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CAZyme Information: MGYG000002967_00067

You are here: Home > Sequence: MGYG000002967_00067

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 Enterococcus_A pallens
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_A; Enterococcus_A pallens
CAZyme ID MGYG000002967_00067
CAZy Family GH32
CAZyme Description Sucrose-6-phosphate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
474 MGYG000002967_1|CGC2 54492.5 4.854
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002967 2610517 MAG United States North America
Gene Location Start: 69190;  End: 70614  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002967_00067.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 38 336 1.2e-80 0.9658703071672355

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18623 GH32_ScrB-like 5.85e-134 44 336 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.
TIGR01322 scrB_fam 6.60e-128 23 455 3 445
sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG1621 SacC 4.08e-111 13 462 8 467
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251 Glyco_hydro_32N 5.42e-96 38 343 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.
cd08996 GH32_FFase 4.21e-89 44 334 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALS36464.1 4.96e-189 9 461 7 468
AIY83614.1 2.05e-145 10 455 10 456
AQP38830.1 6.76e-136 35 456 34 455
CBL39319.1 2.71e-135 35 456 34 455
QWC22504.1 1.39e-116 3 459 2 471

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6NU7_A 6.43e-67 13 458 12 467
Structureof sucrose-6-phosphate hydrolase from Lactobacillus gasseri [Lactobacillus gasseri 224-1],6NU8_A Structure of sucrose-6-phosphate hydrolase from Lactobacillus gasseri in complex with fructose [Lactobacillus gasseri 224-1]
7BWB_A 2.03e-63 17 468 30 474
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A 2.98e-62 17 468 30 474
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
7VCO_A 7.74e-55 16 453 9 458
ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
1UYP_A 1.89e-45 33 462 2 414
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q05936 1.78e-89 13 459 13 469
Sucrose-6-phosphate hydrolase OS=Staphylococcus xylosus OX=1288 GN=scrB PE=3 SV=1
P07819 6.20e-74 36 453 31 453
Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2
P13522 3.39e-73 13 474 15 477
Sucrose-6-phosphate hydrolase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=scrB PE=3 SV=3
P43471 1.87e-70 21 474 20 482
Sucrose-6-phosphate hydrolase OS=Pediococcus pentosaceus OX=1255 GN=scrB PE=3 SV=2
P13394 3.63e-69 35 460 38 460
Sucrose-6-phosphate hydrolase OS=Vibrio alginolyticus OX=663 GN=scrB PE=2 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
0.999749 0.000254 0.000019 0.000001 0.000001 0.000010

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002967_00067.