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CAZyme Information: MGYG000002900_00895

You are here: Home > Sequence: MGYG000002900_00895

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 Actinomyces urogenitalis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces urogenitalis
CAZyme ID MGYG000002900_00895
CAZy Family GH78
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
734 MGYG000002900_20|CGC1 78201.58 4.6924
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002900 2460697 MAG United States North America
Gene Location Start: 30929;  End: 33133  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002900_00895.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 209 705 9.3e-68 0.9325396825396826

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 4.55e-07 309 666 4 340
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.
pfam06202 GDE_C 2.91e-06 393 527 87 228
Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
pfam17390 Bac_rhamnosid_C 5.10e-05 668 704 1 38
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTX05357.1 3.11e-125 51 721 35 664
ANF32625.1 5.33e-119 55 704 3 563
SDT18190.1 7.91e-118 55 704 38 659
QKJ20518.1 6.31e-113 55 706 51 664
QNP55745.1 3.23e-105 55 718 35 668

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3CIH_A 2.06e-37 192 718 176 688
Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
2OKX_A 3.38e-28 303 731 531 937
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]
4XHC_A 5.57e-19 281 664 174 540
ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]

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
1.000036 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002900_00895.