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CAZyme Information: MGYG000001503_01665

You are here: Home > Sequence: MGYG000001503_01665

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 Fermentimonas caenicola
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Fermentimonas; Fermentimonas caenicola
CAZyme ID MGYG000001503_01665
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
799 MGYG000001503_2|CGC18 91464.38 4.5895
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001503 2824716 Isolate not provided not provided
Gene Location Start: 823316;  End: 825715  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001503_01665.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 352 576 4.9e-45 0.6389776357827476

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11350 AmyAc_4 0.0 327 713 1 390
Alpha amylase catalytic domain found in an uncharacterized protein family. 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 (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.
cd11325 AmyAc_GTHase 1.34e-55 326 661 22 361
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
COG0296 GlgB 5.47e-51 223 760 49 570
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523 PulA 5.39e-35 170 508 4 360
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551 AmyAc_family 2.25e-34 343 662 1 257
Alpha amylase catalytic domain family. 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; and 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 this 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CEA14981.1 0.0 1 799 1 799
QRX64494.1 0.0 19 797 11 798
SCD19325.1 0.0 9 799 1 776
BBD44659.1 0.0 9 797 1 779
QKH86932.1 0.0 53 797 219 952

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1EHA_A 6.57e-30 242 614 34 378
CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A 6.57e-30 242 614 34 378
Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EH9_A 6.57e-30 242 614 34 378
CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGD_A 2.09e-29 242 614 34 378
Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A 3.72e-29 242 614 34 378
Crystalstructure of glycosyltrehalose trehalohydrolase (D252S) [Saccharolobus solfataricus],3VGF_A Crystal structure of glycosyltrehalose trehalohydrolase (D252S) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q6LHN1 7.10e-30 226 749 139 645
1,4-alpha-glucan branching enzyme GlgB OS=Photobacterium profundum (strain SS9) OX=298386 GN=glgB PE=3 SV=1
Q55088 3.63e-29 242 614 35 379
Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
Q15VD0 2.19e-28 226 764 149 670
1,4-alpha-glucan branching enzyme GlgB OS=Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) OX=342610 GN=glgB PE=3 SV=1
P95867 2.79e-28 277 614 49 381
Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q8CZE8 5.51e-25 226 752 51 563
1,4-alpha-glucan branching enzyme GlgB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=glgB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000016 0.000515 0.999473 0.000004 0.000001 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001503_01665.