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CAZyme Information: MGYG000003363_02997

You are here: Home > Sequence: MGYG000003363_02997

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 sp900766195
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900766195
CAZyme ID MGYG000003363_02997
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
475 MGYG000003363_153|CGC1 53865.83 6.3158
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003363 4177575 MAG United States North America
Gene Location Start: 5379;  End: 6806  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003363_02997.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 194 453 1e-33 0.9388646288209607

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 1.34e-15 400 473 1 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02808 PLN02808 7.52e-10 342 474 249 384
alpha-galactosidase
PLN02229 PLN02229 8.71e-09 257 474 210 418
alpha-galactosidase
cd14792 GH27 9.64e-09 74 387 14 271
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.
PLN02692 PLN02692 3.02e-05 87 473 83 408
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUU07210.1 2.27e-226 44 475 52 492
QUT44530.1 6.49e-226 44 475 52 492
QUT79686.1 6.49e-226 44 475 52 492
QRM98947.1 6.49e-226 44 475 52 492
QNT67171.1 1.71e-214 3 473 2 473

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AWO_A 4.91e-89 50 474 37 466
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 5.25e-89 50 474 63 492
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 0.000012 1.000040 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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