CAZyme Information: MGYG000001279_02663

Basic Information

• Species: Pseudomonas_E fulva
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E fulva
• CAZyme ID: MGYG000001279_02663
• CAZy Family: GH13
• CAZyme Description: Putative maltooligosyl trehalose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
174		19275	6.089

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001279	4682858	MAG	Italy	Europe

• Gene Location: Start: 7132; End: 7656 Strand: -

Full Sequence      

MPDLYQGNEYWDFSLVDPDNRRPVDYPARRSTLAEAAPLDALLSHWHDGRVKQALVARVL
DCRMANPELFRRGSYLPLTVKGRHADKIVAFARLGDTQRAVIVAPRLASELLGAAQSPHV
PAQNWEDTRVILPFDFSPANSTGLFGGAVVSPVRELMVCAVLSDFPVNLLIEDN

Enzyme Prediction     

No EC number prediction in MGYG000001279_02663.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14511	PRK14511	1.08e-67	1	172	716	877	malto-oligosyltrehalose synthase.
COG3280	TreY	1.52e-49	2	173	722	889	Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism].
PRK14507	PRK14507	1.66e-45	2	134	1510	1652	malto-oligosyltrehalose synthase.
TIGR02401	trehalose_TreY	7.69e-40	2	172	661	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]
cd11336	AmyAc_MTSase	1.28e-27	1	66	594	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDC04054.1	1.76e-116	1	174	751	924
QPH47516.1	1.90e-115	1	174	751	924
QPH42453.1	1.90e-115	1	174	751	924
CRN07794.1	1.90e-115	1	174	751	924
AVF56021.1	1.04e-114	1	174	751	924

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LCU_A	1.36e-17	2	172	607	756	structureof maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
6LCV_A	1.36e-17	2	172	607	756	structureof Mutant S44P of maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
1IV8_A	7.16e-10	1	81	580	661	CrystalStructure of Maltooligosyl trehalose synthase [Sulfolobus acidocaldarius]
5ZCR_A	1.43e-06	1	63	594	653	DSM5389glycosyltrehalose synthase [Saccharolobus shibatae B12],5ZCR_B DSM5389 glycosyltrehalose synthase [Saccharolobus shibatae B12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WQ20	4.65e-18	1	174	621	764	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treY PE=3 SV=1
P9WQ21	4.65e-18	1	174	621	764	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treY PE=1 SV=1
Q44315	2.20e-15	1	174	614	771	Maltooligosyl trehalose synthase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treY PE=1 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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001279_02663.