CAZyme Information: ASPZODRAFT_132364-t33_1-p1

Basic Information

• Species: Penicilliopsis zonata
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata
• CAZyme ID: ASPZODRAFT_132364-t33_1-p1
• CAZy Family: GT62
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
769	KV878341|CGC3	83687.40	6.4656

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PzonataCBS506.65	10027	1073090	158	9869

• Gene Location: location=KV878341:1469790-1472167(+)

Full Sequence      

MAKCPMDDMLRSGAAGAGTRNRDWWPSQLKLNILRQHGEASNPLRDQDYAAAFNSLDYFG
VKKDLAALMTDSQEWWPADFGHYGGLFVRMAWHSAGTYRVFDGRGGGGQGQQRFAPLNSW
PDNVSLDKARRLLWPIKQKYGDKISWADLLLLTGNVALETMGLQTFGFAGGRVDTWEADE
ATNWGGETTWLGNEVRYAAGGGSEGVVKDAGQAVLAADEDKPNRDIYTRELKTPVAASHM
GLIYVNPEGPDGQPDPVAAARDIRTTFGRMAMNDEETVALIAGGHSFGKTHGAGPSEQVG
KEPEAAGLEAQGLGWASSFGAGKGPDAITSGLEVTWTKTPTRWSNNFLEYLFRYDWELTK
SPAGAHQWVAKGADAIIPDAFDAAKKHRPQMLTTDLSLRFDPAYEKIARRFLAHPEQLAD
AFARAWFKLLHRDMGPRIRYLGPEVPAEVLAWQDPIPVVDHPLVGPADVESLKQAILASG
VAPASFIATAWASASTFRGSDKRGGANGARIRLAPQRQWAVNAQPWLEEALAALEAIQKQ
FNASQQSAKRVSLADLIVLAGSAAVAQAARAAGHADVAVPFTPGRMDASQEQTEIESFNY
LEPLADGFRNYGKSTPRMHTEALLVDKAQLLGLTAPEMTALVGGLRVLNTNYDGSPLGVF
TARPGTLTNDFFVHLLDMNTKWAPLGPDLYQGTDRKTGAKKWTASRVDLVFGSHAELRAV
AEVYASVDGEAKFVKDFAAAWTKIMDADRFDLKYVSFPVKQIVVRSSKI

Enzyme Prediction     

No EC number prediction in ASPZODRAFT_132364-t33_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
272957	cat_per_HPI	0.0	1	752	1	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	16	450	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	1	753	15	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	0.0	1	753	3	726	catalase/peroxidase.
173828	catalase_peroxidase_2	2.51e-167	454	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	2	752	5	750
UPK95725.1|AA0	0.0	2	752	65	805
UPM44564.1|AA0	1.13e-283	21	753	5	715
UKZ83034.1|AA0	1.00e-281	11	758	61	792
UKZ91589.1|AA0	4.03e-279	3	753	57	789

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6CEK_A	0.0	2	752	5	727	Crystal structure of the D141N variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],6CEK_B Crystal structure of the D141N variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
5KQK_A	0.0	2	752	5	727	Crystal structure of the Q233E/N240D variant of the catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5KQK_B Crystal structure of the Q233E/N240D variant of the catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
5KQ0_A	0.0	2	752	5	727	Crystal structure of the A290D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5KQ0_B Crystal structure of the A290D variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b]
6CFQ_A	0.0	2	752	5	727	Crystal structure of the D141N variant of catalase-peroxidase from B. pseudomallei with INH bound [Burkholderia pseudomallei],6CFQ_B Crystal structure of the D141N variant of catalase-peroxidase from B. pseudomallei with INH bound [Burkholderia pseudomallei]
5KSF_A	0.0	2	752	5	727	Crystal structure of the D141A variant of the catalase-peroxidase from B. pseudomallei treated with acetate [Burkholderia pseudomallei 1710b],5KSF_B Crystal structure of the D141A variant of the catalase-peroxidase from B. pseudomallei treated with acetate [Burkholderia pseudomallei 1710b],5SYI_A Structure of D141A variant of B. pseudomallei KatG complexed with INH [Burkholderia pseudomallei 1710b],5SYI_B Structure of D141A variant of B. pseudomallei KatG complexed with INH [Burkholderia pseudomallei 1710b],5SYJ_A Crystal structure of the D141A variant of B. pseudomallei KatGin complex with isoniazid [Burkholderia pseudomallei 1710b],5SYJ_B Crystal structure of the D141A variant of B. pseudomallei KatGin complex with isoniazid [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	1	752	1	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	2	752	5	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	3	752	4	750	Catalase-peroxidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=katG PE=3 SV=1
sp|Q2SZ20|KATG_BURTA	0.0	2	752	5	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	753	5	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
1.000068	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPZODRAFT_132364-t33_1-p1.