CAZyme Information: AO090010000722-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090010000722-T-p1
• CAZy Family: PL3
• CAZyme Description: Ortholog(s) have catalase activity and cytoplasm, extracellular region localization

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
751		82628.12	6.1576

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr8_A_oryzae_RIB40:1523833-1526088(-)

Full Sequence      

MADKCPFHNQAPKPNVAGSGTQNRDWWPDQLKLNILRQHTTVSNPLDPDFDYAAAFNSLD
YYALKKDLQDLMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRTFDGRGGGGQGQQRFAPL
NSWPDNVSLDKARRLLWPIKQKYGNKISWADLMILTGNVALESMGFKTFGFAGGRKDTWE
ADESVYWGGETTWLGNDVRYSHGFAGSSKHGAVIADEASHRDIHSRELEKPLAAAHMGLI
YVNPEGPDGNPDPVAAARDIRTTFARMAMNDEETVALIAGGHTFGKTHGAASSDHVGSEP
EAAGLEAQGLGWQNSHGSGKGAHTITSGLEVTWTKTPTQWNLNFLEYLFRFEWVLTKSPA
GANQWVAKDADAFIPDAYDSSKKHRPQMLTTDLSLRFDPAYEKISRRFLENPDQFAEAFA
RAWFKLTHRDMGPRARYIGPEVPAEELSWQDPIPAVNHPVISETDIAALKRDILATGVDP
SKFISTAWASASTFRGSDKRGGANGARIRLAPQRDWEVNNQPWLAAALKALEDIQDKFNS
AQNDGKRVSLADLIVLAGCAAVEKAASDAGHIITVPFTPGRMDASQDQTDVESFNQMEPV
ADGFRNYGTSTARVPAEHYLVDKAQLLTLSAPEMTVLVGGLRALNANYDGSAHGVFTTRP
GQLTNDFFVNLLDMNTSWKASGSGNDIYEGTDRRTGSKKWTATRADLVFGSHAELRAIAE
VYGSSDGKGKFVKDFVAAWAKVMNLDRFDVN

Enzyme Prediction     

No EC number prediction in AO090010000722-T-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223453	KatG	0.0	1	750	14	729	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
173824	catalase_peroxidase_1	0.0	18	447	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.
237891	PRK15061	0.0	1	750	2	725	catalase/peroxidase.
272957	cat_per_HPI	0.0	10	750	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]
173828	catalase_peroxidase_2	0.0	451	747	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	2	750	4	750
UPK95725.1|AA0	0.0	4	751	66	806
UKZ83034.1|AA0	1.26e-312	13	751	61	787
UPM44564.1|AA0	1.19e-310	23	751	5	715
UKZ91589.1|AA0	3.41e-303	6	751	53	789

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5SYV_A	0.0	4	750	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	4	750	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	4	750	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	4	750	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	4	750	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|Q2H7U1|KATG_CHAGB	0.0	4	750	3	739	Catalase-peroxidase OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=katG PE=3 SV=1
sp|Q3BVY2|KATG_XANC5	0.0	4	750	6	747	Catalase-peroxidase OS=Xanthomonas campestris pv. vesicatoria (strain 85-10) OX=316273 GN=katG PE=3 SV=1
sp|Q2TW34|KATG_ASPOR	0.0	1	751	1	751	Catalase-peroxidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=katG PE=3 SV=1
sp|Q2SZ20|KATG_BURTA	0.0	4	750	6	727	Catalase-peroxidase OS=Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) OX=271848 GN=katG PE=3 SV=1
sp|Q7Z7W6|KATG_ASPFU	0.0	3	751	4	750	Catalase-peroxidase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=katG PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000083	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AO090010000722-T-p1.