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CAZyme Information: MGYG000004430_02864

You are here: Home > Sequence: MGYG000004430_02864

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485;
CAZyme ID MGYG000004430_02864
CAZy Family GH27
CAZyme Description Isomalto-dextranase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
473 MGYG000004430_38|CGC1 53287.08 5.043
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004430 3945500 MAG Israel Asia
Gene Location Start: 4129;  End: 5550  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004430_02864.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 185 450 2.4e-34 0.9388646288209607

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17801 Melibiase_C 9.95e-19 402 471 6 74
Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
PLN02808 PLN02808 2.90e-15 297 472 207 384
alpha-galactosidase
cd14792 GH27 3.62e-15 79 384 22 271
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.
PLN02229 PLN02229 4.28e-11 299 472 239 418
alpha-galactosidase
PLN02692 PLN02692 5.79e-07 328 468 261 405
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHF13305.1 3.09e-296 35 471 35 471
QNT67171.1 5.20e-184 8 471 14 473
QUU07210.1 8.55e-175 1 473 13 492
QUT44530.1 4.89e-174 1 473 13 492
QUT79686.1 4.89e-174 1 473 13 492

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AWO_A 3.37e-79 48 472 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]
4NX0_A 1.29e-14 72 471 39 440
Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
3A21_A 1.16e-06 339 472 248 384
CrystalStructure of Streptomyces avermitilis beta-L-Arabinopyranosidase [Streptomyces avermitilis],3A21_B Crystal Structure of Streptomyces avermitilis beta-L-Arabinopyranosidase [Streptomyces avermitilis],3A22_A Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose [Streptomyces avermitilis],3A22_B Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose [Streptomyces avermitilis],3A23_A Crystal Structure of beta-L-Arabinopyranosidase complexed with D-galactose [Streptomyces avermitilis],3A23_B Crystal Structure of beta-L-Arabinopyranosidase complexed with D-galactose [Streptomyces avermitilis]
3CC1_A 8.90e-06 55 445 44 401
ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q44052 1.26e-79 48 472 64 492
Isomalto-dextranase OS=Arthrobacter globiformis OX=1665 GN=imd PE=1 SV=1
Q5AX28 4.72e-09 327 471 253 399
Alpha-galactosidase D OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglD PE=1 SV=2
Q2UI87 6.23e-09 342 471 266 401
Probable alpha-galactosidase D OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglD PE=3 SV=2
Q8VXZ7 1.86e-08 328 472 277 428
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
A2R2S6 2.34e-07 376 471 305 401
Probable alpha-galactosidase D OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglD PE=3 SV=2

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
0.347865 0.055483 0.596195 0.000156 0.000140 0.000166

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004430_02864.