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CAZyme Information: MGYG000001514_00807

You are here: Home > Sequence: MGYG000001514_00807

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 Paenibacillus_A ihumii
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
CAZyme ID MGYG000001514_00807
CAZy Family GH42
CAZyme Description Beta-galactosidase YesZ
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
668 MGYG000001514_10|CGC4 74373.49 6.7425
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001514 5923787 Isolate not provided not provided
Gene Location Start: 266753;  End: 268759  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001514_00807.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 10 371 4.9e-116 0.9865229110512129

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1874 GanA 4.91e-158 3 664 14 673
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam02449 Glyco_hydro_42 3.07e-151 10 376 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 2.29e-42 388 595 1 206
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 3.24e-18 390 493 1 105
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
AZK46351.1 0.0 1 661 1 661
AWV32494.1 0.0 1 663 1 663
AIQ73147.1 0.0 1 663 1 663
ASA19474.1 0.0 1 663 1 722
AYA75551.1 0.0 1 666 1 663

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LVW_A 3.26e-79 8 620 4 634
PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239]
1KWG_A 5.55e-77 8 599 3 593
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 5.22e-68 5 665 39 710
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 1.86e-63 8 486 4 506
ChainA, beta-galactosidase [Marinomonas sp. ef1]
4UCF_A 3.87e-62 2 509 17 534
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 1 664 1 660
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 3 664 2 660
Beta-galactosidase YesZ OS=Bacillus subtilis (strain 168) OX=224308 GN=yesZ PE=1 SV=1
B9LW38 1.79e-78 8 620 4 634
Beta-galactosidase Bga OS=Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) OX=416348 GN=Hlac_2868 PE=1 SV=1
P94804 6.12e-77 8 610 4 612
Beta-galactosidase BgaH OS=Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) OX=1230452 GN=bgaH PE=1 SV=2
Q8GEA9 3.04e-76 8 595 3 589
Beta-galactosidase BgaA OS=Thermus sp. OX=275 GN=bgaA 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
1.000062 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001514_00807.