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CAZyme Information: MGYG000002711_02403

You are here: Home > Sequence: MGYG000002711_02403

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 UMGS856 sp900546265
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS856; UMGS856 sp900546265
CAZyme ID MGYG000002711_02403
CAZy Family GH129
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
629 71148.18 5.3216
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002711 3636319 MAG Canada North America
Gene Location Start: 41096;  End: 42985  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002711_02403.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH129 90 624 3.1e-104 0.8592233009708737

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14244 GH_101_like 2.54e-20 325 464 40 189
Endo-a-N-acetylgalactosaminidase and related glcyosyl hydrolases. This family contains the enzymatically active domain of cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins (EC:3.2.1.97). It has been classified as glycosyl hydrolase family 101 in the Cazy resource. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae and other commensal human bacteria is largely determined by their ability to degrade host glycoproteins and to metabolize the resultant carbohydrates.
cd11336 AmyAc_MTSase 0.003 333 366 46 77
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase). Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
PRK14511 PRK14511 0.003 333 366 52 83
malto-oligosyltrehalose synthase.
pfam12905 Glyco_hydro_101 0.007 324 387 61 125
Endo-alpha-N-acetylgalactosaminidase. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae is largely determined by the ability to degrade host glycoproteins and to metabolize the resultant carbohydrates. This family is the enzymatic region, EC:3.2.1.97, of the cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins. This reaction is exemplified by the S. pneumoniae protein Endo-alpha-N-acetylgalactosaminidase, where Asp764 is the catalytic nucleophile-base and Glu796 the catalytic proton donor.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUH27706.1 4.28e-148 41 624 41 621
QUH27660.1 1.41e-147 24 624 14 626
QNK55038.1 3.66e-125 75 624 77 624
QTH41330.1 2.63e-124 24 624 28 624
QJD87097.1 3.90e-120 54 624 58 625

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5WZN_A 1.54e-114 56 624 46 628
Alpha-N-acetylgalactosaminidaseNagBb from Bifidobacterium bifidum - GalNAc complex [Bifidobacterium bifidum],5WZN_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - GalNAc complex [Bifidobacterium bifidum],5WZP_A Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - ligand free [Bifidobacterium bifidum],5WZP_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - ligand free [Bifidobacterium bifidum],5WZR_A Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - Gal-NHAc-DNJ complex [Bifidobacterium bifidum],5WZR_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - Gal-NHAc-DNJ complex [Bifidobacterium bifidum]
5WZQ_A 6.57e-109 56 624 46 628
Alpha-N-acetylgalactosaminidaseNagBb from Bifidobacterium bifidum - quadruple mutant [Bifidobacterium bifidum],5WZQ_B Alpha-N-acetylgalactosaminidase NagBb from Bifidobacterium bifidum - quadruple mutant [Bifidobacterium bifidum]
5OPQ_A 6.27e-16 49 629 84 666
A3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans],5OPQ_B A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans],5OPQ_C A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans],5OPQ_D A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D-galactose from the non-reducing end of carrageenan oligosaccharides. [Zobellia galactanivorans]

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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002711_02403.