logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004090_01162

You are here: Home > Sequence: MGYG000004090_01162

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 CAG-279 sp900550025
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-279; CAG-279 sp900550025
CAZyme ID MGYG000004090_01162
CAZy Family GH32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
826 MGYG000004090_8|CGC1 91054.19 4.7603
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004090 2636589 MAG United Kingdom Europe
Gene Location Start: 43494;  End: 45974  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004090_01162.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 270 579 1.6e-58 0.9965870307167235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08996 GH32_FFase 1.39e-80 276 569 1 281
Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
smart00640 Glyco_32 6.46e-71 270 703 1 436
Glycosyl hydrolases family 32.
COG1621 SacC 3.48e-60 240 741 5 486
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251 Glyco_hydro_32N 9.40e-55 270 579 1 308
Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.
cd18623 GH32_ScrB-like 2.36e-33 276 571 1 289
glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase). Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose. These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB90817.1 9.44e-228 25 766 289 1008
AXV49252.1 9.38e-227 25 766 308 1027
QUB92629.1 1.33e-225 41 766 13 717
AEA21196.1 1.72e-223 41 766 13 717
QUB89002.1 1.72e-223 41 766 13 717

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7VCO_A 5.40e-33 267 745 27 490
ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
6NUM_A 2.91e-26 267 703 41 475
Thestructure of GH32 from Bifidobacteium adolescentis [Bifidobacterium adolescentis],6NUN_A Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose [Bifidobacterium adolescentis]
7BWB_A 2.95e-26 264 716 47 464
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
1UYP_A 5.07e-26 265 713 2 406
Thethree-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8]
7BWC_A 7.05e-26 264 716 47 464
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0DJA7 1.53e-33 259 744 22 505
Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
F8DVG5 6.68e-33 259 744 22 505
Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1) OX=555217 GN=sacA PE=3 SV=1
P16553 1.54e-30 267 716 25 452
Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
Q70XE6 4.24e-30 262 737 52 577
Fructan 6-exohydrolase OS=Beta vulgaris OX=161934 GN=6-FEH PE=1 SV=1
Q0JDC6 4.85e-30 252 748 33 586
Beta-fructofuranosidase, insoluble isoenzyme 3 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN3 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000282 0.998911 0.000238 0.000188 0.000184 0.000162

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004090_01162.