CAZyme Information: MGYG000001499_01700

Basic Information

• Species: Muricomes contortus_B
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Muricomes; Muricomes contortus_B
• CAZyme ID: MGYG000001499_01700
• CAZy Family: GH13
• CAZyme Description: Sucrose phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
486	MGYG000001499_8|CGC4	56749.31	4.9736

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001499	5155658	Isolate	not provided	not provided

• Gene Location: Start: 224248; End: 225708 Strand: +

Full Sequence      

MKKIENKIMLITYADSMSKDLTELDEILDRHFRDTIGGLHVLPFYPSSGDRGFAVINYDQ
VDPAFGTWDDIDRLAEQYYMMADFMLNHVSIRSGEFRDYMENGDASPYRDMFIHWEEFWP
EGNPTEGQYQALYRRKAVYPYIEFTRKDGKTVHLWNTFFEEQIDINPYAKATKDYYARNL
GTISSHVPLVRFDAFAYASKRPGTSCFFVEPDIWNILDIGMEPLRKTQTEMLPEIHENYQ
IQLKMAEKGYWVYDFALPMLLLHGLKSGRTDRLIHWLNICPRKQFTTLDTHDGIGVVDVA
GLLTEEEIDFVRDDVDEITKEAKQYIKLPSMITAKDGKFKSYQLGSTYYSALRCSDRAYL
IARAVQFYAPGIPQIYYVGLLAGENDIESMKTNPDPRTINRHTFSREELEAAVQKPVCKR
LYELMRFRNNYEAFNGDITIGEDRSDGTLKITWKKENYYTALTADFKELTYQIVYYDEAS
KQECIL

Enzyme Prediction     

EC	2.4.1.7	2.4.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	37	377	4.3e-108	0.9941690962099126

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR03852	sucrose_gtfA	0.0	6	475	1	469	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	440	1	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	4.25e-172	5	440	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	2.74e-148	4	477	1	477	sucrose phosphorylase; Provisional
cd11356	AmyAc_Sucrose_phosphorylase-like_1	8.13e-91	5	439	3	447	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
AYQ75142.1	1.19e-253	1	485	1	486
BCG61532.1	1.67e-188	4	486	3	481
AIQ15040.1	1.93e-187	4	486	3	481
AKG36720.1	1.93e-187	4	486	3	481
QWU16063.1	4.46e-186	4	486	3	481

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6S9V_A	1.06e-130	4	482	17	497	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]
2GDV_A	1.15e-100	4	467	1	468	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
5MB2_B	1.80e-99	4	467	1	468	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]
6FME_A	1.90e-99	4	467	2	469	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol [Bifidobacterium adolescentis ATCC 15703],6FME_B Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol [Bifidobacterium adolescentis ATCC 15703]
5C8B_B	2.39e-99	4	467	3	470	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	1.09e-151	4	478	3	476	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
Q59495	2.39e-150	3	474	2	475	Sucrose phosphorylase OS=Leuconostoc mesenteroides OX=1245 PE=1 SV=1
D9TT09	3.72e-130	4	482	3	483	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	7.79e-122	4	477	3	469	Glucosylglycerol phosphorylase OS=Marinobacter adhaerens (strain DSM 23420 / HP15) OX=225937 GN=gtfA PE=1 SV=1
A0ZZH6	6.28e-100	4	467	1	468	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
1.000031	0.000013	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001499_01700.