CAZyme Information: MGYG000003395_01554

Basic Information

• Species: Superficieibacter sp900766525
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Superficieibacter; Superficieibacter sp900766525
• CAZyme ID: MGYG000003395_01554
• CAZy Family: GH13
• CAZyme Description: Glucosylglycerate phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
561	MGYG000003395_41|CGC2	63802.22	5.8349

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003395	5080781	MAG	United States	North America

• Gene Location: Start: 72311; End: 73996 Strand: -

Full Sequence      

MKEKINQLLNDVYADAFSAAHREALFTAIDRSKSLIAQQRKQGWDESDVVLITYADQFHH
AEQKPLAVFNQFYQKWFKSVFSHVHLLPFCPWSSDDGFSVIDYHRVAPESGDWNDIAELK
TQTKLMFDFVCNHMSAKSEWFNNYLQQKPGFENFFIEMDPETDLSAVTRPRALPLLTPFT
LSDGSVRHLWTTFSEDQIDLNYACPEVLLAMVDVLLHYLLQGADYIRLDAVGFMWKTPGT
SCIHLEKTHLLIKLFRAIADAVAPGTVIITETNVPHKDNISYLGSGSDEAHMVYQFSLPP
LVLHSVHSQDATALCRWAQSLTLPSDKTTWFNFLASHDGVGLNPLRGILPEDDILQLVDK
LQQQGALVNWKNNPDGSRSPYEINVTYMDALSRQDDSDDERLARFTLAHAILLTFPGVPA
VYIQSIMGSRNDYAGVEKLGYNRAINRQKYDATEIEQQLFASDSLRSRAYHILSQLIVLR
RQHKAFHPDSQFTIQTLNPSVLLITRTANDGEEITALFNISDKEQHVDANVQGGFDLINK
HAVMDTSVTLRPWQVTWIKKQ

Enzyme Prediction     

No EC number prediction in MGYG000003395_01554.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	81	423	1.6e-150	0.9970845481049563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11343	AmyAc_Sucrose_phosphorylase-like	0.0	46	492	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.
cd11356	AmyAc_Sucrose_phosphorylase-like_1	0.0	44	502	1	458	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.
cd11355	AmyAc_Sucrose_phosphorylase	6.12e-89	49	494	4	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.
PRK13840	PRK13840	1.12e-78	49	533	5	479	sucrose phosphorylase; Provisional
TIGR03852	sucrose_gtfA	4.85e-68	49	530	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCU56310.1	0.0	1	561	1	560
QRG81036.1	5.14e-309	1	560	1	560
QUC32120.1	8.48e-308	1	560	1	560
SQJ42134.1	2.42e-307	1	560	1	560
SQI70203.1	2.42e-307	1	560	1	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1R7A_A	5.25e-46	46	459	2	415	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDV_A	9.98e-46	46	459	2	415	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
2GDU_A	1.38e-45	46	459	2	415	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	4.97e-45	46	459	2	415	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]
6FME_A	5.14e-45	46	459	3	416	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76041	2.31e-301	1	559	1	559	Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
D7BAR0	2.41e-165	37	558	40	553	Glucosylglycerate phosphorylase OS=Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) OX=526227 GN=Mesil_0665 PE=1 SV=1
G0GBS4	9.77e-154	3	525	5	531	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1
P10249	2.23e-57	50	532	8	476	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
P33910	3.59e-51	46	509	2	456	Sucrose phosphorylase OS=Agrobacterium vitis OX=373 PE=3 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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003395_01554.