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CAZyme Information: MGYG000003584_00411

You are here: Home > Sequence: MGYG000003584_00411

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 HGM11412 sp900770185
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; HGM11412; HGM11412 sp900770185
CAZyme ID MGYG000003584_00411
CAZy Family GH57
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
461 52456.23 6.0845
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003584 1810421 MAG Fiji Oceania
Gene Location Start: 1355;  End: 2740  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003584_00411.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 26 342 2e-22 0.7154046997389034

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10794 GH57N_PfGalA_like 3.35e-84 6 342 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-13 6 149 1 166
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.
pfam03065 Glyco_hydro_57 9.77e-11 1 145 26 172
Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.
cd10793 GH57N_TLGT_like 1.09e-10 26 152 22 148
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.
cd10795 GH57N_MJA1_like 1.65e-08 26 145 42 166
N-terminal catalytic domain of a thermoactive alpha-amylase from Methanococcus jannaschii and similar proteins; glycoside hydrolase family 57 (GH57). The subfamily is represented by a thermostable alpha-amylase (MJA1, EC 3.2.1.1) encoded from the hyperthermophilic archaeon Methanococcus jannaschii locus, M J1611. MJA1 has a broad pH optimum 5.0-8.0. It exhibits extremely thermophilic alpha-amylase activity that catalyzes the hydrolysis of large sugar polymers with alpha-l,6 and alpha-l,4 linkages, and yields products including glucose polymers of 1-7 units. MJ1611 also encodes another alpha-amylase with catalytic features distinct from MJA1, which belongs to glycoside hydrolase family 13 (GH-13), and is not included here. This subfamily also includes many uncharacterized proteins found in bacteria and archaea.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM45997.1 4.11e-220 4 461 6 459
AHF90539.1 3.60e-192 6 461 7 463
QDT00377.1 1.81e-43 10 402 8 393
QAZ69632.1 1.69e-14 4 148 2 146
QWC98984.1 2.63e-11 10 145 9 144

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O57932 6.66e-07 25 209 21 214
Alpha-amylase OS=Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) OX=70601 GN=amyA 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
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003584_00411.