You are browsing environment: HUMAN GUT

CAZyme Information: MGYG000001575_00967

You are here: Home > Sequence: MGYG000001575_00967

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

Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella;
CAZyme ID MGYG000001575_00967
CAZy Family GH170
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
376 MGYG000001575_9|CGC1 41964.75 4.9831
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001575 1745964 MAG United States North America
Gene Location Start: 51965;  End: 53095  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001575_00967.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH170 18 372 1.2e-101 0.9857142857142858

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam19200 DUF871_N 3.45e-106 19 254 2 235
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 9.41e-104 16 372 2 354
Uncharacterized protein [Function unknown].
pfam05913 DUF871 7.35e-35 260 372 1 113
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 0.002 56 112 73 117
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
BCT45938.1 3.83e-126 19 373 5 358
QIX10458.1 1.78e-124 19 373 5 358
QSI24875.1 1.78e-124 19 373 5 358
QNM11117.1 1.78e-124 19 373 5 358
ASU20682.1 3.57e-124 19 373 5 358

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1X7F_A 2.45e-116 17 372 28 381
Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]
2P0O_A 3.62e-31 18 372 5 355
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

1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001575_00967.