logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002943_00938

You are here: Home > Sequence: MGYG000002943_00938

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 Actinomyces oris
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces oris
CAZyme ID MGYG000002943_00938
CAZy Family GH42
CAZyme Description Beta-galactosidase bgaB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
759 81829.04 5.0196
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002943 3026158 MAG United States North America
Gene Location Start: 684;  End: 2963  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 40 407 1.4e-157 0.9946091644204852

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02449 Glyco_hydro_42 0.0 40 409 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.
COG1874 GanA 2.91e-137 37 745 18 672
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam08532 Glyco_hydro_42M 8.32e-28 419 684 1 207
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 1.74e-15 421 542 1 123
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 4.95e-06 693 743 1 56
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
QQQ58730.1 0.0 1 744 1 733
QLF54010.1 0.0 1 744 1 744
QQC40080.1 0.0 1 744 1 733
AMD99363.1 0.0 1 742 1 731
QCT33733.1 0.0 1 743 1 743

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UCF_A 6.16e-133 26 577 10 584
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]
3TTS_A 1.62e-132 37 745 11 674
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]
5E9A_A 6.48e-128 37 709 41 671
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]
4UNI_A 2.41e-126 37 601 25 602
beta-(1,6)-galactosidasefrom Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UNI_B beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UNI_C beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04]
4UOQ_A 1.86e-125 37 601 25 602
Nucleophilemutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOQ_B Nucleophile mutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOQ_C Nucleophile mutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_A beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_B beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_C beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C7ASJ5 2.19e-177 37 733 44 683
Beta-galactosidase OS=Arthrobacter sp. OX=1667 PE=1 SV=1
P19668 8.42e-159 32 710 4 626
Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1
C9S0R2 3.72e-157 32 710 4 626
Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB PE=3 SV=1
D5JGG0 2.32e-153 37 743 10 660
Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1
Q9RFN0 2.66e-139 37 538 9 510
Beta-galactosidase BgaB OS=Carnobacterium maltaromaticum OX=2751 GN=bgaB 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
0.995732 0.004294 0.000008 0.000006 0.000004 0.000005

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002943_00938.