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CAZyme Information: MGYG000000312_02280

You are here: Home > Sequence: MGYG000000312_02280

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 Eisenbergiella sp900539715
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715
CAZyme ID MGYG000000312_02280
CAZy Family GH27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
642 MGYG000000312_31|CGC1 72527.7 5.1714
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000312 2782709 MAG Sweden Europe
Gene Location Start: 23255;  End: 25183  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000312_02280.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 376 619 4.6e-19 0.9563318777292577

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14792 GH27 7.10e-15 248 531 2 248
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.
cd14791 GH36 3.72e-04 248 531 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCK01163.1 2.10e-232 5 640 17 683
AYQ71136.1 9.28e-125 91 617 123 654
QGQ94687.1 4.00e-124 120 627 141 657
AYB43258.1 5.90e-124 82 640 121 682
ACX66631.1 2.55e-122 120 617 150 659

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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000037 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000312_02280.