CAZyme Information: AFUB_084930-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: AFUB_084930-T-p1
• CAZy Family: PL1
• CAZyme Description: Ortholog(s) have catalase activity and cytoplasm, extracellular region localization

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
759	scf_000007_A_fumigatus_A1163|CGC1	83761.87	6.5526

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusA1163	10106	451804	199	9907

• Gene Location: location=scf_000007_A_fumigatus_A1163:1513674-1515953(+)

Full Sequence      

MTQDKCPFKEQSSQPNFAGGGTSNKDWWPDRLKLNILRQHTAVSNPLDADFDYAAAFNSL
DYEGLKKDLRALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVFDGRGGAGQGQQRFAP
LNSWPDNVSLDKARRLLWPIKQKYGNKISWADLLILTGNVALESMGFKTFGFAGGRPDTW
EADEATYWGRETTWLGNDARYAKGFSGSDKRGSLIADEESHKTTHSRELETPLAAAHMGL
IYVNPEGPDGNPDPVAAAHDIRDTFGRMAMNDEETVALIAGGHTFGKTHGAAPADNVGKE
PEAAGLEAQGLGWANKHGSGKGPHTITSGLEVTWTKTPTQWNNNFLEYLFKFEWELTKSP
AGAHQWVAKNADEIIPDAYDASKKHKPTMLTTDLSLRFDPAYEKIARRFLEHPDQFADAF
ARAWFKLTHRDMGPRARYLGPEVPSEVLIWQDPIPAVNHPLVDASDIAALKDEILASGVP
PRSFISTAWAAASTFRGSDKRGGANGARIRLAPQRDWEVNNQPWLREALSALEAVQSRFN
ARGDSKKVSLADLIVLAGCAAVEKAAQDAGHPIKVPFVPGRMDASQEETDVQSFNHMEPF
ADGFRNFAKGPARPRAEHYLVDKAQLLNLSAPEMTVLVGGLRVLNTNYDGSTHGVFTSRP
GALTNDFFVHLLDMNTAWKDVGNGELFEGSDRKTGGKKWTATRADLVFGSNAELRAIAEV
YASNDGDMKFVKDFVAAWNKVMNLDRFDLKGKQTIPARL

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173824	catalase_peroxidase_1	0.0	19	448	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.
173828	catalase_peroxidase_2	0.0	452	746	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.
223453	KatG	0.0	5	750	17	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	0.0	1	750	1	726	catalase/peroxidase.
272957	cat_per_HPI	0.0	18	749	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]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ91289.1|AA0	0.0	5	749	6	750
UPK95725.1|AA0	0.0	1	755	62	811
UPM44564.1|AA0	1.52e-303	23	750	4	715
UKZ91589.1|AA0	1.73e-300	5	751	57	790
UKZ83034.1|AA0	2.28e-300	6	751	58	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5SYV_A	0.0	5	749	6	727	Crystal structure of Burkholderia pseudomallei KatG N240D variant [Burkholderia pseudomallei 1710b],5SYV_B Crystal structure of Burkholderia pseudomallei KatG N240D variant [Burkholderia pseudomallei 1710b]
5TXQ_A	0.0	5	749	6	727	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	5	749	6	727	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	5	749	6	727	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	5	749	6	727	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|A1C8R3|KATG_ASPCL	0.0	1	759	1	760	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|A2Q7T1|KATG_ASPNC	0.0	1	759	1	762	Catalase-peroxidase OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=katG PE=3 SV=1
sp|A1TRV8|KATG_ACIAC	0.0	1	750	1	743	Catalase-peroxidase OS=Acidovorax citrulli (strain AAC00-1) OX=397945 GN=katG PE=3 SV=1
sp|A1DAL6|KATG_NEOFI	0.0	1	759	1	759	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|A4R5S9|KATG1_MAGO7	0.0	5	750	3	737	Catalase-peroxidase 1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=katG1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000067	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AFUB_084930-T-p1.