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CAZyme Information: MGYG000003135_01461

You are here: Home > Sequence: MGYG000003135_01461

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 Cutibacterium granulosum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium granulosum
CAZyme ID MGYG000003135_01461
CAZy Family GH36
CAZyme Description Alpha-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
695 MGYG000003135_8|CGC1 77084.53 6.1052
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003135 2072889 MAG United States North America
Gene Location Start: 83145;  End: 85232  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 8 649 5.1e-206 0.9723837209302325

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02065 Melibiase 1.50e-139 253 591 1 347
Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
COG3345 GalA 3.33e-129 27 645 23 648
Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14791 GH36 4.47e-119 288 583 1 299
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.
pfam16875 Glyco_hydro_36N 2.81e-44 24 244 2 252
Glycosyl hydrolase family 36 N-terminal domain. This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
cd14792 GH27 2.29e-06 319 370 36 84
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
AFV88528.1 2.66e-297 7 693 5 694
ASU61110.1 2.70e-229 3 685 14 717
ADH70209.1 2.79e-228 3 685 11 714
VEI90728.1 2.79e-228 3 685 11 714
APC38605.1 3.95e-228 3 685 11 714

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2XN0_A 9.91e-89 85 649 122 699
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM]
2YFN_A 2.07e-88 85 643 119 682
galactosidasedomain of alpha-galactosidase-sucrose kinase, AgaSK [[Ruminococcus] gnavus E1],2YFO_A GALACTOSIDASE DOMAIN OF ALPHA-GALACTOSIDASE-SUCROSE KINASE, AGASK, in complex with galactose [[Ruminococcus] gnavus E1]
2XN2_A 2.69e-88 85 649 122 699
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]
4FNQ_A 9.96e-86 140 654 176 701
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
6PHU_A 3.39e-85 155 592 205 649
SpAgawild type apo structure [Streptococcus pneumoniae TIGR4],6PHV_A Chain A, Alpha-galactosidase [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P16551 1.15e-140 17 693 15 705
Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1
G1UB44 5.43e-88 85 649 122 699
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
G4T4R7 6.38e-86 85 643 119 682
Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1
P43467 2.23e-84 47 644 89 693
Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1
Q9ALJ4 2.91e-83 140 654 176 701
Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA 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
1.000025 0.000011 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003135_01461.