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CAZyme Information: MGYG000003084_01717

You are here: Home > Sequence: MGYG000003084_01717

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 CAG-724 sp900551005
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; CAG-724; CAG-724 sp900551005
CAZyme ID MGYG000003084_01717
CAZy Family GH151
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
659 74156.88 5.297
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003084 1926204 MAG Spain Europe
Gene Location Start: 1140;  End: 3119  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.51

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH151 25 155 2.6e-55 0.9847328244274809

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14871 GHL6 4.50e-32 24 155 1 135
Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases.
cd03143 A4_beta-galactosidase_middle_domain 5.95e-12 343 430 4 90
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.
COG1874 GanA 1.32e-11 50 435 54 499
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam08532 Glyco_hydro_42M 1.21e-05 383 426 47 90
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.
cd14791 GH36 5.56e-05 73 202 71 189
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QLG40864.1 2.71e-285 1 659 1 659
QHT63046.1 3.25e-285 1 659 1 664
QOS78864.1 1.74e-283 1 659 1 658
AFH63272.1 7.91e-280 1 658 1 658
BCJ98360.1 8.82e-279 1 659 1 658

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6TVK_AAA 1.35e-252 1 659 30 687
ChainAAA, Alpha-L-fucosidase [Paenibacillus thiaminolyticus]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003084_01717.