CAZyme Information: MGYG000000019_01609

Basic Information

• Species: Enterobacter cloacae_O
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter cloacae_O
• CAZyme ID: MGYG000000019_01609
• CAZy Family: GH13
• CAZyme Description: Glucosylglycerate phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
565	MGYG000000019_5|CGC3	63760.27	5.554

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000019	4947669	Isolate	United Kingdom	Europe

• Gene Location: Start: 173858; End: 175555 Strand: +

Full Sequence      

MENNVNAKIKNLINHIYGESFSDAHLDVLLTKLEQAAVNIAEKRKSGWDEKDVVLITYAD
QFSAQGEKALPVFTRFYNEWLSRTFSHVHLLPFYPWSSDDGFSVIDYHSVAPETGTWRDV
AELKKSASLMFDFVCNHMSAKSEWFANYLAQKPGFEDFFISVDPDTDLSAVTRPRALPLL
TPFTLHDGSVRHLWTTFSDDQIDLNFASPQVLIAMVDVLLHYLEEGARYIRLDAVGFMWK
IPGTSCIHLEQTHCLIQLFRAITDAVAPGTVIITETNVPHKDNISYFGDGENEAQMVYQF
SLPPLVLHAVHRQDVKALCQWAGSLALPSAHTTWFNFLASHDGIGLNPLRGILPESEILS
LVENLQQEGALVNWKNNPDGTRSPYEINVTYLDALSAQDSSDEERIARFILAHAVLLSFP
GVPAVYIQSILGSRNDYEGVERLGYNRAINRKKYAAGEVDRELNNKNSIRHQIYSRLTSL
IAIRRGERAFHPDSQAIFEAVGEQILKIVRVAENGERITALFNFSNKMQAVNEPALSGME
LLSKYKISGTDLTLNPWQVMWIKEN

Enzyme Prediction     

No EC number prediction in MGYG000000019_01609.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	85	427	3.2e-152	0.9970845481049563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11343	AmyAc_Sucrose_phosphorylase-like	0.0	50	493	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	48	499	1	452	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	1.16e-93	53	493	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	1.89e-77	53	490	5	435	sucrose phosphorylase; Provisional
cd11324	AmyAc_Amylosucrase	1.04e-67	9	490	16	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
QLA70299.1	0.0	5	565	1	561
QLA00513.1	0.0	5	565	1	561
AOQ00148.1	0.0	1	565	1	565
QMI59376.1	0.0	1	565	1	565
AIN28266.1	0.0	1	565	1	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GDV_A	2.34e-48	53	463	5	415	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
1R7A_A	3.24e-48	53	463	5	415	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDU_A	8.53e-48	53	463	5	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	1.18e-47	53	463	5	415	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]
6FME_A	1.22e-47	53	463	6	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	4.43e-293	8	563	4	559	Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
D7BAR0	7.19e-163	13	562	16	553	Glucosylglycerate phosphorylase OS=Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) OX=526227 GN=Mesil_0665 PE=1 SV=1
G0GBS4	3.08e-156	8	526	6	528	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1
P33910	1.48e-53	50	506	2	451	Sucrose phosphorylase OS=Agrobacterium vitis OX=373 PE=3 SV=1
P10249	8.93e-51	54	533	8	473	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4

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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000019_01609.