logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004830_01387

You are here: Home > Sequence: MGYG000004830_01387

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 CAG-485 sp900549375
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900549375
CAZyme ID MGYG000004830_01387
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
460 52313.85 4.8812
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004830 2642212 MAG China Asia
Gene Location Start: 4789;  End: 6171  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004830_01387.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 156 418 9.8e-34 0.9432314410480349

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 1.01e-16 366 438 6 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
cd14792 GH27 2.39e-11 34 346 2 269
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.
PLN02808 PLN02808 7.02e-06 108 433 104 378
alpha-galactosidase
PLN02229 PLN02229 1.84e-05 264 419 240 397
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUR46778.1 2.73e-193 73 457 1 385
ALJ61711.1 9.58e-181 15 459 17 462
QUT92727.1 1.93e-180 15 459 17 462
QDM09865.1 1.91e-148 9 456 8 461
ALJ47291.1 3.84e-148 9 456 8 461

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AWO_A 1.40e-112 20 456 24 487
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 4.52e-112 20 456 50 513
Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q8VXZ7 3.94e-07 281 433 267 422
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 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
0.000328 0.998898 0.000272 0.000182 0.000157 0.000147

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004830_01387.