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CAZyme Information: MGYG000004336_00974

You are here: Home > Sequence: MGYG000004336_00974

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 Faecalibacterium sp900765105
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium sp900765105
CAZyme ID MGYG000004336_00974
CAZy Family GH32
CAZyme Description Levanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
281 31706.6 5.3508
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004336 2379489 MAG Israel Asia
Gene Location Start: 19602;  End: 20447  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004336_00974.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 8 129 1.9e-28 0.40273037542662116

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1621 SacC 7.22e-59 9 272 214 477
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
TIGR01322 scrB_fam 5.30e-58 10 255 203 444
sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
smart00640 Glyco_32 7.00e-45 9 245 187 437
Glycosyl hydrolases family 32.
cd08996 GH32_FFase 1.44e-34 9 120 177 281
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.
pfam00251 Glyco_hydro_32N 1.56e-32 6 129 180 308
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK98452.1 7.74e-199 1 281 211 491
AXA82442.1 4.46e-198 1 281 211 491
QIA44202.1 2.10e-196 1 281 211 491
ATP01188.1 2.10e-196 1 281 211 491
AXB28040.1 4.23e-196 1 281 211 491

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7VCO_A 1.09e-27 12 272 214 477
ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
3RWK_X 2.03e-21 13 268 232 500
Firstcrystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum]
7BWB_A 1.35e-19 1 254 221 460
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A 1.35e-19 1 254 221 460
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
3PIG_A 2.04e-16 12 267 233 498
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q05936 4.34e-31 7 271 216 480
Sucrose-6-phosphate hydrolase OS=Staphylococcus xylosus OX=1288 GN=scrB PE=3 SV=1
Q9KLT6 3.29e-30 9 263 278 520
Probable sucrose-6-phosphate hydrolase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=VC_A0655 PE=3 SV=1
A5EZZ8 4.46e-30 9 263 278 520
Probable sucrose-6-phosphate hydrolase OS=Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) OX=345073 GN=cscA PE=3 SV=1
Q56660 6.11e-30 9 263 278 520
Probable sucrose-6-phosphate hydrolase OS=Vibrio cholerae OX=666 PE=3 SV=1
P05656 1.90e-29 9 272 218 501
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC 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
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004336_00974.