CAZyme Information: MGYG000000244_01924

Basic Information

• Species: Catenibacterium sp000437715
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium sp000437715
• CAZyme ID: MGYG000000244_01924
• CAZy Family: GH32
• CAZyme Description: Sucrose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
421	MGYG000000244_49|CGC1	48627.84	5.8624

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000244	2463343	Isolate	China	Asia

• Gene Location: Start: 10512; End: 11777 Strand: +

Full Sequence      

MKNRKQAYHIETEKGLINDPNGLSYFKGKYYVFFQWNPNTTDHSYKVWGKTTSQDLIHWS
EPIIALQASEAYDKDGTYSGSAVSDGETLSLYYTGNVKREGVRYPEQCLAQSKDGVHFKK
YGSVLSLPDDYTGHFRDPKVTKEDVWKMIIGGQNKKTGRGNIIQYTSIDGTSFKFNKIIG
ISKQYEMIECPDLFTLDAHEVLIYGLQSRNNDTDECLDAHAVYLIDTLSDLDKGMHMDEG
YDFYAPQTFVDAQGRRIMLAWMSRFSDAQEVEFAKDGHIHCLTMPRELSVKKGKLIQSPV
REMYELCHEIPYTNHMKIQRQAMIEISPLEHISFSINKELSIHFNEGISIERYDWAEQKY
QKKSWPIKINHMEIWLDTSSVEIFANNGEFVYSARLDPQAEDLLLASSKESQNINVYRLE
I

Enzyme Prediction     

No EC number prediction in MGYG000000244_01924.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	9	299	2.2e-80	0.9965870307167235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18623	GH32_ScrB-like	2.86e-120	15	292	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.
COG1621	SacC	1.62e-106	5	402	29	463	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	9.47e-100	9	388	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	6.84e-99	9	299	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.
cd08996	GH32_FFase	2.86e-81	15	290	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUE54017.1	2.17e-89	5	402	6	422
AQP42520.1	2.42e-88	1	420	1	441
SQG79825.1	2.42e-88	1	420	1	441
AKG74596.1	4.32e-87	8	405	31	458
QPC47776.1	2.21e-86	8	402	32	458

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	2.81e-56	7	420	28	481	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
7BWB_A	1.22e-48	8	419	52	482	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A	1.72e-47	8	419	52	482	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
1UYP_A	4.38e-45	5	420	3	428	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	1.18e-44	5	420	3	428	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07819	1.05e-84	5	419	29	478	Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2
P27217	7.39e-74	8	398	30	439	Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3
P37075	8.05e-73	8	407	30	448	Sucrose-6-phosphate hydrolase OS=Salmonella typhimurium OX=90371 GN=scrB PE=3 SV=1
P40714	3.76e-69	8	402	28	454	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
A1STJ9	3.10e-65	8	396	99	513	Probable sucrose-6-phosphate hydrolase OS=Psychromonas ingrahamii (strain 37) OX=357804 GN=Ping_0974 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
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000244_01924.