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CAZyme Information: MGYG000003964_01053

You are here: Home > Sequence: MGYG000003964_01053

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 UBA1740 sp004558975
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UBA1740; UBA1740 sp004558975
CAZyme ID MGYG000003964_01053
CAZy Family CBM67
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
728 82260.82 4.9572
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003964 1589582 MAG United Kingdom Europe
Gene Location Start: 19936;  End: 22122  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003964_01053.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 215 704 1.4e-87 0.9742063492063492
CBM67 8 145 1e-22 0.7386363636363636

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 6.08e-14 325 638 14 338
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.
COG3408 GDB1 9.57e-07 374 677 304 634
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
pfam17390 Bac_rhamnosid_C 1.70e-05 648 709 2 66
Bacterial alpha-L-rhamnosidase C-terminal 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.
pfam02837 Glyco_hydro_2_N 2.62e-04 34 97 83 144
Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
PRK09525 lacZ 4.79e-04 45 87 153 190
beta-galactosidase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBH24613.1 1.27e-127 11 725 21 803
AZN43562.1 2.70e-117 3 709 16 799
QTH43327.1 6.43e-117 14 722 24 796
QNK59208.1 2.91e-116 30 709 33 757
ALS28317.1 1.52e-115 20 709 35 780

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2OKX_A 2.88e-43 260 709 476 944
Crystalstructure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1],2OKX_B Crystal structure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1]
3CIH_A 2.23e-16 215 681 196 674
Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

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
1.000091 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003964_01053.