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CAZyme Information: MGYG000001063_06008

You are here: Home > Sequence: MGYG000001063_06008

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 Robinsoniella sp900540475
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475
CAZyme ID MGYG000001063_06008
CAZy Family GH42
CAZyme Description Beta-galactosidase YesZ
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
659 MGYG000001063_157|CGC2 75074.65 5.7116
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001063 7637037 MAG Sweden Europe
Gene Location Start: 46676;  End: 48655  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001063_06008.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 11 370 3.3e-114 0.9811320754716981

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02449 Glyco_hydro_42 4.33e-129 11 370 2 370
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 1.74e-121 2 658 13 671
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam08532 Glyco_hydro_42M 2.47e-26 389 589 2 202
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 4.29e-14 390 491 1 103
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
QHZ46474.1 6.08e-226 1 653 3 655
QSF98233.1 2.35e-223 1 653 3 655
BCE06187.1 6.24e-223 1 653 1 653
BCE12417.1 6.24e-223 1 653 1 653
BCE14042.1 6.24e-223 1 653 1 653

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LVW_A 1.97e-74 8 611 4 621
PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239]
1KWG_A 9.22e-70 8 508 3 516
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]
5E9A_A 1.09e-59 5 583 39 634
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]
3TTS_A 1.62e-59 4 621 8 634
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]
6Y2K_A 3.92e-56 8 517 4 540
ChainA, beta-galactosidase [Marinomonas sp. ef1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q65KX8 2.87e-222 1 653 1 653
Beta-galactosidase YesZ 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=yesZ PE=3 SV=2
O31529 5.50e-212 4 653 3 653
Beta-galactosidase YesZ OS=Bacillus subtilis (strain 168) OX=224308 GN=yesZ PE=1 SV=1
P19668 1.63e-76 7 584 9 587
Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1
D5JGG0 1.96e-76 3 659 6 662
Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1
C9S0R2 1.65e-75 7 584 9 587
Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB 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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001063_06008.