CAZyme Information: EFQ34482.1

Basic Information

• Species: Colletotrichum graminicola
• Lineage: Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola
• CAZyme ID: EFQ34482.1
• CAZy Family: PL27
• CAZyme Description: Catalase-peroxidase [Source:UniProtKB/TrEMBL;Acc:E3QUE4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
776	GG697380|CGC2	84465.54	5.2643

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgraminicolaM1-001	12400	645133	380	12020

• Gene Location: location=GG697380:291672-295038(-)

Full Sequence      

MHAKLSNCLLAASAILPSVSAQGCPFAKRDGSVSSELPKRDTAATFGRCPTISNEAGGGT
RSRDWWPCQLRLDVLRQFQPSTNPYGGDFDYVKAFSSLDYDALKADLRALLTESQDWWPA
DFGHYGGLFIRLCWHSAGTYRAIDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLLWPIKQ
KYGNKISWADLILLAGNTALDDMGFKTLGFAAGRPDTWQADESIYWGGETTFVPKGNDVR
YNGSTDIFERADKLEKPLASTNMGLIYVNPEGPDGSSNPAASANDIRTAFHRMGMNDSET
VALIAGGHAFGKTHGAVSADNIGPEPEAASIGEMGLGWHNSVGDGNGVNQMTSGLEVIWT
KTPTKWSNDYLESLLHNKWTLVTSPAGHHQWEAVNGTLDYPDPFDATKFRKATMLTSDLA
LINDPSYLNITTRWVDHPDELADAFAKAWFKLLHRDMGPRARYLGPEVPQETFIWQDPLP
AREGDLMDDADVATLKSTILAVPGLDVSKLASVAWASASTFRGSDKRGGANGARIALEPQ
VNWVANNPTQLSAVLDALKKVQADFNTGSKKVSLADLIVLGGTAAVEKAAADAGVKVTVP
FAPGRVDATQDQTDIESFGYLEPQADGFRNYGRGTARARTEEFLVDKAAQLTLSPPEMTV
LVGGLRALGAVFDGSNTGVLTEKKGQLTNDYFKNLLDISTVWSQSDTDGETWKGVDRKTK
TEKWTATRADLVFGSHAELRAISEVYASSDANEKFVNDFVAAWTKVMNLDRFDLQK

Enzyme Prediction     

No EC number prediction in EFQ34482.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
237891	PRK15061	0.0	47	775	4	726	catalase/peroxidase.
223453	KatG	0.0	34	775	3	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
173824	catalase_peroxidase_1	0.0	57	473	1	409	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.
272957	cat_per_HPI	0.0	56	774	10	713	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	4.48e-179	477	771	1	297	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ83034.1|AA0	0.0	9	774	6	786
UKZ91589.1|AA0	0.0	9	775	6	789
UKZ91289.1|AA0	0.0	48	776	6	752
UPK95725.1|AA0	0.0	48	776	66	807
UPM44564.1|AA0	1.46e-278	62	775	5	715

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5SX0_A	0.0	48	774	6	727	Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH7.5 [Burkholderia pseudomallei 1710b]
5SXT_A	0.0	48	774	6	727	Crystal structure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXT_B Crystal structure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b]
5SX1_A	0.0	48	774	6	727	Crystal structure of D141E variant of B. pseudomallei KatG [Burkholderia pseudomallei 1710b],5SX1_B Crystal structure of D141E variant of B. pseudomallei KatG [Burkholderia pseudomallei 1710b]
5SXX_A	0.0	48	774	6	727	Crystal structure of the E198A variant of Burkholderia pseudomallei catalase-peroxidase KatG with INH [Burkholderia pseudomallei 1710b],5SXX_B Crystal structure of the E198A variant of Burkholderia pseudomallei catalase-peroxidase KatG with INH [Burkholderia pseudomallei 1710b]
5L05_A	0.0	48	774	6	727	Crystal structure of catalase-peroxidase KATG of burkholderia pseudomallei treated with INH [Burkholderia pseudomallei 1710b],5L05_B Crystal structure of catalase-peroxidase KATG of burkholderia pseudomallei treated with INH [Burkholderia pseudomallei 1710b],5SW6_A Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6 [Burkholderia pseudomallei 1710b],5SW6_B Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6 [Burkholderia pseudomallei 1710b],5SX0_B Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH7.5 [Burkholderia pseudomallei 1710b],5SX3_A Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5 [Burkholderia pseudomallei 1710b],5SX3_B Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5 [Burkholderia pseudomallei 1710b],5SXQ_A Crystal structure of B. pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXQ_B Crystal structure of B. pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXS_A Crystal structure of catalase-peroxidase KatG with isonicotinic acid hydrazide and AMP bound [Burkholderia pseudomallei 1710b],5SXS_B Crystal structure of catalase-peroxidase KatG with isonicotinic acid hydrazide and AMP bound [Burkholderia pseudomallei 1710b],5SYL_A B. pseudomallei KatG with KCN bound [Burkholderia pseudomallei 1710b],5SYL_B B. pseudomallei KatG with KCN bound [Burkholderia pseudomallei 1710b],6MPY_A B. pseudomallei KatG crystallized in the presence of benzoyl hydrazide [Burkholderia pseudomallei],6MPY_B B. pseudomallei KatG crystallized in the presence of benzoyl hydrazide [Burkholderia pseudomallei],6MQ0_A B. pseudomallei KatG crystallized in the presence of furoyl hydrazide [Burkholderia pseudomallei],6MQ0_B B. pseudomallei KatG crystallized in the presence of furoyl hydrazide [Burkholderia pseudomallei],6MQ1_A Chain A, Catalase-peroxidase [Burkholderia pseudomallei],6MQ1_B Chain B, Catalase-peroxidase [Burkholderia pseudomallei]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q2SZ20|KATG_BURTA	0.0	48	774	6	727	Catalase-peroxidase OS=Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) OX=271848 GN=katG PE=3 SV=1
sp|Q48E42|KATG_PSE14	0.0	44	774	2	755	Catalase-peroxidase OS=Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OX=264730 GN=katG PE=3 SV=1
sp|Q3KE62|KATG_PSEPF	0.0	44	776	2	755	Catalase-peroxidase OS=Pseudomonas fluorescens (strain Pf0-1) OX=205922 GN=katG PE=3 SV=1
sp|Q2TW34|KATG_ASPOR	0.0	54	774	15	750	Catalase-peroxidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=katG PE=3 SV=1
sp|Q4ZNN4|KATG_PSEU2	0.0	44	774	2	755	Catalase-peroxidase OS=Pseudomonas syringae pv. syringae (strain B728a) OX=205918 GN=katG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.074383	0.925602	CS pos: 21-22. Pr: 0.8731

TMHMM  Annotations     

There is no transmembrane helices in EFQ34482.1.