CAZyme Information: MGYG000002889_02066

Basic Information

• Species: Pantoea sp002920175
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Pantoea; Pantoea sp002920175
• CAZyme ID: MGYG000002889_02066
• CAZy Family: GH13
• CAZyme Description: Glucosylglycerate phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
563		63592.29	5.9341

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002889	4513078	MAG	United States	North America

• Gene Location: Start: 40634; End: 42325 Strand: -

Full Sequence      

METITALLDKIYADTFPQAARERLLSHIIAARDAVKLPRKAHWDEQDIVLITYADQFREA
EVPTLQSFSRFYQQHLQSTFPLVHLLPFFPYSSDDGFSVIDYHQVNPLCGDWPDVASLHQ
ETRLMFDFVCNHMSAHSAWFKHYLALDPGWDDFFISMPPATDLSAVTRPRTSPLLTPFEM
ANGEMRFIWTTFSADQIDLNFGNPEVLIRMVDVLLDYLQKGADYVRLDAVGYMWKTPGTR
CIHLEKTHLLVKLFRAIADIVAPGTVIITETNVPHKDNVSYFGNSHDEAQMVYQFSLPPL
VLHAIHSGSGRALRQWAGALEPGQGGTTFFNFLASHDGIGLNPARGILSEVEIVALVRDL
ALEGALVSYKNNPDGTTSPYEINVSYLDALNHQNDDDDTRLRRFLLAHAILLAFPGVPAI
YIQSILGSRNDYEGVKAAGHNRAINRQKFDLKTIEAALADGDSLRHAIYTRLSQLIQLRT
RQPAFHPDNPMRLYDSDNALLVLRRHPPQQEDSGLLCVFNLSAKTVEVTLPEARLFQDAI
TERKIDGTQPLTLDAWQFVWLRS

Enzyme Prediction     

No EC number prediction in MGYG000002889_02066.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	82	422	7.9e-146	0.9912536443148688

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11343	AmyAc_Sucrose_phosphorylase-like	0.0	45	491	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	43	501	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	1.81e-85	48	488	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	2.45e-71	50	485	7	435	sucrose phosphorylase; Provisional
cd11324	AmyAc_Amylosucrase	6.70e-65	83	485	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
QAV46135.1	0.0	1	562	1	561
QAV50976.1	0.0	1	562	1	561
QGY56680.1	0.0	1	562	1	561
AZI52548.1	0.0	1	562	1	561
AOE39314.1	0.0	1	562	1	561

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3UCQ_A	4.49e-45	83	526	128	607	Crystalstructure of amylosucrase from Deinococcus geothermalis [Deinococcus geothermalis DSM 11300],3UER_A Crystal structure of amylosucrase from Deinococcus geothermalis in complex with turanose [Deinococcus geothermalis DSM 11300]
1R7A_A	1.73e-43	48	485	5	436	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDV_A	3.26e-43	48	485	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	4.49e-43	48	485	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]
4AYS_A	1.55e-42	83	561	123	644	TheStructure of Amylosucrase from D. radiodurans [Deinococcus radiodurans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76041	8.31e-226	2	562	3	559	Glucosylglycerate phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjM PE=1 SV=2
D7BAR0	4.51e-158	39	561	43	553	Glucosylglycerate phosphorylase OS=Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) OX=526227 GN=Mesil_0665 PE=1 SV=1
G0GBS4	1.85e-154	44	561	53	580	Glucosylglycerate phosphorylase OS=Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) OX=869211 GN=Spith_0877 PE=1 SV=1
P33910	2.72e-52	45	501	2	451	Sucrose phosphorylase OS=Agrobacterium vitis OX=373 PE=3 SV=1
P10249	2.94e-47	49	529	8	472	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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002889_02066.