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CAZyme Information: MGYG000000143_00294

You are here: Home > Sequence: MGYG000000143_00294

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 Turicibacter sanguinis
Lineage Bacteria; Firmicutes; Bacilli; Haloplasmatales_A; Turicibacteraceae; Turicibacter; Turicibacter sanguinis
CAZyme ID MGYG000000143_00294
CAZy Family GH42
CAZyme Description Beta-galactosidase BglY
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
677 MGYG000000143_1|CGC7 78409.89 5.6286
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000143 2958073 Isolate United Kingdom Europe
Gene Location Start: 306964;  End: 308997  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 16 388 4.9e-155 0.9946091644204852

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1874 GanA 0.0 11 676 16 671
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam02449 Glyco_hydro_42 0.0 16 390 1 376
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.
pfam08532 Glyco_hydro_42M 4.54e-79 401 613 2 207
Beta-galactosidase trimerisation domain. This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation.
cd03143 A4_beta-galactosidase_middle_domain 6.79e-37 402 612 1 154
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.
pfam08533 Glyco_hydro_42C 1.59e-04 623 676 1 57
Beta-galactosidase C-terminal domain. This domain is found at the C-terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJS18191.1 0.0 1 677 1 677
AMC08162.1 0.0 1 675 1 675
ABX31553.1 9.63e-312 8 646 12 653
ANY74983.1 2.07e-305 12 676 10 680
CEP78374.1 1.25e-303 8 676 12 684

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5E9A_A 8.16e-272 8 652 36 683
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]
4OIF_A 8.08e-238 12 676 16 683
3Dstructure of Gan42B, a GH42 beta-galactosidase from G. [Geobacillus stearothermophilus],4OIF_B 3D structure of Gan42B, a GH42 beta-galactosidase from G. [Geobacillus stearothermophilus],4OIF_C 3D structure of Gan42B, a GH42 beta-galactosidase from G. [Geobacillus stearothermophilus]
4OJY_A 8.37e-238 12 676 17 684
3Dstructure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],4OJY_B 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],4OJY_C 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus]
5DFA_A 6.54e-237 12 676 16 683
3Dstructure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],5DFA_B 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],5DFA_C 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus]
3TTS_A 4.01e-185 13 647 11 644
ChainA, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_A Chain A, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q0TUR6 2.82e-271 8 676 11 687
Beta-galactosidase Pbg OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=pbg PE=3 SV=1
C8WV58 5.90e-268 7 645 10 651
Beta-galactosidase BglY OS=Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) OX=521098 GN=bglY PE=1 SV=1
Q65CX4 4.12e-224 12 638 2 632
Beta-galactosidase GalA 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=lacA PE=1 SV=2
O07012 2.98e-221 12 675 2 668
Beta-galactosidase GanA OS=Bacillus subtilis (strain 168) OX=224308 GN=ganA PE=1 SV=2
Q9KI47 2.91e-196 13 675 11 674
Beta-galactosidase BgaA OS=Planococcus sp. (strain 'SOS Orange') OX=128803 GN=bgaA 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
1.000063 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000143_00294.