CAZyme Information: MGYG000004370_00805

Basic Information

• Species: CAG-484 sp900321895
• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; CAG-484; CAG-484 sp900321895
• CAZyme ID: MGYG000004370_00805
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
681	MGYG000004370_8|CGC2	78731.71	9.4692

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004370	1784002	MAG	Israel	Asia

• Gene Location: Start: 22970; End: 25015 Strand: +

Full Sequence      

MKKLLLKFCIFSFFLCSSLHQVYADVLNQNLDSVANSSKQNIEYKIDGKISKELKEAIED
VYGKENVDEIYNVILDKVVASINSRPAELKQQDLLRSSDWYKNEIIYMFYVDQFGVIQQN
KSNTFSDATKMLKYLKNLGVTTLYILPFADSPMKDAGFDVKNPQTVRQDLGGMKEFISFV
KQAKAYGFRIKADLVLNHFSSEHEWFKRLEQGDESALKYFVYTDKEPKYRKYQDEKLGTV
IEYVEDDGKVSKRRLIFPENVENNYRKVTVNGKIYYLYHTFYPFQLDINWENPEVLYYAL
DTITNWTNLGIDIFRMDAIPYLIKEKGTSAENLPRTHSVIKILSDYIQLTAPSSVMQVEA
CQQPKDILPYFGKERDVDILINNKVKTIKRTNEAQIAYHFPYMPALWASFVTEDKKYFID
AYKNTPQIPKTAAWGMFLRVHDELTLEMVSPEVRKIVYNDLIAKGAEFRKGFGISGRLSN
FLDKNPDRIEMAYSILFSLPGIPIIYYGDEVGVTNNFENAKISALLRSKNKIANLLSVFD
SRDINRGKVSAKLFYGSSLGYYKYNSQVYNRVSNLIKIRKALPVMRNGDFELLTTKSKSN
FAYLRKNKTQQILVINNLSKEKLCADITLPLDIIVKNEGNIVKLKNLINGDNIKVNISLK
NRTMHLRLAPHQTLWLDITPN

Enzyme Prediction     

No EC number prediction in MGYG000004370_00805.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	125	513	2.2e-120	0.9858356940509915

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11334	AmyAc_TreS	6.10e-113	100	518	1	380	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	3.43e-88	53	585	15	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	4.04e-53	105	632	2	495	Glycosidase [Carbohydrate transport and metabolism].
cd11343	AmyAc_Sucrose_phosphorylase-like	3.22e-47	102	591	1	444	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	1.44e-43	133	583	32	440	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	0.0	1	681	1	680
AKB34836.1	7.56e-233	50	677	24	649
QCR16547.1	3.07e-212	87	677	88	668
BBL63642.1	3.07e-212	87	677	88	668
AKB40115.1	3.07e-212	87	677	88	668

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5X7U_A	8.50e-91	100	629	7	502	Trehalosesynthase from Thermobaculum terrenum [Thermobaculum terrenum ATCC BAA-798]
5H2T_A	9.72e-80	96	620	18	512	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	1.57e-79	98	620	33	534	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	1.38e-77	99	619	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]
5YKB_A	2.68e-77	99	619	9	503	TheN253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site conformation [Deinococcus radiodurans R1],5YKB_B The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site conformation [Deinococcus radiodurans R1],5YKB_C The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site conformation [Deinococcus radiodurans R1],5YKB_D The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site conformation [Deinococcus radiodurans R1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0R6E0	8.58e-79	98	620	33	534	Trehalose synthase/amylase TreS OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=treS PE=1 SV=1
P9WQ19	3.02e-75	100	620	43	536	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS PE=1 SV=1
P9WQ18	3.02e-75	100	620	43	536	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 SV=1
P72235	8.50e-74	99	620	14	514	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
O06458	1.06e-69	100	629	5	499	Trehalose synthase OS=Thermus thermophilus OX=274 GN=treS PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000610	0.796623	0.201958	0.000278	0.000267	0.000238

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004370_00805.