logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002683_02131

You are here: Home > Sequence: MGYG000002683_02131

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
Lineage Bacteria; Firmicutes_A; Clostridia; RUG12999; RUG12999; ;
CAZyme ID MGYG000002683_02131
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
640 MGYG000002683_193|CGC1 70817.15 4.6633
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002683 3225682 MAG Canada North America
Gene Location Start: 1561;  End: 3483  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002683_02131.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 220 378 4.1e-16 0.44884488448844884

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.69e-32 546 638 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 8.08e-12 493 576 19 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 6.75e-06 609 640 2 33
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 9.65e-05 248 388 200 318
Beta-mannanase [Carbohydrate transport and metabolism].
pfam02156 Glyco_hydro_26 0.005 257 314 183 235
Glycosyl hydrolase family 26.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AMJ39775.1 2.12e-64 10 522 13 532
AUO19576.1 3.35e-52 140 638 64 579
BAD39558.1 1.87e-51 80 629 18 577
ALS21301.1 7.32e-49 142 638 173 666
AFH64572.2 3.71e-48 192 638 232 669

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2DDX_A 3.59e-07 207 350 81 218
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 3.29e-06 207 350 103 240
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
0.001645 0.531312 0.466414 0.000236 0.000192 0.000187

TMHMM  Annotations      download full data without filtering help

start end
5 27