dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000093_01854

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Basic Information help

Species

Klebsiella_A grimontii

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella_A; Klebsiella_A grimontii

CAZyme ID

MGYG000000093_01854

CAZy Family

GH13

CAZyme Description

Maltooligosyl trehalose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
846	MGYG000000093_2\|CGC13	94877.2	5.0836

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000093	6212272	Isolate	United Kingdom	Europe

Gene Location

Start: 791072; End: 793612 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000093_01854.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	24	307	5.2e-120	0.9898648648648649

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
PRK14511	PRK14511	1	819	3	855	malto-oligosyltrehalose synthase.
COG3280	TreY	1	831	2	877	Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism].
PRK14507	PRK14507	2	824	742	1671	malto-oligosyltrehalose synthase.
cd11336	AmyAc_MTSase	5	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.
TIGR02401	trehalose_TreY	3	818	1	802	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]

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QXW42034.1	1	846	1	846
AWT20779.1	1	846	1	846
QLT88258.1	1	846	1	846
QQQ22520.1	1	846	1	846
QHI87801.1	1	846	1	846

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LCU_A	2.80e-133	2	823	1	744	structureof maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
6LCV_A	5.52e-133	2	823	1	744	structureof Mutant S44P of maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
5ZCR_A	7.09e-111	6	769	5	684	DSM5389glycosyltrehalose synthase [Saccharolobus shibatae B12],5ZCR_B DSM5389 glycosyltrehalose synthase [Saccharolobus shibatae B12]
3HJE_A	7.90e-102	5	774	5	665	Crystalstructure of sulfolobus tokodaii hypothetical maltooligosyl trehalose synthase [Sulfurisphaera tokodaii str. 7]
1IV8_A	1.04e-91	4	766	3	671	CrystalStructure of Maltooligosyl trehalose synthase [Sulfolobus acidocaldarius]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44315	2.89e-143	3	811	4	748	Maltooligosyl trehalose synthase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treY PE=1 SV=1
P9WQ21	1.22e-118	5	804	7	730	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treY PE=1 SV=1
P9WQ20	1.22e-118	5	804	7	730	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treY PE=3 SV=1
P14898	7.02e-10	26	117	174	260	Alpha-amylase 2 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyB PE=1 SV=2
P32818	6.62e-09	26	119	184	273	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1

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
0.999840	0.000194	0.000002	0.000001	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000093_01854.