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CAZyme Information: MGYG000003683_01801

You are here: Home > Sequence: MGYG000003683_01801

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 Bifidobacterium pseudocatenulatum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pseudocatenulatum
CAZyme ID MGYG000003683_01801
CAZy Family GH27
CAZyme Description Alpha-galactosidase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
473 MGYG000003683_3|CGC10 52940.53 4.3812
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003683 2206268 Isolate China Asia
Gene Location Start: 382336;  End: 383757  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003683_01801.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 164 359 3.8e-46 0.777292576419214

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14792 GH27 3.33e-90 13 340 1 268
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.
PLN02899 PLN02899 1.19e-82 10 353 28 388
alpha-galactosidase
PLN03231 PLN03231 2.34e-73 13 349 1 354
putative alpha-galactosidase; Provisional
pfam16499 Melibiase_2 1.05e-25 13 334 2 275
Alpha galactosidase A.
PLN02808 PLN02808 1.08e-24 13 342 32 291
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTL82598.1 0.0 15 473 1 459
AZN75635.1 0.0 15 473 1 459
QAY33946.1 9.26e-289 15 473 1 456
QOL35351.1 6.23e-287 15 473 1 456
AAN24032.1 5.85e-286 5 473 6 469

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NX0_A 2.54e-114 13 364 25 377
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 4.05e-113 13 364 25 377
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 5.78e-109 13 424 12 401
ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A 4.66e-24 13 344 9 273
ChainA, alpha-galactosidase [Oryza sativa]
3H53_A 1.01e-23 13 340 9 288
ChainA, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H53_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8RX86 2.91e-25 13 395 40 351
Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
Q8VXZ7 8.60e-25 13 334 73 326
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
P14749 1.62e-24 13 378 56 343
Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q9FXT4 4.92e-23 13 344 64 328
Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
P17050 8.47e-23 13 340 26 305
Alpha-N-acetylgalactosaminidase OS=Homo sapiens OX=9606 GN=NAGA PE=1 SV=2

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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003683_01801.