logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000211_00659

You are here: Home > Sequence: MGYG000000211_00659

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 Bacteroides sp900556215
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900556215
CAZyme ID MGYG000000211_00659
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
463 MGYG000000211_2|CGC2 53780.52 5.668
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000211 6486320 Isolate China Asia
Gene Location Start: 107636;  End: 109027  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000211_00659.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 171 421 5.8e-32 0.9694323144104804

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 8.08e-20 370 441 7 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
cd14792 GH27 8.21e-10 44 348 9 269
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
PLN02229 PLN02229 2.87e-05 370 438 346 414
alpha-galactosidase
PLN02808 PLN02808 5.85e-05 370 438 313 380
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALJ61711.1 0.0 1 463 1 463
QUT92727.1 0.0 1 463 1 463
ALJ47291.1 5.84e-166 9 459 6 461
QRQ58762.1 5.84e-166 9 459 6 461
SCV06693.1 5.84e-166 9 459 6 461

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AWO_A 1.29e-132 19 459 21 487
Arthrobacterglobiformis T6 isomalto-dextranse [Arthrobacter globiformis],5AWP_A Arthrobacter globiformis T6 isomalto-dextranase complexed with isomaltose [Arthrobacter globiformis],5AWQ_A Arthrobacter globiformis T6 isomalto-dextranse complexed with panose [Arthrobacter globiformis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q44052 5.55e-133 19 459 47 513
Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000228 0.999148 0.000171 0.000156 0.000138 0.000133

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000211_00659.