CAZyme Information: MGYG000000001_00779

Basic Information

• Species: GCA-900066495 sp902362365
• Lineage: Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; GCA-900066495; GCA-900066495 sp902362365
• CAZyme ID: MGYG000000001_00779
• CAZy Family: GH13
• CAZyme Description: Sucrose 6(F)-phosphate phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
209	MGYG000000001_7|CGC1	24405.97	6.5001

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000001	3219617	Isolate	United Kingdom	Europe

• Gene Location: Start: 39643; End: 40272 Strand: +

Full Sequence      

MTVKNKVQLITYPDSLGGDLKSLNKVLDTYFKDTFKGGIHILPPFPSSGDRGFAPLTYDK
IEPAFGTWEGIRKIGEKHDILVDIMVNHISQKSEFFQDFLKHGKKSKYADLFLTLDKIWP
DEKPVQEDIDKMFLRRDLPYSKFTIEETGEEEMVWTTFGKQDPSEQIDLDINSLKVKELF
TEFFKNFSKQGVKIVRLDCSWIYNQKTRY

Enzyme Prediction     

No EC number prediction in MGYG000000001_00779.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	38	199	2.1e-49	0.42857142857142855

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11355	AmyAc_Sucrose_phosphorylase	1.09e-101	4	198	1	190	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
cd11343	AmyAc_Sucrose_phosphorylase-like	1.81e-76	4	198	1	183	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
TIGR03852	sucrose_gtfA	1.55e-71	5	198	1	189	sucrose phosphorylase. In the forward direction, this enzyme uses phosphate to cleave sucrose into D-fructose + alpha-D-glucose 1-phosphate. Characterized representatives from Streptococcus mutans and Bifidobacterium adolescentis represent well-separated branches of a molecular phylogenetic tree. In S. mutans, the region including this gene has been associated with neighboring transporter genes and multiple sugar metabolism.
PRK13840	PRK13840	1.16e-58	4	198	2	193	sucrose phosphorylase; Provisional
cd11356	AmyAc_Sucrose_phosphorylase-like_1	1.87e-45	9	198	8	185	Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CED94009.1	1.03e-109	1	198	1	198
AGF59506.1	8.32e-109	1	198	1	198
AQR98194.1	8.32e-109	1	198	1	198
AGX06313.1	1.53e-106	1	198	1	198
AYQ72405.1	5.97e-106	1	198	1	198

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6S9V_A	7.97e-100	1	198	15	211	Crystalstructure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum [Thermoanaerobacterium thermosaccharolyticum DSM 571],6S9V_B Crystal structure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum [Thermoanaerobacterium thermosaccharolyticum DSM 571]
5C8B_B	6.67e-35	1	198	1	194	Structuralinsights into the redesign of a sucrose phosphorylase by induced loop repositioning [Bifidobacterium adolescentis]
2GDV_A	3.07e-34	3	198	1	192	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
2GDU_A	3.07e-34	3	198	1	192	E232Qmutant of sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS in complex with sucrose [Bifidobacterium adolescentis],2GDU_B E232Q mutant of sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS in complex with sucrose [Bifidobacterium adolescentis]
5MB2_B	3.07e-34	3	198	1	192	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D9TT09	2.93e-99	1	198	1	197	Sucrose 6(F)-phosphate phosphorylase OS=Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) OX=580327 GN=spp PE=1 SV=1
P10249	1.90e-52	1	198	1	193	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
Q59495	7.45e-49	1	198	1	196	Sucrose phosphorylase OS=Leuconostoc mesenteroides OX=1245 PE=1 SV=1
E4PMA5	8.56e-42	1	198	1	190	Glucosylglycerol phosphorylase OS=Marinobacter adhaerens (strain DSM 23420 / HP15) OX=225937 GN=gtfA PE=1 SV=1
A0ZZH6	1.68e-33	3	198	1	192	Sucrose phosphorylase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=sucP PE=1 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000001_00779.