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CAZyme Information: MGYG000000144_02310

You are here: Home > Sequence: MGYG000000144_02310

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 Barnesiella intestinihominis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella intestinihominis
CAZyme ID MGYG000000144_02310
CAZy Family CBM35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
662 MGYG000000144_4|CGC4 74777.52 5.9404
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000144 3314966 Isolate United Kingdom Europe
Gene Location Start: 227487;  End: 229475  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000144_02310.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 1.99e-18 277 560 3 293
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 1.43e-07 277 571 2 268
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.
pfam17801 Melibiase_C 1.01e-06 599 660 15 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJR78498.1 3.60e-218 16 660 22 673
QJR69930.1 5.10e-218 16 660 22 673
AII65845.1 5.10e-218 16 660 22 673
QJR74262.1 5.10e-218 16 660 22 673
QJR65668.1 5.10e-218 16 660 22 673

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
0.000573 0.998425 0.000290 0.000224 0.000221 0.000211

TMHMM  Annotations      download full data without filtering help

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