dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lactococcus_A piscium_C

Lineage

Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Lactococcus_A; Lactococcus_A piscium_C

CAZyme ID

MGYG000002997_00627

CAZy Family

GH32

CAZyme Description

Sucrose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489	MGYG000002997_6\|CGC1	54902.99	4.6711

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002997	1565244	MAG	United States	North America

Gene Location

Start: 8917; End: 10386 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000002997_00627.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	28	332	2.9e-104	0.9897610921501706

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	4.87e-148	4	477	9	472	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd08996	GH32_FFase	6.82e-141	34	325	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.
TIGR01322	scrB_fam	2.77e-136	23	463	13	443	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
pfam00251	Glyco_hydro_32N	1.55e-132	28	334	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	1.52e-130	34	327	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
CEN28721.1	0.0	1	489	1	489
QDJ25698.1	0.0	1	489	1	489
ALS35830.1	5.22e-195	1	488	2	490
APV52892.1	5.69e-189	1	489	1	489
QCV45121.1	5.69e-189	1	489	1	489

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	2.69e-102	1	473	3	468	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
7BWB_A	1.33e-88	10	337	35	352	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A	2.05e-87	10	337	35	352	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
1UYP_A	1.54e-68	23	451	2	393	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	4.25e-68	23	451	2	393	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
P40714	1.09e-97	26	458	27	443	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
P0DJA7	1.64e-89	27	457	32	461	Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
F8DVG5	4.59e-89	27	457	32	461	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	9.39e-89	27	478	27	464	Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
P07819	1.26e-82	23	463	28	452	Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2

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
1.000057	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002997_00627.

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