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CAZyme Information: MGYG000001437_01693

You are here: Home > Sequence: MGYG000001437_01693

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 Staphylococcus schleiferi
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus schleiferi
CAZyme ID MGYG000001437_01693
CAZy Family GH35
CAZyme Description Beta-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
590 MGYG000001437_2|CGC5 68796.95 5.7517
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001437 2461191 Isolate not provided not provided
Gene Location Start: 360326;  End: 362098  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23 3.2.1.38 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH35 10 328 1.1e-126 0.993485342019544

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01301 Glyco_hydro_35 1.02e-155 9 328 1 316
Glycosyl hydrolases family 35.
COG1874 GanA 9.94e-81 3 575 1 594
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
PLN03059 PLN03059 1.04e-59 6 583 26 725
beta-galactosidase; Provisional
pfam02449 Glyco_hydro_42 2.66e-08 30 170 8 160
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAD7358615.1 0.0 1 590 1 590
QGS46428.1 0.0 1 590 1 590
QPA34679.1 0.0 1 590 1 590
QPA24449.1 0.0 1 590 1 590
AKS68240.1 0.0 1 590 1 590

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4E8C_A 1.67e-251 1 590 1 590
Crystalstructure of streptococcal beta-galactosidase in complex with galactose [Streptococcus pneumoniae TIGR4],4E8C_B Crystal structure of streptococcal beta-galactosidase in complex with galactose [Streptococcus pneumoniae TIGR4],4E8D_A Crystal structure of streptococcal beta-galactosidase [Streptococcus pneumoniae TIGR4],4E8D_B Crystal structure of streptococcal beta-galactosidase [Streptococcus pneumoniae TIGR4]
4MAD_A 5.31e-142 1 585 15 591
ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans]
6EON_A 2.80e-124 4 585 28 607
GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482]
3D3A_A 4.15e-119 4 585 8 587
Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7KDV_A 4.88e-108 8 572 23 607
ChainA, Beta-galactosidase [Mus musculus],7KDV_C Chain C, Beta-galactosidase [Mus musculus],7KDV_E Chain E, Beta-galactosidase [Mus musculus],7KDV_G Chain G, Beta-galactosidase [Mus musculus],7KDV_I Chain I, Beta-galactosidase [Mus musculus],7KDV_K Chain K, Beta-galactosidase [Mus musculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P48982 6.92e-120 10 554 37 573
Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1
Q3UPY5 1.30e-113 10 581 54 626
Beta-galactosidase-1-like protein 2 OS=Mus musculus OX=10090 GN=Glb1l2 PE=1 SV=1
Q8IW92 7.34e-109 10 570 54 613
Beta-galactosidase-1-like protein 2 OS=Homo sapiens OX=9606 GN=GLB1L2 PE=1 SV=1
P23780 1.17e-106 8 572 40 624
Beta-galactosidase OS=Mus musculus OX=10090 GN=Glb1 PE=1 SV=1
Q58D55 2.71e-106 10 590 40 646
Beta-galactosidase OS=Bos taurus OX=9913 GN=GLB1 PE=2 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
1.000052 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001437_01693.