CAZyme Information: MGYG000001322_00322

Basic Information

• Species: Gemmiger variabilis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger; Gemmiger variabilis
• CAZyme ID: MGYG000001322_00322
• CAZy Family: GH32
• CAZyme Description: Sucrose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489	MGYG000001322_9|CGC5	55359.37	5.32

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001322	3237471	Isolate	not provided	not provided

• Gene Location: Start: 273495; End: 274964 Strand: +

Full Sequence      

MEQVNTLSRARAYEAQHRTPAERRPLFHAVPPVGWCNDPNGWSCFGGQYHLFYQYHPYSN
TWGPMHWGHTVTTDFLHWQDRPCALAPDAPFDRNGCFSGGAIEWQGRQLLLYTGVMPEGS
AEIQQQCLAVGDGVDYQKAAAPVISCDEQPAGASRKDFRDPFLFRQDGMLYMLLGGRGFN
GHGRLLLYRNPRPEDPAAKWEFVQVLAENDGSLGSMWECPGLFTLEGRTVLVVSPQFVHQ
AADDRYHCGNDTAALIGDWNGPGTPFVRRADRPLDSGLDFYAPQTLETPDGRRVLIGWMQ
NWDHCYPPEGAPWYGQMSLPRELFWKGETLCQRPVAELDAVRRLRTEHRSVEVDGQPLAL
EGVHGRVLDCELTVDVHEAPRFGVRFACGQDRWAEIRFDLDDGLLRLDRRHAGGFRDALE
LRETPLLFPVGDTLRLRMVLDRYSAEFFLQDGQQVASMTLYNAAPEADGILFFARGRARM
DLQLYDLAL

Enzyme Prediction     

No EC number prediction in MGYG000001322_00322.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	28	334	1.2e-88	0.9965870307167235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	1.18e-116	16	487	21	484	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd08996	GH32_FFase	3.20e-116	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	5.97e-105	22	457	12	439	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
pfam00251	Glyco_hydro_32N	1.97e-103	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	1.15e-98	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL25413.1	3.63e-137	7	487	5	493
AHF26463.1	1.43e-136	6	487	59	546
CUU49756.1	2.74e-134	7	483	12	488
QUC67231.1	1.33e-132	10	487	12	493
QTE72106.1	2.66e-132	10	487	12	493

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	6.06e-79	25	481	27	478	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
7BWB_A	1.45e-64	24	347	49	359	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A	2.12e-63	24	347	49	359	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
6NUM_A	1.01e-52	25	461	41	485	Thestructure of GH32 from Bifidobacteium adolescentis [Bifidobacterium adolescentis],6NUN_A Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose [Bifidobacterium adolescentis]
3PIG_A	6.04e-52	7	461	21	485	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P16553	1.60e-86	25	478	25	465	Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
P40714	2.57e-81	25	478	26	466	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
P0DJA7	1.17e-72	21	481	26	492	Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
F8DVG5	2.30e-72	21	481	26	492	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
P27217	5.18e-68	25	465	28	442	Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3

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
1.000024	0.000018	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001322_00322.