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CAZyme Information: MGYG000000853_00277

You are here: Home > Sequence: MGYG000000853_00277

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 Prevotella sp900549175
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900549175
CAZyme ID MGYG000000853_00277
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
475 MGYG000000853_8|CGC1 53414.99 4.5374
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000853 3157276 MAG China Asia
Gene Location Start: 12219;  End: 13646  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000853_00277.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 182 452 7e-32 0.9344978165938864

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 2.92e-16 404 473 5 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02229 PLN02229 3.11e-07 370 470 308 414
alpha-galactosidase
PLN02808 PLN02808 4.60e-07 342 474 249 384
alpha-galactosidase
cd14792 GH27 1.51e-06 86 387 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67171.1 4.50e-264 1 473 1 473
QUU07210.1 1.02e-193 40 475 50 492
QUT44530.1 4.13e-193 40 475 50 492
QUT79686.1 4.13e-193 40 475 50 492
QRM98947.1 4.13e-193 40 475 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 5.72e-87 50 474 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 6.07e-87 50 474 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 0.000041 1.000003 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000853_00277.