CAZyme Information: MGYG000002500_02660

Basic Information

• Species: Enterobacter cloacae
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter cloacae
• CAZyme ID: MGYG000002500_02660
• CAZy Family: GH13
• CAZyme Description: Glucosylglycerate phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
561	MGYG000002500_2|CGC39	63732.24	6.343

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002500	5087499	Isolate	not provided	not provided

• Gene Location: Start: 2642065; End: 2643750 Strand: -

Full Sequence      

MNDKIKNLINLVYGESFSEAHRETLSGKISRAAAVITEKRKAGWDEKDIVLITYADQFYN
KGEKALPVFTRFYNRWLSRSFSHVHLLPFYPWSSDDGFSVIDYHDVAPETGTWQDVAELK
QYASLMFDFVCNHMSAKSQWFAHYLAQKPGYEDFFISVDPQTDLSAVTRPRALPLLTPFT
LDDGSVRHLWTTFSDDQIDLNFASPEVLIAMVDVLLHYLMEGARYIRLDAVGFMWKIPGT
SCIHLEQTHRLIQLFRAITDAVAPGTVIITETNVPHKDNVSYFGDGKNEAQMVYQFSLPP
LVLHAVHRQDVRALCQWATSLELPSKQTTWFNFLASHDGIGLNPLRGILPESEILSLVET
LQQEGALVNWKNNPDGTRSPYEINVTYLDALSAKKDEDTLRIARFILAHAVLLSFPGVPA
IYIQSIIGSRNDYEGVERLGYNRAINRKKYQAGEIDHKLDDINSLRHKVYSGLSALISLR
RQEKAFHPDSQARFETSGEHVLKIVRIADNGERITALFNFSNDIQHVPSNSQAGKDLITG
NNINDTTLTLNPWQVMWIKEN

Enzyme Prediction     

No EC number prediction in MGYG000002500_02660.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	81	423	1.2e-152	0.9970845481049563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11343	AmyAc_Sucrose_phosphorylase-like	0.0	46	489	1	442	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	490	1	446	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	1.07e-89	49	489	4	430	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	9.66e-77	51	495	7	440	sucrose phosphorylase; Provisional
cd11324	AmyAc_Amylosucrase	2.72e-67	84	486	103	536	Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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
ASQ18263.1	0.0	1	561	1	561
QCZ37169.1	0.0	1	561	1	561
QGN43093.1	0.0	1	561	1	561
AOE95760.1	0.0	1	561	1	561
AIV29987.1	0.0	1	561	1	561

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GDV_A	2.89e-47	49	486	5	436	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
1R7A_A	4.00e-47	49	486	5	436	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDU_A	1.05e-46	49	486	5	436	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	1.45e-46	49	486	5	436	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]
6FME_A	1.50e-46	49	486	6	437	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	1.45e-283	1	559	1	559	Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
D7BAR0	1.56e-163	38	558	41	553	Glucosylglycerate phosphorylase OS=Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) OX=526227 GN=Mesil_0665 PE=1 SV=1
G0GBS4	2.76e-153	3	521	5	527	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1
P10249	1.57e-49	50	532	8	476	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
P33910	2.42e-48	46	502	2	451	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
1.000086	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002500_02660.