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CAZyme Information: MGYG000000098_00649

You are here: Home > Sequence: MGYG000000098_00649

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 bouchesdurhonensis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides bouchesdurhonensis
CAZyme ID MGYG000000098_00649
CAZy Family CBM35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
705 MGYG000000098_3|CGC1 80721.91 7.2403
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000098 4868436 Isolate Canada North America
Gene Location Start: 139381;  End: 141498  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000098_00649.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 6.40e-12 300 579 3 278
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 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. GH36 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.
cd14792 GH27 1.41e-09 300 543 2 214
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
EIY66649.1 3.11e-215 9 705 56 748
QUT74114.1 7.09e-214 9 705 56 748
BCI61924.1 1.67e-205 12 703 7 688
QQA08702.1 4.00e-188 16 704 17 673
ALJ44661.1 1.60e-187 16 704 17 673

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000556 0.998433 0.000503 0.000172 0.000164 0.000151

TMHMM  Annotations      download full data without filtering help

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