CAZyme Information: An01g01830-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An01g01830-T-p1
• CAZy Family: PL1
• CAZyme Description: Putative catalase-peroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
762	An01_A_niger_CBS_513_88|CGC24	84251.04	6.6302

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

• Gene Location: location=An01_A_niger_CBS_513_88:436559-438847(+)

Full Sequence      

MAEAKCPFSQSRSNANVAGGGTRNTDWWPDQLNLGILRQHAPASNPFERDFDYTAAFNSL
DYYALKKDLHALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVFDGRGGGGQGQQRFAP
LNSWPDNASLDKARRLLWPIKQKYGAKISWADLMLLAGNVALESMGFKTYGFSGGRADTW
EADESVYWGGESTWMGNDVRYSDGFPGVTKHGALSGDEPPHRNIHTRDLEKPLAASHMGL
IYVNPEGPDGNPDPVAAARDIRTTFGRMGMNDEETVALIAGGHSFGKTHGAASSENVDVE
PAAAGLENQGLGWSNRYQSGKGPHTITSGIEVTWTKTPTKWSHAFLEYLFRFDWELTKSP
GGANQWQAKNTEAIIPDAYDPSKKHLPKMLTTDLSLRYDPAYEKIARRFLDHPDEFADAF
SRAWFKLLHRDMGPRTRYIGPEAPTEDLIWQDPIPAVNHTLVDANDIAALKRTILDTGLN
KSNFVSTAWASASTFRGTDKRGGANGARIRLAPQRQWEVNNQPWLEETLSALEKIQKDFN
DRVSSTGKKISLADLIVLAGCAAVEKAAQEAGQTITVPFTPGRMDASQEQTEVESFSHLE
PVADGFRNYGKSSSRVRAEHYLVDKAHLLTLTAPEMTVLVGGLRVLNTNYDGSKHGVLTS
SPGRLTNDFFTNVLDMNTAWKAKDGGRDLYEGTDRKTGQPKWTATRADLVFGSHAELRAL
AEVYGSSDGQEKFVKDFVSAWDKVMNLDRFDLKGSGIARSKL

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223453	KatG	0.0	2	753	14	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
272957	cat_per_HPI	0.0	5	752	3	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]
237891	PRK15061	0.0	1	753	1	726	catalase/peroxidase.
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	749	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
UKZ91289.1|AA0	0.0	4	752	5	750
UPK95725.1|AA0	0.0	1	752	62	805
UKZ91589.1|AA0	9.46e-311	8	754	55	790
UKZ83034.1|AA0	1.44e-309	8	754	55	788
UPM44564.1|AA0	3.21e-301	24	753	5	715

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5SXX_A	0.0	3	752	4	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]
5SYY_A	0.0	3	752	4	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	3	752	4	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]
5SYU_A	0.0	3	752	4	727	Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b],5SYU_B Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b]
5V53_A	0.0	3	752	4	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|Q3BVY2|KATG_XANC5	0.0	3	752	4	747	Catalase-peroxidase OS=Xanthomonas campestris pv. vesicatoria (strain 85-10) OX=316273 GN=katG PE=3 SV=1
sp|Q7Z7W6|KATG_ASPFU	0.0	1	762	1	759	Catalase-peroxidase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=katG PE=1 SV=1
sp|Q4US88|KATG_XANC8	0.0	3	752	4	747	Catalase-peroxidase OS=Xanthomonas campestris pv. campestris (strain 8004) OX=314565 GN=katG PE=3 SV=1
sp|Q4P914|KATG_USTMA	0.0	5	761	3	748	Catalase-peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=katG PE=3 SV=2
sp|Q8NJN2|KATG_TALMA	0.0	1	753	1	738	Catalase-peroxidase OS=Talaromyces marneffei OX=37727 GN=katG PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in An01g01830-T-p1.