CAZyme Information: FOYG_15298-t42_2-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOYG_15298-t42_2-p1
• CAZy Family: PL1
• CAZyme Description: catalase-peroxidase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
777		85132.10	7.1693

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931	17642	660029	362	17280

• Gene Location: location=JH717849.1:308000-310536(+)

Full Sequence      

MHVQSLLLASGLVPLAASQGCPFAKRATDANLVPPREIPEDFGICRVASNQAGGGTRSRD
FWPCALRLDVLRQFSPQYNPLGADFDYTEAFKSLDFAALKKDLNTLLTDSQDWWPADHGN
YGGLFIRMSWHSAGTYRAMDGRGGSGMGQQRFAPLDSWPDNQNLDKARRLLWPIKQKYGS
KISWADLMVLAGNVALEHSGFETLGFAGGRADTWEADESIYWGAESTFVPKGNDVRYNGS
TDIYERADKLEKPLGATHFGLIYVNPEGPDGSSDPKASALDIRTAFGRMGMDDEETAALI
IGGHTLGKTHGAVPAKNIGPEPMAADLGEMGLGWHNSVNEGNGPDQMTSGLEVIWSTTPT
KWSNHFLKSLLGNNWTLVESPAGHKQWEALNGKLEYPDPFVKGKFRRPTMLTSDLALIND
PSYLKICKRWHDNPKELNAAFARAWYKLLHRDLGPVSRYLGPEVAKEKFIWQDPLPERKG
DIIGEADISSLKSAILSADSLDVSKLVSTAWNSASTFRGTDKRGGANGARIALEPQVNWV
SNNPKQLKQVLSALKKVQKDFNSKSGSKKVSLADLIVLGGVAAIEKAAQAAGFKNLEVPF
TPGRVDATQNQTDLVQFGYLEPLADGFRNYGHGTARARTEEILVDRAALLTLTPPEMTVL
VGGLRALNANYDGSSNGILTEKKGQLTNDFFVNLLSPAYSWAKKDSQGELWTGTDRATKS
VKWTATRADLVFGSHAELRAISEVYGSADAKEKFVKDFISAWTKVMNLDRFDVKAEK

Enzyme Prediction     

No EC number prediction in FOYG_15298-t42_2-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
272957	cat_per_HPI	0.0	52	773	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]
173824	catalase_peroxidase_1	0.0	53	469	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.
223453	KatG	0.0	43	774	16	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	0.0	52	774	12	726	catalase/peroxidase.
173828	catalase_peroxidase_2	7.91e-172	473	770	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	1	773	1	786
UKZ91589.1|AA0	0.0	1	774	1	789
UKZ91289.1|AA0	0.0	50	776	13	753
UPK95725.1|AA0	3.35e-308	44	773	69	805
UPM44564.1|AA0	4.97e-277	58	774	5	715

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5CJH_A	0.0	19	777	2	764	Crystal Structure of Eukaryotic Oxoiron MagKatG2 at pH 8.5 [Pyricularia oryzae 70-15],5CJH_B Crystal Structure of Eukaryotic Oxoiron MagKatG2 at pH 8.5 [Pyricularia oryzae 70-15],5JHX_A Crystal Structure of Fungal MagKatG2 at pH 3.0 [Pyricularia oryzae 70-15],5JHX_B Crystal Structure of Fungal MagKatG2 at pH 3.0 [Pyricularia oryzae 70-15],5JHY_A Crystal Structure of Fungal MagKatG2 at pH 5.5 [Pyricularia oryzae 70-15],5JHY_B Crystal Structure of Fungal MagKatG2 at pH 5.5 [Pyricularia oryzae 70-15],5JHZ_A Crystal Structure of Fungal MagKatG2 at pH 7.0 [Pyricularia oryzae 70-15],5JHZ_B Crystal Structure of Fungal MagKatG2 at pH 7.0 [Pyricularia oryzae 70-15]
5WHQ_A	0.0	49	776	24	759	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	0.0	49	776	24	759	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]
3UT2_A	0.0	19	777	2	764	Crystal Structure of Fungal MagKatG2 [Pyricularia oryzae 70-15],3UT2_B Crystal Structure of Fungal MagKatG2 [Pyricularia oryzae 70-15]
5L05_A	3.02e-307	52	773	13	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|A1C8R3|KATG_ASPCL	0.0	49	777	15	754	Catalase-peroxidase OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=katG PE=3 SV=1
sp|B2WH84|KATG_PYRTR	0.0	43	774	4	744	Catalase-peroxidase OS=Pyrenophora tritici-repentis (strain Pt-1C-BFP) OX=426418 GN=katG PE=3 SV=1
sp|Q0CD12|KATG_ASPTN	0.0	43	776	2	731	Catalase-peroxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=katG PE=3 SV=1
sp|Q8NJN2|KATG_TALMA	0.0	49	777	15	741	Catalase-peroxidase OS=Talaromyces marneffei OX=37727 GN=katG PE=2 SV=1
sp|Q2TW34|KATG_ASPOR	0.0	50	773	15	750	Catalase-peroxidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=katG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.171247	0.828734	CS pos: 18-19. Pr: 0.7028

TMHMM  Annotations     

There is no transmembrane helices in FOYG_15298-t42_2-p1.