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CAZyme Information: MGYG000001270_01370

You are here: Home > Sequence: MGYG000001270_01370

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Corynebacterium sp902373425
Lineage Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium sp902373425
CAZyme ID MGYG000001270_01370
CAZy Family GH13
CAZyme Description Putative maltooligosyl trehalose synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
840 92954.4 4.9291
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001270 2256923 MAG Italy Europe
Gene Location Start: 646;  End: 3168  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 5.4.99.15

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 35 321 1.4e-100 0.9898648648648649

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11336 AmyAc_MTSase 0.0 8 735 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.
PRK14507 PRK14507 0.0 8 831 745 1692
malto-oligosyltrehalose synthase.
PRK14511 PRK14511 0.0 2 829 1 877
malto-oligosyltrehalose synthase.
COG3280 TreY 0.0 7 830 5 889
Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism].
TIGR02401 trehalose_TreY 0.0 7 829 2 825
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]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ64796.1 0.0 1 840 1 840
QRP15105.1 0.0 1 840 1 840
QRP10994.1 0.0 1 840 1 840
ACR17533.1 0.0 1 840 1 840
QPR30625.1 0.0 1 830 1 816

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LCU_A 9.04e-184 7 828 3 755
structureof maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
6LCV_A 5.07e-183 7 828 3 755
structureof Mutant S44P of maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
5ZCR_A 1.89e-98 6 692 2 631
DSM5389glycosyltrehalose synthase [Saccharolobus shibatae B12],5ZCR_B DSM5389 glycosyltrehalose synthase [Saccharolobus shibatae B12]
1IV8_A 9.40e-88 6 680 2 605
CrystalStructure of Maltooligosyl trehalose synthase [Sulfolobus acidocaldarius]
3HJE_A 9.16e-86 6 790 3 682
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
P9WQ21 3.34e-223 8 830 7 763
Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treY PE=1 SV=1
P9WQ20 3.34e-223 8 830 7 763
Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treY PE=3 SV=1
Q44315 1.29e-181 4 831 2 771
Maltooligosyl trehalose synthase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treY PE=1 SV=1
O06988 9.18e-16 20 136 166 279
Intracellular maltogenic amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=bbmA PE=3 SV=2
Q9R9H8 1.21e-15 20 136 166 279
Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 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
1.000090 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001270_01370.