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CAZyme Information: MGYG000002436_02976

You are here: Home > Sequence: MGYG000002436_02976

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 Pigmentiphaga sp002188635
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Pigmentiphaga; Pigmentiphaga sp002188635
CAZyme ID MGYG000002436_02976
CAZy Family GH13
CAZyme Description Maltooligosyl trehalose synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
895 MGYG000002436_35|CGC1 98427.89 6.6451
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002436 5862145 Isolate Canada North America
Gene Location Start: 61327;  End: 64014  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002436_02976.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 42 351 9e-126 0.9898648648648649

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14507 PRK14507 0.0 7 895 729 1690
malto-oligosyltrehalose synthase.
cd11336 AmyAc_MTSase 0.0 23 784 1 659
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.
COG3280 TreY 0.0 20 895 3 888
Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism].
PRK14511 PRK14511 0.0 20 894 4 876
malto-oligosyltrehalose synthase.
TIGR02401 trehalose_TreY 0.0 21 893 1 823
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
AZG08126.1 0.0 14 895 11 892
QDZ27380.1 9.66e-315 20 893 3 933
ANN77576.1 1.32e-310 21 893 4 896
ALM82504.1 6.08e-301 7 895 6 907
BBK43530.1 1.33e-300 21 893 4 856

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LCV_A 3.20e-135 20 893 1 754
structureof Mutant S44P of maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
6LCU_A 4.82e-134 20 893 1 754
structureof maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
5ZCR_A 3.07e-99 24 797 5 664
DSM5389glycosyltrehalose synthase [Saccharolobus shibatae B12],5ZCR_B DSM5389 glycosyltrehalose synthase [Saccharolobus shibatae B12]
1IV8_A 7.33e-92 23 812 4 669
CrystalStructure of Maltooligosyl trehalose synthase [Sulfolobus acidocaldarius]
3HJE_A 2.56e-86 35 797 14 646
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 1.23e-149 21 893 4 767
Maltooligosyl trehalose synthase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treY PE=1 SV=1
P9WQ20 2.80e-148 32 861 21 744
Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treY PE=3 SV=1
P9WQ21 2.80e-148 32 861 21 744
Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treY PE=1 SV=1
Q9R9H8 6.61e-11 41 137 183 275
Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 SV=2
O06988 6.61e-11 41 137 183 275
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
1.000062 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002436_02976.