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CAZyme Information: MGYG000001240_01107

You are here: Home > Sequence: MGYG000001240_01107

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 Prevotella sp900557405
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900557405
CAZyme ID MGYG000001240_01107
CAZy Family CBM67
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1321 MGYG000001240_28|CGC1 148810.95 7.5396
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001240 2497614 MAG Austria Europe
Gene Location Start: 18958;  End: 22923  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001240_01107.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 377 910 3.9e-150 0.998015873015873
GH33 935 1305 1.7e-31 0.935672514619883
CBM67 162 351 6.2e-27 0.9375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 7.11e-119 486 843 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.
pfam13088 BNR_2 8.19e-84 962 1303 1 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam08531 Bac_rhamnosid_N 1.20e-52 195 368 1 170
Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd15482 Sialidase_non-viral 6.65e-38 941 1318 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.
pfam05592 Bac_rhamnosid 9.68e-35 378 478 1 101
Bacterial alpha-L-rhamnosidase concanavalin-like 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
BCS84864.1 0.0 50 1321 13 1269
QNT66960.1 0.0 10 1321 6 1326
QNL37629.1 0.0 48 1318 29 1284
QIU95828.1 0.0 48 1318 29 1284
QGT69954.1 0.0 48 1321 27 1285

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6I60_A 3.51e-165 56 911 43 899
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 1.58e-115 51 911 12 995
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 6.49e-96 51 928 10 866
Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
2OKX_A 1.42e-10 340 923 398 954
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]
4X6K_A 2.38e-06 1085 1317 240 471
Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
T2KPL4 6.56e-127 47 925 34 921
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
T2KNB2 6.35e-123 49 938 40 910
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 3.38e-117 51 911 38 879
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
Q82PP4 6.65e-115 51 911 12 995
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
T2KM26 2.34e-23 297 916 513 1142
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.004708 0.993772 0.000731 0.000301 0.000229 0.000225

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001240_01107.