logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002279_00109

You are here: Home > Sequence: MGYG000002279_00109

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 Dorea_A longicatena_B
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Dorea_A; Dorea_A longicatena_B
CAZyme ID MGYG000002279_00109
CAZy Family GH42
CAZyme Description Beta-galactosidase BglY
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
676 MGYG000002279_1|CGC3 77998.33 6.3696
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002279 3143549 Isolate China Asia
Gene Location Start: 130523;  End: 132553  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 13 383 9.6e-147 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 5 671 13 671
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam02449 Glyco_hydro_42 8.80e-174 13 385 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 6.34e-69 397 610 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 1.53e-31 399 530 1 132
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 7.85e-06 619 672 1 58
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
QHB24566.1 0.0 8 674 11 675
QEI32069.1 0.0 8 674 11 675
QRT30718.1 0.0 1 669 6 670
QJU15391.1 5.83e-305 9 669 11 670
ANU74556.1 2.36e-304 9 669 11 670

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5E9A_A 2.40e-248 6 648 37 680
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 1.64e-216 9 655 16 663
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 1.70e-216 9 655 17 664
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 1.32e-215 9 655 16 663
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 1.72e-166 10 657 11 656
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
C8WV58 9.35e-247 6 639 12 645
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
Q0TUR6 2.61e-226 9 639 15 650
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
O07012 1.62e-207 9 640 2 634
Beta-galactosidase GanA OS=Bacillus subtilis (strain 168) OX=224308 GN=ganA PE=1 SV=2
Q65CX4 1.67e-207 9 647 2 641
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
Q09HN2 1.17e-175 10 640 11 638
Beta-galactosidase BgaP OS=Planococcus sp. (strain L4) OX=377621 GN=bgaP 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
1.000057 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002279_00109.