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CAZyme Information: MGYG000000452_00570

You are here: Home > Sequence: MGYG000000452_00570

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 Barnesiella sp002159975
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp002159975
CAZyme ID MGYG000000452_00570
CAZy Family GH32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
791 MGYG000000452_10|CGC1 86399.44 4.4732
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000452 2678398 MAG Sweden Europe
Gene Location Start: 43117;  End: 45492  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000452_00570.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 265 571 3e-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 1.97e-78 271 561 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 7.78e-65 265 693 1 436
Glycosyl hydrolases family 32.
COG1621 SacC 6.61e-58 236 730 7 485
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251 Glyco_hydro_32N 1.53e-48 265 571 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.
cd18622 GH32_Inu-like 2.08e-35 270 558 1 286
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave 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). 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB92629.1 8.79e-220 54 791 26 742
AXV49252.1 4.44e-217 15 791 298 1052
QUB90817.1 2.84e-216 15 791 279 1033
AEA21196.1 3.64e-216 54 791 26 742
QUB89002.1 3.64e-216 54 791 26 742

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7VCO_A 4.96e-26 262 727 27 483
ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
6NUM_A 1.13e-25 262 724 41 507
Thestructure of GH32 from Bifidobacteium adolescentis [Bifidobacterium adolescentis],6NUN_A Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose [Bifidobacterium adolescentis]
1UYP_A 1.14e-25 259 703 1 406
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]
3PIG_A 1.61e-25 262 692 41 474
beta-fructofuranosidasefrom Bifidobacterium longum [Bifidobacterium longum],3PIG_B beta-fructofuranosidase from Bifidobacterium longum [Bifidobacterium longum],3PIJ_A beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum],3PIJ_B beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum]
1W2T_A 2.75e-25 259 703 1 406
beta-fructosidasefrom Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_B beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_C beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_D beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_E beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_F beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P16553 1.41e-30 262 716 25 461
Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
P43471 8.98e-28 227 740 2 495
Sucrose-6-phosphate hydrolase OS=Pediococcus pentosaceus OX=1255 GN=scrB PE=3 SV=2
P40714 4.15e-26 262 703 26 450
Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
Q70XE6 6.39e-26 257 730 52 580
Fructan 6-exohydrolase OS=Beta vulgaris OX=161934 GN=6-FEH PE=1 SV=1
B6DZD2 5.89e-25 249 729 49 582
Fructan 1-exohydrolase OS=Aegilops tauschii OX=37682 GN=1-FEH PE=3 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
0.011690 0.984054 0.001831 0.000866 0.000761 0.000739

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000452_00570.