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CAZyme Information: MGYG000001639_00509

You are here: Home > Sequence: MGYG000001639_00509

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 Haloferax massiliensis
Lineage Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Haloferax; Haloferax massiliensis
CAZyme ID MGYG000001639_00509
CAZy Family AA2
CAZyme Description Catalase-peroxidase 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
718 79890.35 3.9094
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001639 3991467 Isolate not provided not provided
Gene Location Start: 523992;  End: 526148  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001639_00509.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 62 174 4.6e-16 0.43137254901960786

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 3 717 14 713
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 4 718 30 730
Catalase (peroxidase I) [Inorganic ion transport and metabolism].
cd00649 catalase_peroxidase_1 0.0 2 412 3 407
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 4 718 17 726
catalase/peroxidase.
cd08200 catalase_peroxidase_2 9.14e-176 418 714 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 0.0 1 718 1 715
QPC71243.1 7.75e-263 7 718 60 774
BCS01357.1 2.09e-32 42 394 6 265
BCS13101.1 2.09e-32 42 394 6 265
QMW47926.1 8.08e-29 42 394 6 265

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3UW8_A 0.0 4 718 22 731
CrystalStructure 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]
1ITK_A 0.0 4 718 22 731
Crystalstructure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3VLM_A 0.0 4 718 22 731
CrystalStructure 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]
3VLH_A 0.0 4 718 22 731
CrystalStructure Analysis of the Arg409Leu Variants of KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLH_B Crystal Structure Analysis of the Arg409Leu Variants of KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLI_A Crystal Structure Analysis of the Cyanide Arg409Leu Variant KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLI_B Crystal Structure Analysis of the Cyanide Arg409Leu Variant KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLJ_A Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLJ_B Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049]
3VLK_A 0.0 4 718 22 731
CrystalStructure 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q3IQZ9 0.0 9 718 9 713
Catalase-peroxidase OS=Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara) OX=348780 GN=katG PE=3 SV=1
O73955 0.0 1 718 1 720
Catalase-peroxidase OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OX=64091 GN=katG PE=3 SV=1
Q24YU1 0.0 7 717 25 729
Catalase-peroxidase OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=katG PE=3 SV=1
Q2RZX7 0.0 1 718 15 729
Catalase-peroxidase OS=Salinibacter ruber (strain DSM 13855 / M31) OX=309807 GN=katG PE=3 SV=1
O59651 0.0 4 718 22 731
Catalase-peroxidase 2 OS=Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) OX=272569 GN=katG2 PE=1 SV=3

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
1.000039 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001639_00509.