logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001283_00429

You are here: Home > Sequence: MGYG000001283_00429

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 Scardovia wiggsiae
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Scardovia; Scardovia wiggsiae
CAZyme ID MGYG000001283_00429
CAZy Family GH42
CAZyme Description Beta-galactosidase BgaB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
761 MGYG000001283_2|CGC5 84532.23 4.9282
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001283 1508369 MAG Italy Europe
Gene Location Start: 204049;  End: 206334  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 66 437 3.5e-147 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 2.51e-179 66 439 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 4.34e-106 57 710 11 641
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam08532 Glyco_hydro_42M 9.92e-55 452 657 1 199
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 3.80e-25 454 576 1 124
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAQ32207.1 0.0 32 754 4 735
QAY32329.1 0.0 45 752 4 695
AZI16129.1 0.0 45 753 4 709
AUD84502.1 0.0 45 753 4 709
AEI98104.1 0.0 45 753 4 709

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UCF_A 3.30e-257 45 718 4 665
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]
4UNI_A 5.34e-237 40 751 2 694
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 4.31e-236 40 751 2 694
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]
3TTS_A 5.04e-119 61 723 9 668
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 5.97e-98 53 659 31 638
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A1A399 3.08e-312 43 751 2 699
Beta-galactosidase BgaB OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=bgaB PE=1 SV=2
D4QFE7 1.81e-256 45 718 4 665
Beta-galactosidase BbgII OS=Bifidobacterium bifidum OX=1681 GN=bbgII PE=3 SV=1
Q93GI5 3.78e-246 46 751 4 690
Beta-galactosidase III OS=Bifidobacterium longum subsp. infantis OX=1682 GN=beta-galIII PE=1 SV=1
C7ASJ5 2.58e-164 60 731 41 686
Beta-galactosidase OS=Arthrobacter sp. OX=1667 PE=1 SV=1
P19668 2.62e-141 61 657 7 589
Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 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
1.000027 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001283_00429.