dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000773_01023

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Basic Information help

Species

Bulleidia sp900539965

Lineage

Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Bulleidia; Bulleidia sp900539965

CAZyme ID

MGYG000000773_01023

CAZy Family

GH32

CAZyme Description

5-dehydro-2-deoxygluconokinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
804	MGYG000000773_14\|CGC1	91780.31	4.653

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000773	2056602	MAG	Japan	Asia

Gene Location

Start: 40751; End: 43165 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000773_01023.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	37	347	2.8e-88	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18623	GH32_ScrB-like	5.52e-150	43	340	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.
TIGR01322	scrB_fam	6.47e-131	22	452	3	443	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG1621	SacC	6.95e-122	3	469	18	469	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd01167	bac_FRK	3.52e-112	487	786	3	294	Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
pfam00251	Glyco_hydro_32N	7.35e-98	37	347	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQP38736.1	1.59e-204	1	478	1	481
CBL38537.1	3.63e-203	1	478	1	481
QCP34478.1	8.35e-199	1	482	1	487
QMW71993.1	2.17e-196	1	482	1	487
BCD35034.1	2.17e-196	1	482	1	487

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	1.75e-63	36	452	29	458	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
6NU7_A	4.32e-62	27	474	27	486	Structureof sucrose-6-phosphate hydrolase from Lactobacillus gasseri [Lactobacillus gasseri 224-1],6NU8_A Structure of sucrose-6-phosphate hydrolase from Lactobacillus gasseri in complex with fructose [Lactobacillus gasseri 224-1]
5EY7_A	2.72e-49	490	800	25	322	Crystalstructure of Fructokinase from Vibrio cholerae O395 in apo form [Vibrio cholerae O395],5EY7_B Crystal structure of Fructokinase from Vibrio cholerae O395 in apo form [Vibrio cholerae O395],5EYN_A Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose, ADP, Beryllium trifluoride and calcium ion bound form [Vibrio cholerae O395],5F0Z_A Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose, ADP and calcium ion bound form [Vibrio cholerae O395],5F11_A Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose bound form [Vibrio cholerae O395]
5YGG_A	3.42e-48	490	800	25	322	Crystalstructure of Fructokinase Double-Mutant (T261C-H108C) from Vibrio cholerae O395 in fructose, ADP and potassium ion bound form [Vibrio cholerae O395]
7BWB_A	6.48e-48	36	452	52	460	Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07819	2.30e-87	14	452	10	453	Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2
Q05936	6.19e-79	3	452	8	463	Sucrose-6-phosphate hydrolase OS=Staphylococcus xylosus OX=1288 GN=scrB PE=3 SV=1
P27217	1.14e-76	27	462	21	449	Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3
P37075	2.20e-76	27	452	21	438	Sucrose-6-phosphate hydrolase OS=Salmonella typhimurium OX=90371 GN=scrB PE=3 SV=1
P13394	2.56e-76	28	452	32	453	Sucrose-6-phosphate hydrolase OS=Vibrio alginolyticus OX=663 GN=scrB PE=2 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000773_01023.