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CAZyme Information: MGYG000000163_02015

You are here: Home > Sequence: MGYG000000163_02015

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 Enterococcus_C asini
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_C; Enterococcus_C asini
CAZyme ID MGYG000000163_02015
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
879 100131.49 5.3847
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000163 2560364 Isolate China Asia
Gene Location Start: 70748;  End: 73387  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000163_02015.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 221 583 2.3e-96 0.9865229110512129
CE12 2 203 2.1e-55 0.9904761904761905

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02449 Glyco_hydro_42 8.27e-102 221 583 1 371
Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.
COG1874 GanA 6.99e-90 217 869 17 670
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
cd01821 Rhamnogalacturan_acetylesterase_like 1.81e-55 2 204 2 198
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
COG2755 TesA 1.10e-18 2 206 10 210
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229 SGNH_hydrolase 2.29e-17 3 202 1 186
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGN30568.1 0.0 1 876 1 877
AMG48416.1 0.0 1 871 1 872
AUJ86489.1 0.0 1 871 1 872
AYJ44998.1 0.0 1 871 1 872
AIZ15679.1 7.79e-211 132 871 109 837

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LVW_A 1.25e-62 219 695 4 494
PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239]
1KWG_A 5.33e-61 219 870 3 643
Crystalstructure of Thermus thermophilus A4 beta-galactosidase [Thermus thermophilus],1KWK_A Crystal structure of Thermus thermophilus A4 beta-galactosidase in complex with galactose [Thermus thermophilus]
4UCF_A 2.27e-54 214 772 18 580
Crystalstructure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_B Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_C Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UZS_A Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_B Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_C Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17]
5E9A_A 2.80e-46 218 869 41 706
Crystalstructure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_B Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_C Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_D Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_E Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_F Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3]
6Y2K_A 2.92e-46 219 714 4 522
ChainA, beta-galactosidase [Marinomonas sp. ef1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q65KX8 1.09e-139 215 869 4 657
Beta-galactosidase YesZ OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=yesZ PE=3 SV=2
O31529 1.17e-134 215 871 3 659
Beta-galactosidase YesZ OS=Bacillus subtilis (strain 168) OX=224308 GN=yesZ PE=1 SV=1
P94804 7.50e-63 219 692 4 487
Beta-galactosidase BgaH OS=Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) OX=1230452 GN=bgaH PE=1 SV=2
B9LW38 6.83e-62 219 695 4 494
Beta-galactosidase Bga OS=Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) OX=416348 GN=Hlac_2868 PE=1 SV=1
O69315 2.92e-60 219 870 3 643
Beta-galactosidase OS=Thermus thermophilus OX=274 PE=1 SV=1

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
1.000024 0.000008 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000163_02015.