CAZyme Information: MGYG000001950_00902

Basic Information

• Species: Gastranaerophilus phascolarctosicola
• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Gastranaerophilus; Gastranaerophilus phascolarctosicola
• CAZyme ID: MGYG000001950_00902
• CAZy Family: GH13
• CAZyme Description: Trehalose synthase/amylase TreS

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
603	MGYG000001950_58|CGC1	70147.37	9.2426

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001950	1886233	MAG	Denmark	Europe

• Gene Location: Start: 106; End: 1917 Strand: +

Full Sequence      

MKIARHSIEERPVSLKKSDETRPDDWYKDEIIYMFYVDQFGVNDGETSSTFHDTTKMFKY
LKDLGVTTLYMLPFAESPMTDAGFDVKNPQNVRKDLGGMKEFKEFITKAKQEGFKIKADL
VLNHFSDEHEWFKSLQNGDLSKLNYFIVRETMPEYKKYQDEKLGTVVEYVEEDGKISKRR
LIFPENTENNWRKITVNGKDYFVYHTFYPFQLDINWENPQVLYYCLQTISYWSNLGIDIF
RMDAIPYLSKEPGTNAENQPKTHAIIKLLSNYIQATAPSSVIQVEACQVPKDILPYFGKE
RTVQWDERELKRTDEAQIAYHFPYMPAIWASLITKDKKYFFDANKATPEIPSTSAWGIFL
RVHDELTLEMVSPEIRELIYNELSPKGASFRKGFGVSGRLANFLDNNPNRIEMAFSILLS
LPGIPIIYYGDEIGVSNNFANANKSAIKRRIKQRTSKIKLLSAFDSRDIHRGEVPYKLFY
GSTNNYYAYNSRVYKKVRNLIHIRKNLPAMTRGEFIPLKTKSPHNFAYIRKDKNQQILVI
NNLSNEKLIAEIKIPMNIILKNDGHITSLKNLINGDDIRVDVSLTNRTMHLRVAPYGVLW
LEL

Enzyme Prediction     

No EC number prediction in MGYG000001950_00902.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	51	436	1.4e-120	0.9886685552407932

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11334	AmyAc_TreS	2.44e-113	26	438	1	378	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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.
cd11324	AmyAc_Amylosucrase	6.37e-90	1	510	38	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.
COG0366	AmyA	2.43e-54	31	563	2	503	Glycosidase [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	6.86e-46	60	513	31	403	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. 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	2.00e-44	26	509	1	441	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOR37731.1	2.07e-311	4	602	77	676
AKB34836.1	3.36e-226	1	602	49	649
QCR16547.1	1.67e-214	14	602	89	668
BBL63642.1	1.67e-214	14	602	89	668
AKB40115.1	1.67e-214	14	602	89	668

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5X7U_A	9.88e-94	26	544	7	492	Trehalosesynthase from Thermobaculum terrenum [Thermobaculum terrenum ATCC BAA-798]
5H2T_A	6.64e-90	26	544	22	511	Structureof trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_B Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_C Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_D Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_E Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_F Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_G Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_H Structure of trehalose synthase [Thermomonospora curvata DSM 43183]
3ZO9_A	5.55e-84	26	544	35	533	ChainA, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZO9_B Chain B, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZOA_A Chain A, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],3ZOA_B Chain B, Trehalose Synthase/amylase Tres [Mycolicibacterium smegmatis],5JY7_A Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_B Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_C Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_D Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_E Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_F Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_G Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155],5JY7_H Complex of Mycobacterium smegmatis trehalose synthase with maltokinase [Mycolicibacterium smegmatis MC2 155]
4WF7_A	1.39e-81	25	544	9	503	Crystalstructures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis [Deinococcus radiodurans R1],4WF7_B Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis [Deinococcus radiodurans R1],4WF7_C Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis [Deinococcus radiodurans R1],4WF7_D Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis [Deinococcus radiodurans R1]
4LXF_A	1.63e-81	26	544	62	554	Crystalstructure of M. tuberculosis TreS [Mycobacterium tuberculosis H37Rv],4LXF_B Crystal structure of M. tuberculosis TreS [Mycobacterium tuberculosis H37Rv]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P72235	1.25e-84	25	544	14	513	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
A0R6E0	3.04e-83	26	544	35	533	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P9WQ19	5.71e-81	26	544	43	535	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS PE=1 SV=1
P9WQ18	5.71e-81	26	544	43	535	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 SV=1
O06458	7.13e-71	26	544	5	489	Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS 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
0.999823	0.000217	0.000003	0.000000	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001950_00902.