CAZyme Information: MGYG000001317_03195

Basic Information

• Species: Citrobacter portucalensis_A
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter portucalensis_A
• CAZyme ID: MGYG000001317_03195
• CAZy Family: GH13
• CAZyme Description: Glucosylglycerate phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
568	MGYG000001317_10|CGC14	64771.48	5.9853

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001317	5150259	Isolate	not provided	not provided

• Gene Location: Start: 1005201; End: 1006907 Strand: +

Full Sequence      

MGPLPREMKVNQKIQKCLSEVYGDTFTSLHYAALIARLDKSQKLIKKHRKAHWDEGDVVL
ITYADQFNGDDKKPLPTFNQFYNEWLKSTFSHVHLLPFYPWSSDDGFSVINYYQVAEETG
DWNDIKQLGESSRLMFDFVCNHMSAKSEWFNNYLQQLDGYEDFFIAMDPDTDLSNVTRPR
ALPLLTPFTLKDNTVRHLWTTFSDDQIDLNYANPLVLLAMVDVLLNYLEQGADYVRLDAV
GFMWKEPGTTCIHLEKTHQLIKLFRAIADCVAPGTAIVTETNVPHKDNISYYGNGRDEAH
MVYQFSLPPLVLHAVQRQDATTLCKWAQSLELPSSETTWFNFLASHDGIGLNPLRGLLPE
EEIMRLVTELQQEGALVNWKNNPDGSRSPYEINVTYMDALTPGNSSNTERFARFILAHAI
LLSFPGVPAIYIQSILGSRNDYKGVEALGYNRAINRKKYHIRQIEAELADETNLRHAVYH
ELSRLIVLRRSNKAFHPDSDFKINSVTAAVMQIKRTAETGEEITGLFNISGHTQTISIDI
ENGLDLISGKTISGKELTLHAWQVMWVK

Enzyme Prediction     

No EC number prediction in MGYG000001317_03195.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	90	432	4e-150	0.9970845481049563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11343	AmyAc_Sucrose_phosphorylase-like	0.0	55	498	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	53	503	1	450	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	1.21e-94	58	503	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	4.75e-79	58	495	5	435	sucrose phosphorylase; Provisional
TIGR03852	sucrose_gtfA	1.45e-68	58	537	3	468	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
QET66668.1	0.0	1	568	1	568
AYL66232.1	0.0	1	568	1	568
BBV30711.1	0.0	1	568	1	568
BBV35724.1	0.0	1	568	1	568
AWS96803.1	0.0	1	568	1	568

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6S9V_A	1.80e-43	58	543	21	495	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	4.47e-42	58	495	5	436	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDV_A	8.43e-42	58	495	5	436	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
2GDU_A	1.16e-41	58	495	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	4.10e-41	58	495	5	436	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76041	2.26e-310	10	568	1	559	Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
D7BAR0	2.07e-160	1	567	1	553	Glucosylglycerate phosphorylase OS=Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) OX=526227 GN=Mesil_0665 PE=1 SV=1
G0GBS4	5.47e-155	8	530	1	527	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1
P10249	2.60e-56	59	539	8	481	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
P33910	2.74e-48	55	496	2	436	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
1.000081	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001317_03195.