CAZyme Information: MGYG000000761.1_00076

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus
• CAZyme ID: MGYG000000761.1_00076
• CAZy Family: GH13
• CAZyme Description: Sucrose phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483	MGYG000000761.1_3|CGC1	56629.33	5.0282

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000761.1	1538831	MAG	Bangladesh	Asia

• Gene Location: Start: 19923; End: 21374 Strand: +

Full Sequence      

MGIQNKTMLITYSDSLGKDLKDLKENLEKYFKDAVGGVHILPFFPSTGDRGFAPIDYDEV
DPKFGDWKDIKALGERYYLMFDFMINHISRKSKYYKDYQEKHEDSEYKDLFLNWDKFWPE
NRPSQADIDLIYKRKDRAPKQEIKFKDGSVENLWNTFGEEQIDLDVRTEVTMDFIKKNID
NLSKKGCDIIRLDAFAYAIKKLDTNDFFVEPEIWDLLDKIREMAVKNNVEILPEIHEHYK
IQFKIASHDYFIYDFALPMLTLYSLYSGKVDRLKNWLEKSPMKQFTTLDTHDGIGVVDVK
DIMTDDEIAFTTDQLYKVGANVNRKYSTAEYNNLDIYQINTTYYSALGDDDKKYFIARLI
QAFAPGIPQVYYVGFLAGKNDLKLLEETKEGRNINRHYYSNEEIAREVERPIVKALLMLF
KFRNRSEAFDLEGSISVENEGENIIIITRKNKDGSAVAKARIDIKNLTYKVTENDKEIEF
LNI

Enzyme Prediction     

EC	2.4.1.7	2.4.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	36	372	2.2e-122	0.9941690962099126

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR03852	sucrose_gtfA	0.0	5	474	1	470	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.
cd11355	AmyAc_Sucrose_phosphorylase	0.0	5	435	2	433	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	0.0	4	435	1	445	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.
PRK13840	PRK13840	6.20e-159	3	459	1	463	sucrose phosphorylase; Provisional
cd11356	AmyAc_Sucrose_phosphorylase-like_1	8.17e-95	4	429	3	442	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
ACV28293.1	0.0	1	483	1	483
QEY06394.1	2.00e-294	1	480	1	480
VEI60739.1	2.00e-294	1	480	1	480
AEZ61571.1	1.06e-291	1	480	1	480
AFJ26298.1	1.47e-291	1	480	19	498

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6S9V_A	4.64e-134	1	481	15	501	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]
1R7A_A	2.75e-107	3	456	1	461	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDV_A	5.47e-107	3	456	1	461	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
2GDU_A	7.72e-107	3	456	1	461	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]
5C8B_B	2.06e-106	1	456	1	463	Structuralinsights into the redesign of a sucrose phosphorylase by induced loop repositioning [Bifidobacterium adolescentis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P10249	3.65e-291	1	480	1	480	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
Q59495	1.67e-233	1	478	1	481	Sucrose phosphorylase OS=Leuconostoc mesenteroides OX=1245 PE=1 SV=1
D9TT09	1.62e-133	1	481	1	487	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
E4PMA5	1.99e-121	1	477	1	471	Glucosylglycerol phosphorylase OS=Marinobacter adhaerens (strain DSM 23420 / HP15) OX=225937 GN=gtfA PE=1 SV=1
A0ZZH6	3.00e-106	3	456	1	461	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
1.000048	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000761.1_00076.