGGCN
GAKIRFAPQKDWPVNAGVDKIIAALEPIKEKYSTLSTADLIVLAGQVALEDAGKVKIDFL
GGRTDAQNGDGDDILAPREYYNSSVTAVRDNIKILGVSPEEAVALAARPRSAAQQKALGF
SGSYSNSSATLSNEYFKVLLNETWTAVSKKEFKAGDKDIYMLDTDLALLEAPELKASVEK
FASNEFAFKQTFSKAWNKVMTADHFKADSY

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	460	683	4.2e-28	0.8901960784313725
AA2	76	189	9.7e-23	0.43529411764705883

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223453	KatG	0.0	57	685	67	727	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	0.0	57	685	54	723	catalase/peroxidase.
272957	cat_per_HPI	1.02e-169	52	685	47	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	2.05e-149	57	406	42	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	5.05e-62	450	680	12	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	690	1	687
UIZ20725.1|AA0	0.0	1	690	1	687
UIZ20718.1|AA0	0.0	1	690	1	687
UPM44564.1|AA0	1.99e-142	42	685	23	712
UKZ91289.1|AA0	3.24e-129	57	685	57	748

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WHQ_A	6.56e-135	57	685	69	754	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]
1ITK_A	5.15e-134	57	685	59	728	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3UW8_A	1.70e-133	57	685	59	728	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]
3VLK_A	1.70e-133	57	685	59	728	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]
5WHS_A	3.96e-133	57	685	69	754	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0C8F0|KATG_ECOLX	4.16e-144	57	685	66	731	Catalase-peroxidase OS=Escherichia coli OX=562 GN=katG PE=3 SV=1
sp|Q7BSW8|KATG2_ECO57	4.16e-144	57	685	66	731	Catalase-peroxidase 2 OS=Escherichia coli O157:H7 OX=83334 GN=katG2 PE=3 SV=1
sp|A5IA67|KATG2_LEGPC	2.62e-142	57	685	71	738	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Corby) OX=400673 GN=katG2 PE=3 SV=1
sp|Q5X8J8|KATG2_LEGPA	3.69e-142	57	685	71	738	Catalase-peroxidase 2 OS=Legionella pneumophila (strain Paris) OX=297246 GN=katG2 PE=3 SV=1
sp|Q9WXB9|KATG2_LEGPN	5.21e-142	57	685	71	738	Catalase-peroxidase 2 OS=Legionella pneumophila OX=446 GN=katG2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000207	0.999756	CS pos: 21-22. Pr: 0.9718

TMHMM  Annotations     

There is no transmembrane helices in PPTG_04280-t26_1-p1.