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CAZyme Information: MGYG000001524_01503

You are here: Home > Sequence: MGYG000001524_01503

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 RUG013 sp001486445
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; RUG013; RUG013 sp001486445
CAZyme ID MGYG000001524_01503
CAZy Family GH36
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
529 MGYG000001524_9|CGC5 57814.7 4.6129
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001524 2090171 Isolate not provided not provided
Gene Location Start: 1097806;  End: 1099395  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001524_01503.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 3.57e-58 216 521 4 295
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.
COG3345 GalA 5.56e-18 212 488 289 581
Alpha-galactosidase [Carbohydrate transport and metabolism].
pfam02065 Melibiase 8.82e-13 220 368 47 190
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.
cd06592 GH31_NET37 3.35e-07 218 369 5 151
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.
cd14792 GH27 4.04e-06 214 434 1 188
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
ACV21706.1 4.03e-160 27 523 90 584
VEG99344.1 4.03e-160 27 523 90 584
AEB07485.1 4.45e-154 53 527 82 556
SDR67186.1 1.15e-145 53 528 58 532
ADU21146.1 2.45e-131 47 520 46 511

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LCJ_A 3.25e-43 179 513 119 445
TtGalA,alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_B TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_C TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_D TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_E TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCJ_F TtGalA, alpha-galactosidase from Thermus thermopilus in apo form [Thermus thermophilus HB8],6LCK_A TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCK_B TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCK_C TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG) [Thermus thermophilus HB8],6LCL_A TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8],6LCL_C TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8],6LCL_E TtGalA, alpha-galactosidase from Thermus thermophilus in complex with stachyose [Thermus thermophilus HB8]
5M0X_A 1.57e-25 216 528 208 509
Structureof apo structure of GH36 alpha-galactosidase from Thermotoga maritima [Thermotoga maritima],5M12_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with intact cyclopropyl-carbasugar. [Thermotoga maritima],5M16_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with a hydrolysed cyclopropyl carbasugar. [Thermotoga maritima],5M1I_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in a covalent complex with a cyclopropyl carbasugar. [Thermotoga maritima],6GVD_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8],6GWG_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose covalently linked to the nucleophile [Thermotoga maritima MSB8],6GX8_A Alpha-galactosidase from Thermotoga maritima in complex with hydrolysed cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8]
6GTA_A 1.62e-24 216 528 208 509
Alpha-galactosidasemutant D378A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 3,5 difluorophenyl leaving group [Thermotoga maritima MSB8],6GWF_A Alpha-galactosidase mutant D387A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 2,4-dinitro leaving group [Thermotoga maritima MSB8]
2YFN_A 2.16e-07 220 391 335 496
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G4FEF4 7.70e-25 216 528 185 486
Alpha-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=galA PE=1 SV=1
G4T4R7 1.30e-06 220 391 335 496
Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1
Q9UUZ4 2.09e-06 220 368 354 508
Alpha-galactosidase C OS=Aspergillus niger OX=5061 GN=aglC PE=1 SV=1
P16551 8.15e-06 258 396 328 473
Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA 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
0.999995 0.000061 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001524_01503.