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CAZyme Information: MGYG000002288_02676

You are here: Home > Sequence: MGYG000002288_02676

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 Bacillus_A luti
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A luti
CAZyme ID MGYG000002288_02676
CAZy Family GH170
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
240 MGYG000002288_11|CGC1 26993.65 5.153
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002288 5512240 Isolate China Asia
Gene Location Start: 64799;  End: 65521  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002288_02676.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH170 4 238 4.3e-87 0.6514285714285715

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam19200 DUF871_N 1.60e-135 5 239 1 234
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 1.18e-88 3 238 2 234
Uncharacterized protein [Function unknown].
cd00551 AmyAc_family 0.001 50 99 76 117
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
QUG94197.1 6.96e-172 1 239 1 239
AXY07886.1 6.96e-172 1 239 1 239
QDF26257.1 6.96e-172 1 239 1 239
QWH70610.1 9.88e-172 1 239 1 239
AMR01331.1 9.88e-172 1 239 1 239

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1X7F_A 1.98e-171 1 239 25 263
Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]

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
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002288_02676.