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CAZyme Information: MGYG000000054_03672

You are here: Home > Sequence: MGYG000000054_03672

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 Bacteroides acidifaciens
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides acidifaciens
CAZyme ID MGYG000000054_03672
CAZy Family GH78
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
832 93852.12 8.3458
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000054 5213730 Isolate United Kingdom Europe
Gene Location Start: 8078;  End: 10576  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000054_03672.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 1 430 6e-124 0.7896825396825397
GH33 465 816 1.8e-37 0.9093567251461988

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 4.47e-152 2 363 1 340
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.
pfam13088 BNR_2 1.31e-98 482 812 1 279
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd15482 Sialidase_non-viral 1.11e-45 461 828 4 339
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
COG4692 COG4692 1.23e-30 467 830 29 374
Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
pfam17390 Bac_rhamnosid_C 1.34e-22 365 445 1 78
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
QIU95828.1 0.0 1 832 457 1288
QRQ56894.1 0.0 1 832 455 1286
ALJ45265.1 0.0 1 832 455 1286
SCV09602.1 0.0 1 832 455 1286
QUR43127.1 0.0 1 832 455 1286

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6I60_A 4.15e-77 1 431 462 899
Structureof alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
3W5M_A 1.78e-55 4 438 599 1002
CrystalStructure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6GSZ_A 9.82e-36 1 447 426 865
Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q82PP4 9.25e-55 4 438 599 1002
Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 PE=1 SV=1
T2KNB2 4.93e-52 5 460 474 905
Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22090 PE=1 SV=2
P9WF03 1.05e-46 6 431 471 879
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KPL4 4.88e-42 1 456 486 933
Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1
T2KM26 6.41e-13 2 432 728 1138
Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2

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
1.000037 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000054_03672.