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CAZyme Information: MGYG000000132_00127

You are here: Home > Sequence: MGYG000000132_00127

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 Beduini sp902363625
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Beduini; Beduini sp902363625
CAZyme ID MGYG000000132_00127
CAZy Family GH170
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
365 41437.37 4.9409
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000132 2897757 Isolate Canada North America
Gene Location Start: 116951;  End: 118048  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000132_00127.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH170 4 361 4.5e-121 0.9942857142857143

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3589 COG3589 3.29e-126 1 364 1 360
Uncharacterized protein [Function unknown].
pfam19200 DUF871_N 9.14e-126 4 240 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.
pfam05913 DUF871 1.30e-42 246 361 1 116
Bacterial protein of unknown function (DUF871). This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
cd00551 AmyAc_family 0.003 50 98 77 117
Alpha amylase catalytic domain family. 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; and 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 this 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
QSI24875.1 1.17e-163 1 360 1 359
QIX10458.1 2.36e-163 1 360 1 359
QJA04157.1 4.75e-163 1 360 1 359
QNM11117.1 2.73e-162 1 360 1 359
ASU20682.1 3.88e-162 1 360 1 359

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1X7F_A 5.20e-128 4 358 29 381
Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A 7.17e-29 5 358 6 355
Crystalstructure of a conserved protein from locus EF_2437 in Enterococcus faecalis with an unknown function [Enterococcus faecalis V583]

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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000132_00127.