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CAZyme Information: MGYG000001951_02224

You are here: Home > Sequence: MGYG000001951_02224

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-873 sp900548975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900548975
CAZyme ID MGYG000001951_02224
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
477 MGYG000001951_38|CGC1 53549.14 5.0143
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001951 2929441 MAG Denmark Europe
Gene Location Start: 9793;  End: 11226  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001951_02224.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 205 455 1e-28 0.9344978165938864

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 7.39e-15 407 475 6 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02808 PLN02808 7.84e-09 347 476 252 384
alpha-galactosidase
cd14792 GH27 1.37e-05 90 389 28 271
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 1.70e-05 379 476 315 418
alpha-galactosidase
PLN02692 PLN02692 1.52e-04 371 472 293 405
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67171.1 4.48e-227 1 475 1 473
QCP71216.1 2.16e-189 1 477 2 475
QCD40129.1 2.16e-189 1 477 2 475
VEH14482.1 8.81e-186 49 477 41 468
QUT44530.1 1.71e-185 45 477 50 492

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AWO_A 3.57e-85 54 476 38 466
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 3.76e-85 54 476 64 492
Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000030 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001951_02224.