CAZyme Information: FOMG_14782-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_14782-t38_1-p1
• CAZy Family: PL3
• CAZyme Description: catalase-peroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
801		88566.10	7.0289

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

• Gene Location: location=JH659343.1:318522-321041(-)

Full Sequence      

MPRFLFPSSRILSLSVARRTLNLNLNQQTTRLSLHTSAPKMADERKCPVAHKVPNVAGHG
VTHQKWWPEALKTNILRQHSAVTNPYGENFNYAEAFNSIDYNELKEDLRKVCRDSQDWWP
ADFGHYGGLFVRMSWHAVGTYRVFDGRGGGRQGQQRFAPLNSWPDNVSLDKARRLLWPVK
QKYGNKVSWADLIVMAGNVALEDMGFKTIGFAAGRPDTWEADEATYYGGEDTWLGNDVRY
SDGHPGTTKPGATDSDQPPHKNIHTRELEKPLAAAHHGLIYVNPEGPDGNPDPVAAARDI
RETFGRMAMNDEETVALIAGGHTVGKTHGAGSTDHVGPEPEAADLAQQGLGWSNSYKTGK
GPHTTTSGLEVTWTSTPVKWSHDYLKYLFQFEWELTKSPAGAHQWVAKDANATVPDAFDP
NKKQKPTMLTTDLSLRFDPEYEKISRRFLENPDQFNEAFAKAWFKLTHRDMGPRDRYLGP
EVPKEVFLWQDPVPERDYKLVDDGDISAIKNEILKSGIDVSKLVSTAWASASTFRGSDLR
GGANGARIRLQPQKDWEVNNPAQLSKVLSTLEGIQKKFNDSQSSGKAISLADVIVLAGSA
AVEKAAKDAGVNITVPFAPGRTDATQEQTDVKSVNHLQPFADGFRNYGSSTDRVKLEHQL
IDRAQLLTLSVPELTALIGGLRALNTNYDGSSHGIFTNRPGVLTNDFFVNLLDMSTEWKA
VGNGDIFEGTDRKTGAKKWTGTRVDLVFGSHAELRATAETYAEAGGQEKLVKDFVAAWTK
VMNLDRFDLANGSSPKASPRL

Enzyme Prediction     

No EC number prediction in FOMG_14782-t38_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
237891	PRK15061	0.0	42	790	1	726	catalase/peroxidase.
223453	KatG	0.0	35	790	6	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
173824	catalase_peroxidase_1	0.0	58	487	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	45	792	2	716	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	0.0	491	786	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
UPK95725.1|AA0	0.0	44	801	64	817
UKZ91289.1|AA0	0.0	41	801	1	762
UPM44564.1|AA0	1.52e-304	62	789	4	714
UKZ83034.1|AA0	1.22e-303	38	795	49	792
UKZ91589.1|AA0	3.03e-297	38	789	49	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5SYU_A	0.0	41	790	1	728	Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b],5SYU_B Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b]
5TXQ_A	0.0	41	790	1	728	Crystal structure of the A143D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5TXQ_B Crystal structure of the A143D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
5SYY_A	0.0	41	790	1	728	Crystal structure of the S324G variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5SYY_B Crystal structure of the S324G variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
5SYW_A	0.0	41	790	1	728	Crystal structure of Burkhoderia pseudomallei KatG variant Q233E [Burkholderia pseudomallei 1710b],5SYW_B Crystal structure of Burkhoderia pseudomallei KatG variant Q233E [Burkholderia pseudomallei 1710b]
5V53_A	0.0	41	790	1	728	Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei with acetate bound [Burkholderia pseudomallei 1710b],5V53_B Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei with acetate bound [Burkholderia pseudomallei 1710b]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A1DAL6|KATG_NEOFI	0.0	46	789	5	749	Catalase-peroxidase OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=katG PE=3 SV=1
sp|A5FD11|KATG_FLAJ1	0.0	43	790	7	757	Catalase-peroxidase OS=Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) OX=376686 GN=katG PE=3 SV=1
sp|A4R5S9|KATG1_MAGO7	0.0	46	792	3	739	Catalase-peroxidase 1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=katG1 PE=1 SV=1
sp|A2Q7T1|KATG_ASPNC	0.0	44	789	3	752	Catalase-peroxidase OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=katG PE=3 SV=1
sp|A9AGE5|KATG_BURM1	0.0	41	789	1	727	Catalase-peroxidase OS=Burkholderia multivorans (strain ATCC 17616 / 249) OX=395019 GN=katG PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000050	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FOMG_14782-t38_1-p1.