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CAZyme Information: MGYG000004233_00640

You are here: Home > Sequence: MGYG000004233_00640

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; Lachnospirales; Lachnospiraceae; Fusicatenibacter;
CAZyme ID MGYG000004233_00640
CAZy Family GH42
CAZyme Description Beta-galactosidase BgaA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
668 76516.22 5.4808
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004233 2952530 MAG United Kingdom Europe
Gene Location Start: 31072;  End: 33078  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004233_00640.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 10 374 1.4e-111 0.9919137466307277

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02449 Glyco_hydro_42 4.75e-70 10 375 2 375
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 4.35e-64 1 666 13 671
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam08532 Glyco_hydro_42M 6.52e-35 387 600 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 1.91e-20 389 599 1 154
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.
cd01653 GATase1 0.001 415 479 7 83
Type 1 glutamine amidotransferase (GATase1)-like domain. Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCU02119.1 0.0 1 665 1 688
QHQ63164.1 0.0 1 665 1 670
CBL23048.1 0.0 1 665 1 663
BCZ46023.1 1.82e-316 1 665 1 663
ANU76468.1 1.12e-313 1 665 1 667

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5XB7_A 2.56e-258 4 668 9 696
GH42alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_B GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_C GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_D GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_E GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_F GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis]
3TTS_A 6.97e-55 3 630 8 638
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 4.97e-53 4 665 39 706
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]
4UOQ_A 3.89e-50 3 662 22 690
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]
4UNI_A 7.25e-50 3 662 22 690
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D9SM34 1.57e-71 7 665 4 655
Beta-galactosidase BgaA OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=bgaA PE=1 SV=1
P19668 9.65e-66 1 668 4 664
Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1
D5JGG0 1.63e-65 2 665 6 660
Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1
C9S0R2 9.38e-65 1 668 4 664
Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB PE=3 SV=1
Q5FJ41 5.09e-60 1 665 4 665
Beta-galactosidase LacZ OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=lacZ 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
1.000031 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004233_00640.