logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002872_01955

You are here: Home > Sequence: MGYG000002872_01955

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 UMGS874 sp900546315
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS874; UMGS874 sp900546315
CAZyme ID MGYG000002872_01955
CAZy Family GH116
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
835 93613.96 4.855
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002872 3007809 MAG United States North America
Gene Location Start: 11578;  End: 14085  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002872_01955.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH116 440 734 3.9e-55 0.7245179063360881

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam12215 Glyco_hydr_116N 2.22e-54 16 322 2 309
beta-glucosidase 2, glycosyl-hydrolase family 116 N-term. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N-terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335 in the downstream family pfam04685.
COG4354 COG4354 3.64e-42 17 742 16 721
Uncharacterized protein, contains GBA2_N and DUF608 domains [Function unknown].
pfam04685 DUF608 1.97e-40 387 734 19 362
Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.
pfam17389 Bac_rhamnosid6H 1.16e-05 415 560 77 215
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZN43107.1 1.37e-293 6 823 5 847
ANE45793.1 6.12e-293 3 797 2 822
QUH30377.1 1.27e-291 6 831 4 856
QHT59778.1 2.46e-291 6 823 5 847
AEE95836.1 9.79e-290 6 799 8 835

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7DKW_A 9.33e-25 17 704 59 744
ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKW_B Chain B, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKX_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKY_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]
7W2V_A 3.99e-24 17 729 102 817
ChainA, Glucosylceramidase [Thermoanaerobacterium xylanolyticum LX-11]
7DKS_A 4.93e-24 17 704 59 744
ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKT_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKU_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKV_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]
5FJS_A 8.40e-24 17 704 55 740
Bacterialbeta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5FJS_B Bacterial beta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5O0S_A Crystal structure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with unreacted beta Cyclophellitol Cyclosulfate probe ME711 [Thermoanaerobacterium xylanolyticum LX-11]
5NPF_A 8.56e-24 17 704 58 743
Crystalstructure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with beta Cyclophellitol Cyclosulfate probe ME594 [Thermoanaerobacterium xylanolyticum]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.999979 0.000087 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002872_01955.