dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003382_01977

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Basic Information help

Species

Pantoea agglomerans

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Pantoea; Pantoea agglomerans

CAZyme ID

MGYG000003382_01977

CAZy Family

GH13

CAZyme Description

Maltooligosyl trehalose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
842	MGYG000003382_22\|CGC1	93734.65	4.8338

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003382	4723531	MAG	United States	North America

Gene Location

Start: 39639; End: 42167 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003382_01977.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	25	309	1.4e-121	0.9898648648648649

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
cd11336	AmyAc_MTSase	6	737	1	660	Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase). Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. 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.
PRK14511	PRK14511	1	842	2	878	malto-oligosyltrehalose synthase.
PRK14507	PRK14507	3	828	742	1676	malto-oligosyltrehalose synthase.
TIGR02401	trehalose_TreY	4	841	1	825	malto-oligosyltrehalose synthase. This enzyme, formally named (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase, is the TreY enzyme of the TreYZ pathway of trehalose biosynthesis, an alternative to the OtsAB pathway. Trehalose may be incorporated into more complex compounds but is best known as compatible solute. It is one of the most effective osmoprotectants, and unlike the various betaines does not require nitrogen for its synthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG3280	TreY	1	841	1	888	Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QIA51378.1	1	842	1	842
QTC49005.1	1	842	1	842
AOE41157.1	1	842	1	842
AYP23360.1	1	842	1	842
AZI50924.1	1	842	1	842

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LCU_A	1.06e-126	3	818	1	734	structureof maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
6LCV_A	2.09e-126	3	818	1	734	structureof Mutant S44P of maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
5ZCR_A	1.75e-102	7	706	5	627	DSM5389glycosyltrehalose synthase [Saccharolobus shibatae B12],5ZCR_B DSM5389 glycosyltrehalose synthase [Saccharolobus shibatae B12]
1IV8_A	3.62e-90	5	752	3	661	CrystalStructure of Maltooligosyl trehalose synthase [Sulfolobus acidocaldarius]
3HJE_A	1.84e-88	6	777	5	670	Crystalstructure of sulfolobus tokodaii hypothetical maltooligosyl trehalose synthase [Sulfurisphaera tokodaii str. 7]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44315	3.05e-141	1	823	1	751	Maltooligosyl trehalose synthase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treY PE=1 SV=1
P9WQ20	1.96e-130	6	821	7	743	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treY PE=3 SV=1
P9WQ21	1.96e-130	6	821	7	743	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treY PE=1 SV=1
Q9R9H8	1.66e-12	27	120	186	275	Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 SV=2
O06988	1.66e-12	27	120	186	275	Intracellular maltogenic amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=bbmA PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000060	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003382_01977.