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CAZyme Information: MGYG000002213_00193

You are here: Home > Sequence: MGYG000002213_00193

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UMGS1872;
CAZyme ID MGYG000002213_00193
CAZy Family GH42
CAZyme Description Beta-galactosidase BgaA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
650 MGYG000002213_6|CGC1 73993.71 5.0117
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002213 2465575 MAG Spain Europe
Gene Location Start: 20277;  End: 22229  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002213_00193.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 6 380 2e-126 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 8.32e-140 6 382 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 2.63e-131 1 635 16 644
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam08532 Glyco_hydro_42M 4.01e-53 392 601 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 5.03e-26 394 525 1 133
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
QQQ99503.1 0.0 1 647 1 647
ANU45745.1 0.0 1 647 1 647
QIX93296.1 0.0 1 647 1 647
AVQ18862.1 1.19e-300 1 646 1 646
QNM14994.1 2.13e-291 1 649 1 647

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3TTS_A 2.67e-100 1 637 9 645
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]
1KWG_A 4.76e-95 3 615 2 604
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]
6LVW_A 1.41e-92 1 491 1 497
PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239]
4OIF_A 1.42e-84 4 585 18 601
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 1.45e-84 4 585 19 602
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D9SM34 6.46e-122 1 636 1 628
Beta-galactosidase BgaA OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=bgaA PE=1 SV=1
P19668 3.51e-100 4 631 10 628
Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1
C9S0R2 5.25e-99 4 631 10 628
Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB PE=3 SV=1
Q9X6C6 2.31e-96 3 646 2 641
Beta-galactosidase BgaT OS=Thermus brockianus OX=56956 GN=bgaT PE=1 SV=1
D5JGG0 7.45e-96 2 641 9 638
Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 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
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002213_00193.