CAZyme Information: MGYG000001724_01262

Basic Information

• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella
• CAZyme ID: MGYG000001724_01262
• CAZy Family: GH32
• CAZyme Description: Sucrose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
251		27530.92	4.8538

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001724	1316907	MAG	Sweden	Europe

• Gene Location: Start: 515; End: 1270 Strand: -

Full Sequence      

MSNALGRDLAKLVAAVDAAASECGHGAYGQRFHIMPPAGWLNDPNGLCQADGVFHAYFQY
APFDVNGGVKMWGHATSRDLMEWEYVGAPLLPDEPFDCHGVYSGSALVEDGRIRVLYTGN
VKLPDADGVFDYVNSGRRADTVYVESLDGQTFSQKRVVLASEDYPEDLTCHVRDPKVWRD
DDGRYHMVLGARRRVGGPHVESRFCAMHGEGAGRDVGEILVYGSADMLSWELEPCVCARA
LWLYVGVPGLS

Enzyme Prediction     

No EC number prediction in MGYG000001724_01262.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	33	233	1.4e-48	0.5699658703071673

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18623	GH32_ScrB-like	1.89e-74	39	233	1	165	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	1.51e-55	28	231	13	186	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
pfam00251	Glyco_hydro_32N	3.20e-52	33	234	1	174	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.
COG1621	SacC	4.23e-51	28	233	28	204	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	1.61e-49	33	234	1	177	Glycosyl hydrolases family 32.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIA33159.1	4.71e-161	1	233	1	236
AEB06470.1	5.71e-98	1	232	1	231
SDR64968.1	8.59e-84	1	232	1	212
QRT30958.1	4.55e-83	3	230	2	205
CCG93499.1	2.56e-82	3	230	2	205

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	1.10e-29	28	240	25	208	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
1UYP_A	4.01e-27	32	236	6	180	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]
1W2T_A	4.01e-27	32	236	6	180	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]
7BWB_A	3.10e-26	28	231	48	217	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
6NU7_A	8.03e-26	28	231	32	205	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P27217	7.72e-38	31	232	29	198	Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3
P07819	3.47e-37	30	192	30	179	Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2
P16553	1.72e-35	32	233	27	199	Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
P37075	1.03e-31	31	230	29	196	Sucrose-6-phosphate hydrolase OS=Salmonella typhimurium OX=90371 GN=scrB PE=3 SV=1
P40714	8.15e-31	32	233	28	200	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000030	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001724_01262.