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CAZyme Information: MGYG000004132_01552

You are here: Home > Sequence: MGYG000004132_01552

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 V9D3004 sp900760345
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; V9D3004; V9D3004 sp900760345
CAZyme ID MGYG000004132_01552
CAZy Family GH27
CAZyme Description Alpha-galactosidase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
421 MGYG000004132_23|CGC1 48877.5 4.7054
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004132 2510246 MAG United Kingdom Europe
Gene Location Start: 4644;  End: 5909  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004132_01552.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 170 398 7.3e-57 0.9344978165938864

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14792 GH27 8.57e-93 10 335 1 266
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.
PLN02899 PLN02899 9.44e-81 10 335 31 373
alpha-galactosidase
PLN03231 PLN03231 9.87e-79 10 337 1 345
putative alpha-galactosidase; Provisional
PLN02808 PLN02808 8.66e-40 3 420 25 383
alpha-galactosidase
PLN02692 PLN02692 6.54e-38 4 421 50 409
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ97904.1 6.29e-211 1 420 1 427
ADL53311.1 1.37e-209 1 418 1 425
BCN31086.1 8.17e-209 1 420 1 427
AEY64483.1 1.03e-206 1 421 1 428
QHQ63254.1 5.84e-204 1 421 1 437

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NX0_A 2.23e-149 1 395 16 415
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]
4NXK_A 3.63e-148 1 395 16 415
Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
3CC1_A 3.30e-127 1 395 4 399
ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
6F4C_B 5.20e-32 4 420 3 360
Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]
1UAS_A 1.13e-28 4 420 3 359
ChainA, alpha-galactosidase [Oryza sativa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8RX86 1.69e-38 3 418 33 389
Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
Q9FT97 1.11e-36 4 421 48 407
Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1
P14749 4.14e-36 4 420 50 407
Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q42656 1.52e-33 4 420 18 375
Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1
Q8VXZ7 2.54e-31 3 420 66 427
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1

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
1.000047 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004132_01552.