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CAZyme Information: MGYG000001468_00621

You are here: Home > Sequence: MGYG000001468_00621

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Blastococcus massiliensis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Geodermatophilaceae; Blastococcus; Blastococcus massiliensis
CAZyme ID MGYG000001468_00621
CAZy Family AA2
CAZyme Description Catalase-peroxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
739 MGYG000001468_1|CGC3 80966.27 4.518
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001468 3864310 Isolate not provided not provided
Gene Location Start: 619668;  End: 621887  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001468_00621.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 80 195 2.3e-16 0.44313725490196076

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR00198 cat_per_HPI 0.0 24 738 5 713
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]
COG0376 KatG 0.0 18 739 13 730
Catalase (peroxidase I) [Inorganic ion transport and metabolism].
cd00649 catalase_peroxidase_1 0.0 30 440 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.
PRK15061 PRK15061 0.0 24 739 7 726
catalase/peroxidase.
cd08200 catalase_peroxidase_2 1.28e-160 444 735 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QZY04649.1 1.69e-274 33 738 3 714
QPC71243.1 1.63e-257 26 739 50 774
BCS24344.1 1.76e-27 72 420 6 265
QQK46267.1 2.35e-26 72 420 5 264
BCR82705.1 4.40e-26 72 420 6 265

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5KSG_A 2.29e-318 24 738 8 727
Crystalstructure of the W153F variant of catalase-peroxidase from B. pseudomallei treated with isoniazid [Burkholderia pseudomallei 1710b],5KSG_B Crystal structure of the W153F variant of catalase-peroxidase from B. pseudomallei treated with isoniazid [Burkholderia pseudomallei 1710b]
5L05_A 4.83e-318 24 738 8 727
Crystalstructure of catalase-peroxidase KATG of burkholderia pseudomallei treated with INH [Burkholderia pseudomallei 1710b],5L05_B Crystal structure of catalase-peroxidase KATG of burkholderia pseudomallei treated with INH [Burkholderia pseudomallei 1710b],5SW6_A Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6 [Burkholderia pseudomallei 1710b],5SW6_B Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6 [Burkholderia pseudomallei 1710b],5SX0_B Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH7.5 [Burkholderia pseudomallei 1710b],5SX3_A Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5 [Burkholderia pseudomallei 1710b],5SX3_B Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5 [Burkholderia pseudomallei 1710b],5SXQ_A Crystal structure of B. pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXQ_B Crystal structure of B. pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXS_A Crystal structure of catalase-peroxidase KatG with isonicotinic acid hydrazide and AMP bound [Burkholderia pseudomallei 1710b],5SXS_B Crystal structure of catalase-peroxidase KatG with isonicotinic acid hydrazide and AMP bound [Burkholderia pseudomallei 1710b],5SYL_A B. pseudomallei KatG with KCN bound [Burkholderia pseudomallei 1710b],5SYL_B B. pseudomallei KatG with KCN bound [Burkholderia pseudomallei 1710b],6MPY_A B. pseudomallei KatG crystallized in the presence of benzoyl hydrazide [Burkholderia pseudomallei],6MPY_B B. pseudomallei KatG crystallized in the presence of benzoyl hydrazide [Burkholderia pseudomallei],6MQ0_A B. pseudomallei KatG crystallized in the presence of furoyl hydrazide [Burkholderia pseudomallei],6MQ0_B B. pseudomallei KatG crystallized in the presence of furoyl hydrazide [Burkholderia pseudomallei],6MQ1_A Chain A, Catalase-peroxidase [Burkholderia pseudomallei],6MQ1_B Chain B, Catalase-peroxidase [Burkholderia pseudomallei]
5SX0_A 1.35e-317 24 738 8 727
Crystalstructure of an oxoferryl species of catalase-peroxidase KatG at pH7.5 [Burkholderia pseudomallei 1710b]
5SXT_A 1.35e-317 24 738 8 727
Crystalstructure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXT_B Crystal structure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b]
5KSN_A 1.91e-317 24 738 8 727
Crystalstructure of the S324G variant of catalase-peroxidase from B. pseudomallei with INH bound [Burkholderia pseudomallei 1710b],5KSN_B Crystal structure of the S324G variant of catalase-peroxidase from B. pseudomallei with INH bound [Burkholderia pseudomallei 1710b]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q04657 0.0 10 739 17 746
Catalase-peroxidase OS=Mycobacterium intracellulare OX=1767 GN=katG PE=3 SV=1
Q24YU1 0.0 28 738 17 729
Catalase-peroxidase OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=katG PE=3 SV=1
Q11KP9 0.0 28 738 15 725
Catalase-peroxidase OS=Chelativorans sp. (strain BNC1) OX=266779 GN=katG PE=3 SV=1
Q0S5Y0 0.0 10 738 13 741
Catalase-peroxidase OS=Rhodococcus jostii (strain RHA1) OX=101510 GN=katG PE=3 SV=1
Q2FSF4 0.0 30 737 19 729
Catalase-peroxidase OS=Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) OX=323259 GN=katG PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001468_00621.