CAZyme Information: MGYG000000027_01981

Basic Information

• Species: Mitsuokella jalaludinii
• Lineage: Bacteria; Firmicutes_C; Negativicutes; Selenomonadales; Selenomonadaceae; Mitsuokella; Mitsuokella jalaludinii
• CAZyme ID: MGYG000000027_01981
• CAZy Family: GH32
• CAZyme Description: Sucrose-6-phosphate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
493	MGYG000000027_22|CGC1	56308.16	5.0257

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000027	2393573	Isolate	United Kingdom	Europe

• Gene Location: Start: 27859; End: 29340 Strand: -

Full Sequence      

MSNEQKQLTPDEFIAANESKVNKRWYPRFHIAPRVGWCNDPNGFAYFGGQYHFFYQHYPY
EPKWGPMHWAHVTSKDLVHWERQPVALFPDHPYDADGCFTGSGIEKDGKLYLLYTGHVDL
LKKPGQPDRIETQALAVSTDGIHFEKSEKNPVITLPEGVSTGEDHHFRDPKVWQHNGRYY
AVVGAQTADEVGQVLVFESEDLEDWQFKHVMAKAHGNQGFMWECPNFAEFDGHEALILSP
QGVKPEGKRYLNLHQSVSMLGKMDYESGIFYHDAFHILDHGFDFYAPQVTQTPDGRCLMI
GWLAMWESAMPEQADGWSCQMTVPRELHYRKDRLVTPPAKELTALRKAAHTAPELVMTDE
TPLTDWSYETGEFCADFDLTEAEGLAVHFTAGFDDTVSLMVEKQSGAVTLVRKSAATGRK
EERYAQLPAGERHLSLRVYEDRSSLEFFINDGDIVMSTRFYPKTAERVIVLEPQEGTVRM
TEGVFYELDDIFA

Enzyme Prediction     

No EC number prediction in MGYG000000027_01981.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	30	336	5.8e-104	0.9897610921501706

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR01322	scrB_fam	7.74e-159	5	463	1	445	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG1621	SacC	4.99e-158	1	485	3	482	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd18623	GH32_ScrB-like	5.38e-143	36	331	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.
cd08996	GH32_FFase	5.14e-136	36	327	1	279	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	2.45e-125	30	333	1	301	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AJQ28974.1	1.49e-179	18	488	24	494
BDA10014.1	2.46e-161	22	488	23	490
QIB59957.1	1.40e-160	22	488	23	490
SNU97695.1	1.57e-154	5	473	4	477
BDA10020.1	9.90e-154	8	488	7	493

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	2.83e-112	20	491	20	488	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
7BWB_A	2.44e-97	3	461	26	460	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A	3.81e-96	3	461	26	460	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]
6NUM_A	2.22e-85	1	491	14	515	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	9.68e-82	14	491	28	515	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	3.52e-118	25	488	23	475	Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
P40714	3.29e-113	14	488	13	476	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
F8DVG5	3.61e-103	16	462	19	473	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
P0DJA7	7.19e-103	16	462	19	473	Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
P27217	1.91e-93	26	462	27	439	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
1.000054	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000027_01981.