Species | ||||||||||||
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Lineage | Bacteria; Patescibacteria; Saccharimonadia; Saccharimonadales; Saccharimonadaceae; UBA1103; | |||||||||||
CAZyme ID | MGYG000000376_00600 | |||||||||||
CAZy Family | CBM48 | |||||||||||
CAZyme Description | 1,4-alpha-glucan branching enzyme GlgB | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2064; End: 3794 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 142 | 439 | 1.5e-54 | 0.9933554817275747 |
CBM48 | 3 | 82 | 1e-15 | 0.9078947368421053 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11325 | AmyAc_GTHase | 6.86e-113 | 76 | 474 | 1 | 402 | 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 | 3.78e-93 | 15 | 573 | 40 | 626 | 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]. |
PRK12313 | PRK12313 | 1.75e-71 | 3 | 573 | 26 | 625 | 1,4-alpha-glucan branching protein GlgB. |
cd11350 | AmyAc_4 | 2.14e-64 | 103 | 474 | 6 | 382 | 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. |
PRK05402 | PRK05402 | 1.52e-62 | 15 | 573 | 135 | 721 | 1,4-alpha-glucan branching protein GlgB. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QJU06769.1 | 6.89e-233 | 4 | 575 | 13 | 592 |
QJU05945.1 | 1.38e-232 | 4 | 575 | 13 | 592 |
QCT39943.1 | 1.38e-232 | 4 | 575 | 13 | 592 |
QHU89524.1 | 9.15e-231 | 4 | 575 | 13 | 592 |
QUB37887.1 | 1.00e-216 | 4 | 575 | 9 | 587 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5GR1_A | 2.12e-52 | 3 | 550 | 148 | 739 | Crystalstructure of branching enzyme Y500A/D501A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142],5GR6_A Crystal structure of branching enzyme Y500A/D501A double mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142] |
5GQZ_A | 2.89e-52 | 3 | 550 | 148 | 739 | Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142] |
5GR0_A | 2.89e-52 | 3 | 550 | 148 | 739 | Crystalstructure of branching enzyme D501A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142] |
5GQU_A | 3.95e-52 | 3 | 550 | 148 | 739 | Crystalstructure of branching enzyme from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQV_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltohexaose [Crocosphaera subtropica ATCC 51142],5GQY_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142] |
5GR3_A | 5.40e-52 | 3 | 550 | 148 | 739 | Crystalstructure of branching enzyme L541A/W655A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P95867 | 5.72e-55 | 5 | 466 | 4 | 448 | Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1 |
A1U0K1 | 7.19e-55 | 15 | 576 | 41 | 630 | 1,4-alpha-glucan branching enzyme GlgB OS=Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) OX=351348 GN=glgB PE=3 SV=1 |
Q2JK68 | 1.46e-53 | 15 | 530 | 152 | 698 | 1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-2-3B'a(2-13)) OX=321332 GN=glgB PE=3 SV=1 |
Q608L5 | 1.56e-53 | 14 | 530 | 139 | 671 | 1,4-alpha-glucan branching enzyme GlgB OS=Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) OX=243233 GN=glgB PE=3 SV=1 |
Q2JT08 | 7.61e-53 | 15 | 530 | 152 | 698 | 1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-3-3Ab) OX=321327 GN=glgB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000050 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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