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CAZyme Information: MGYG000002357_01405

You are here: Home > Sequence: MGYG000002357_01405

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 Bacillus licheniformis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis
CAZyme ID MGYG000002357_01405
CAZy Family GH42
CAZyme Description Beta-galactosidase YesZ
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
665 MGYG000002357_1|CGC21 74472.91 6.6286
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002357 4208157 Isolate South Korea Asia
Gene Location Start: 1384813;  End: 1386810  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002357_01405.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 12 371 9.4e-122 0.9811320754716981

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1874 GanA 2.60e-178 5 659 14 670
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam02449 Glyco_hydro_42 7.87e-159 12 377 1 375
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.
pfam08532 Glyco_hydro_42M 1.08e-50 390 596 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 1.84e-24 392 595 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.
pfam08533 Glyco_hydro_42C 3.31e-09 604 659 1 56
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
AZN80000.1 0.0 1 665 1 665
AYC50998.1 0.0 1 665 1 665
QNH42446.1 0.0 1 665 1 665
AUZ30109.1 0.0 1 665 1 665
QAW37077.1 0.0 1 665 1 665

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1KWG_A 2.13e-85 10 596 3 590
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 2.76e-84 10 619 4 634
PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239]
5E9A_A 1.43e-71 2 571 35 620
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]
6Y2K_A 2.76e-68 10 497 4 515
ChainA, beta-galactosidase [Marinomonas sp. ef1]
4UCF_A 2.31e-67 6 511 19 534
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q65KX8 0.0 3 665 1 663
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 0.0 6 659 3 657
Beta-galactosidase YesZ OS=Bacillus subtilis (strain 168) OX=224308 GN=yesZ PE=1 SV=1
P94804 2.81e-89 10 620 4 619
Beta-galactosidase BgaH OS=Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) OX=1230452 GN=bgaH PE=1 SV=2
O69315 1.16e-84 10 596 3 590
Beta-galactosidase OS=Thermus thermophilus OX=274 PE=1 SV=1
D5JGG0 5.01e-84 1 663 2 664
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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002357_01405.