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CAZyme Information: MGYG000004105_01164

You are here: Home > Sequence: MGYG000004105_01164

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 Alistipes_A sp900546005
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900546005
CAZyme ID MGYG000004105_01164
CAZy Family GH78
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
546 MGYG000004105_5|CGC3 62909.81 5.0637
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004105 2464466 MAG United Kingdom Europe
Gene Location Start: 207497;  End: 209137  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.40

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 88 540 1.2e-75 0.8591269841269841

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 7.44e-21 207 540 8 339
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 6.80e-05 298 427 337 479
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
TIGR01577 oligosac_amyl 7.51e-04 312 443 365 480
oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGA22924.1 4.39e-312 20 546 20 546
QIX67530.1 7.26e-244 4 546 2 542
AST55162.1 1.23e-243 4 546 7 547
QUT93874.1 1.23e-243 4 546 7 547
QUT21624.1 2.94e-243 4 546 2 542

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4XHC_A 2.19e-119 35 540 39 541
ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]
3CIH_A 2.68e-22 91 540 194 635
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000515 0.992614 0.006201 0.000273 0.000198 0.000176

TMHMM  Annotations      download full data without filtering help

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