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CAZyme Information: MGYG000001792_02872

You are here: Home > Sequence: MGYG000001792_02872

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; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA11452;
CAZyme ID MGYG000001792_02872
CAZy Family GH36
CAZyme Description Alpha-galactosidase Mel36A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
454 50939.11 6.1005
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001792 3531580 MAG Denmark Europe
Gene Location Start: 866;  End: 2230  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001792_02872.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH36 10 367 2.3e-77 0.5305232558139535

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 1.61e-87 69 358 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.
pfam02065 Melibiase 2.36e-39 71 366 42 347
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 9.04e-29 62 366 284 592
Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14792 GH27 2.46e-08 74 277 5 174
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.
cd06592 GH31_NET37 4.62e-04 119 245 48 185
glucosidase NET37. NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QYM79268.1 2.14e-128 1 431 262 702
ANS77143.1 8.49e-125 1 428 223 662
AVM43342.1 1.03e-122 1 452 237 699
BBI32765.1 5.80e-122 1 451 248 710
QYY36366.1 3.86e-119 1 454 246 712

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4FNQ_A 1.90e-25 28 357 284 626
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
3MI6_A 4.65e-25 15 357 275 627
ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367]
4FNP_A 1.47e-24 28 357 284 626
Crystalstructure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNP_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNS_A Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_B Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_C Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus],4FNS_D Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus in complex with 1-deoxygalactonojirimycin [Geobacillus stearothermophilus]
2XN0_A 1.47e-24 15 366 278 639
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]
4FNR_A 2.63e-24 28 357 284 626
Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G1UB44 8.06e-24 15 366 278 639
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
Q9ALJ4 1.44e-23 28 357 284 626
Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1
Q5AU92 1.97e-23 12 301 290 592
Alpha-galactosidase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglC PE=1 SV=1
Q5ARP5 6.16e-23 13 367 264 636
Probable alpha-galactosidase G OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aglG PE=2 SV=1
Q9UUZ4 6.30e-23 28 301 303 589
Alpha-galactosidase C OS=Aspergillus niger OX=5061 GN=aglC 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
1.000046 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001792_02872.