CAZyme Information: EPrPIT00000023155-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000023155-p1
• CAZy Family: GH81
• CAZyme Description: Catalase-peroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
688		73922.48	5.9017

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC1157:3731-5797(+)

Full Sequence      

MNIRVTTLLAAIAALTVGDVFASKCPFGYDAQAAIPGQDRTLSSEQYASANCDTIDYDAV
KKDLTFLMTDSKDFWPADFGHYGGLMIRLAWHCNGSYRVSDGRGGCDGGRIRFNPERAWE
DNTNLDKALTLLEPVKQKYGNALSWGDLVVLAGNVAIESMGGPVLGFCGGRRDDADGTNS
IQLGPTPEQAAIAPCAVNGQCKSPLGPTTIGLIYVNPEGPMGNPDPTLSVADIRDTFARM
GMNDRETVALIGGGHAFGKTHGACTTGAGPGPLKDPVHPWPGTCGDGPLKGKGNNTFTSG
FEGAWTFTPTKWGNGYFRGLTGLTWEKFIGPGGHNQWRPVPETNPPVRMLTADIALLKDP
SYLAIAKEFATNLTSLNDAFAHAWYKLTSRDMGPVARCRGNNIPSAQPFQNPLPAAPAKL
PDFNAVRSNIKALLNTASSGLTSDKSGYGKPYNGALFINAAWQCASTFRLTDYAGGCNGA
KIRFAPQKDWPANAGVDKVIAALEPIKKQFPDLSTADLIVLAGSVALEDAGSSKIDFLGG
RVDALDGSGVEHLAPREYYSTALIAVRDNMKIMGLTKYDAVALAGRPRSPVQQKTLGFKG
SYTTDPSKFSNQYFKLLLTEKWTKVSAKEYKADGKDIYMLDTDVALLEDVELKEVVQAYA
DDDEIFSFAFADAWAKLMTADHYNTDSY

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	459	681	9e-30	0.8862745098039215
AA2	77	188	3.2e-24	0.42745098039215684

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223453	KatG	0.0	54	684	66	728	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
237891	PRK15061	0.0	54	681	53	721	catalase/peroxidase.
272957	cat_per_HPI	7.14e-173	55	684	52	712	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	2.44e-152	54	404	41	405	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.
173823	plant_peroxidase_like	2.18e-56	77	389	12	255	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPT50360.1|AA0	0.0	1	688	1	687
UIZ20725.1|AA0	0.0	1	688	1	687
UIZ20718.1|AA0	0.0	1	688	1	687
UPM44564.1|AA0	1.05e-134	55	686	41	715
UKZ91289.1|AA0	7.67e-134	54	684	56	749

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ITK_A	6.22e-135	55	686	59	731	Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
5WHQ_A	8.70e-135	54	684	68	755	Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A [Neurospora crassa OR74A],5WHQ_B Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A [Neurospora crassa OR74A]
3UW8_A	2.05e-134	55	686	59	731	Crystal Structure Analysis of the Ser305Thr Variants of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3UW8_B Crystal Structure Analysis of the Ser305Thr Variants of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049]
3VLK_A	2.05e-134	55	686	59	731	Crystal Structure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLK_B Crystal Structure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLL_A Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA [Haloarcula marismortui ATCC 43049],3VLL_B Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA [Haloarcula marismortui ATCC 43049]
3VLM_A	5.73e-134	55	686	59	731	Crystal Structure Analysis of the Met244Ala Variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLM_B Crystal Structure Analysis of the Met244Ala Variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q88GQ0|KATG_PSEPK	8.81e-147	54	684	53	749	Catalase-peroxidase OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=katG PE=3 SV=1
sp|A5W241|KATG_PSEP1	8.81e-147	54	684	53	749	Catalase-peroxidase OS=Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) OX=351746 GN=katG PE=3 SV=1
sp|Q1IAY6|KATG_PSEE4	2.85e-146	54	684	54	742	Catalase-peroxidase OS=Pseudomonas entomophila (strain L48) OX=384676 GN=katG PE=3 SV=1
sp|Q9WXB9|KATG2_LEGPN	3.64e-145	54	684	70	739	Catalase-peroxidase 2 OS=Legionella pneumophila OX=446 GN=katG2 PE=2 SV=1
sp|Q5ZZ17|KATG2_LEGPH	3.64e-145	54	684	70	739	Catalase-peroxidase 2 OS=Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) OX=272624 GN=katG2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000218	0.999770	CS pos: 22-23. Pr: 0.9755

TMHMM  Annotations     

There is no transmembrane helices in EPrPIT00000023155-p1.