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CAZyme Information: MGYG000001222_00650

You are here: Home > Sequence: MGYG000001222_00650

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 UMGS1326 sp900550775
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; UMGS1326; UMGS1326 sp900550775
CAZyme ID MGYG000001222_00650
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
560 63175.04 4.5179
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001222 2203618 MAG Austria Europe
Gene Location Start: 44940;  End: 46622  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001222_00650.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 130 251 5.7e-17 0.3927392739273927

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 3.52e-37 466 558 1 93
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam07833 Cu_amine_oxidN1 9.63e-14 424 495 24 92
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam07833 Cu_amine_oxidN1 1.83e-07 528 559 1 32
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
COG4124 ManB2 1.14e-06 128 251 159 290
Beta-mannanase [Carbohydrate transport and metabolism].
pfam02156 Glyco_hydro_26 1.64e-04 126 222 133 235
Glycosyl hydrolase family 26.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUO18272.1 3.47e-107 23 438 183 623
AUO19576.1 4.23e-81 39 558 43 579
BAD39558.1 6.97e-57 84 558 117 586
AFH64572.2 3.44e-56 29 558 136 669
AFC32267.1 3.44e-56 29 558 136 669

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2DDX_A 9.28e-07 102 215 68 182
Crystalstructure of beta-1,3-xylanase from Vibrio sp. AX-4 [Vibrio sp. AX-4],3VPL_A Crystal structure of a 2-fluoroxylotriosyl complex of the Vibrio sp. AX-4 Beta-1,3-xylanase [Vibrio sp.]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D5MP61 8.13e-06 102 215 90 204
Beta-1,3-xylanase XYL4 OS=Vibrio sp. OX=678 GN=xyl4 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000294 0.998937 0.000199 0.000196 0.000185 0.000162

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001222_00650.