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CAZyme Information: MGYG000002328_00661

You are here: Home > Sequence: MGYG000002328_00661

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 Enterocloster asparagiformis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster asparagiformis
CAZyme ID MGYG000002328_00661
CAZy Family GH170
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
276 MGYG000002328_41|CGC1 30715.14 4.8098
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002328 6168028 Isolate not provided not provided
Gene Location Start: 8978;  End: 9808  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002328_00661.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH170 3 267 2.2e-83 0.7285714285714285

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam19200 DUF871_N 3.00e-120 4 241 1 235
DUF871 N-terminal domain. This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
COG3589 COG3589 3.77e-85 1 268 1 264
Uncharacterized protein [Function unknown].
cd11326 AmyAc_Glg_debranch 0.007 42 75 101 131
Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASN95847.1 1.15e-157 1 269 1 269
QRP39378.1 1.15e-157 1 269 1 269
ANU44542.1 6.65e-157 1 269 1 269
QIX89835.1 6.65e-157 1 269 1 269
QJU19892.1 7.72e-156 1 269 1 269

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1X7F_A 7.33e-91 3 276 28 299
Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A 1.66e-19 2 237 3 232
Crystalstructure of a conserved protein from locus EF_2437 in Enterococcus faecalis with an unknown function [Enterococcus faecalis V583]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2XHV5 4.35e-07 18 229 13 215
6-phospho-N-acetylmuramidase OS=Staphylococcus aureus (strain USA300) OX=367830 GN=mupG 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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002328_00661.