logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004461_03450

You are here: Home > Sequence: MGYG000004461_03450

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; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; ;
CAZyme ID MGYG000004461_03450
CAZy Family GH57
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
461 51942.41 5.269
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004461 4658877 MAG Israel Asia
Gene Location Start: 5514;  End: 6899  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004461_03450.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 9 179 5.7e-24 0.4360313315926893

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10794 GH57N_PfGalA_like 2.81e-95 8 345 1 305
N-terminal catalytic domain of alpha-galactosidase; glycoside hydrolase family 57 (GH57). Alpha-galactosidases (GalA, EC 3.2.1.22) catalyze the hydrolysis of alpha-1,6-linked galactose residues from oligosaccharides and polymeric galactomannans. Based on sequence similarity, the majority of eukaryotic and bacterial GalAs have been classified into glycoside hydrolase family GH27, GH36, and GH4, respectively. This subfamily is represented by a novel type of GalA from Pyrococcus furiosus (PfGalA), which belongs to the GH57 family. PfGalA is an extremely thermo-active and thermostable GalA that functions as a bacterial-like GalA, however, without the capacity to hydrolyze polysaccharides. It specifically catalyzes the hydrolysis of para-nitrophenyl-alpha-galactopyranoside, and to some extent that of melibiose and raffinose. PfGalA has a pH optimum between 5.0-5.5.
cd01022 GH57N_like 6.81e-16 7 151 2 166
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
cd10793 GH57N_TLGT_like 2.27e-14 30 154 24 148
N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57). 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity.
pfam03065 Glyco_hydro_57 4.61e-14 28 154 43 179
Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.
pfam01074 Glyco_hydro_38 1.16e-11 6 215 1 196
Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM45997.1 2.81e-267 1 459 1 459
AHF90539.1 2.15e-210 8 460 7 464
QDT00377.1 5.22e-51 12 432 8 422
QAZ69632.1 1.76e-16 6 150 2 146
BCW88139.1 4.31e-16 12 157 26 170

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1K1X_A 1.08e-09 27 185 21 182
Crystalstructure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis],1K1X_B Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis],1K1Y_A Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose [Thermococcus litoralis],1K1Y_B Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose [Thermococcus litoralis]
1K1W_A 1.89e-09 27 147 21 145
Crystalstructure of 4-alpha-glucanotransferase from thermococcus litoralis [Thermococcus litoralis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9V298 8.81e-11 30 152 28 150
Alpha-amylase OS=Pyrococcus abyssi (strain GE5 / Orsay) OX=272844 GN=amyA PE=3 SV=1
P49067 6.25e-10 27 185 22 183
Alpha-amylase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=amyA PE=1 SV=2
O32462 5.92e-09 27 185 21 182
4-alpha-glucanotransferase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=jgt PE=1 SV=1
O32450 1.36e-08 27 152 21 150
4-alpha-glucanotransferase OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1809 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
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004461_03450.