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CAZyme Information: MGYG000003943_00129

You are here: Home > Sequence: MGYG000003943_00129

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 NSJ-50 sp014385105
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810; NSJ-50; NSJ-50 sp014385105
CAZyme ID MGYG000003943_00129
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
561 MGYG000003943_1|CGC4 63306.61 4.3712
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003943 2095283 MAG United Kingdom Europe
Gene Location Start: 133627;  End: 135312  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003943_00129.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 130 253 7.9e-17 0.39933993399339934

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 4.21e-32 466 558 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 4.63e-08 449 495 46 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 5.31e-07 528 561 1 34
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.
pfam02156 Glyco_hydro_26 4.97e-05 121 283 121 299
Glycosyl hydrolase family 26.
COG4124 ManB2 1.16e-04 128 270 159 296
Beta-mannanase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUO18272.1 2.24e-92 23 438 183 623
AUO19576.1 1.58e-81 39 556 43 576
AEI42662.1 6.84e-49 29 560 133 668
AFH64572.2 9.65e-49 29 560 136 671
AFC32267.1 9.65e-49 29 560 136 671

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2DDX_A 3.03e-08 113 217 71 184
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 2.93e-07 113 217 93 206
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
0.000639 0.997684 0.000969 0.000243 0.000224 0.000213

TMHMM  Annotations      download full data without filtering help

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