dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Acetatifactor sp003447295

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp003447295

CAZyme ID

MGYG000004250_01299

CAZy Family

GH32

CAZyme Description

Sucrose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
496	MGYG000004250_12\|CGC1	57409.25	6.3473

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004250	3091301	MAG	United Kingdom	Europe

Gene Location

Start: 40814; End: 42304 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000004250_01299.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	33	323	1.2e-99	0.9658703071672355

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	4.69e-140	3	492	4	485	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd08996	GH32_FFase	4.55e-127	39	321	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.
pfam00251	Glyco_hydro_32N	6.22e-120	33	329	1	305	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.
TIGR01322	scrB_fam	3.85e-117	29	465	14	444	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
cd18623	GH32_ScrB-like	8.91e-116	39	323	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
ADD03329.1	4.69e-168	4	494	5	492
AIQ14407.1	2.19e-158	4	492	2	489
AKG37843.1	5.55e-158	4	492	9	496
QWU15422.1	8.99e-158	4	492	13	500
BCG60901.1	5.48e-156	4	492	11	498

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	8.84e-81	32	494	29	488	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
7BWB_A	1.95e-68	29	338	49	357	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A	2.90e-67	29	338	49	357	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
1UYP_A	2.10e-66	32	477	6	418	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	5.80e-66	32	477	6	418	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
P0DJA7	1.12e-80	30	495	27	503	Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
F8DVG5	1.70e-79	30	495	27	503	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
P07819	1.09e-78	1	465	1	454	Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2
P40714	5.89e-73	32	489	28	474	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
P05656	6.85e-72	29	494	35	512	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
1.000030	0.000026	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004250_01299.

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