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CAZyme Information: MGYG000001812_00509

You are here: Home > Sequence: MGYG000001812_00509

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
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; ;
CAZyme ID MGYG000001812_00509
CAZy Family GH13
CAZyme Description Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1482 165515.58 6.1449
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001812 3064175 MAG Denmark Europe
Gene Location Start: 23793;  End: 28241  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001812_00509.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH133 1049 1426 2.1e-92 0.978494623655914
GH13 180 379 2.3e-34 0.9047619047619048

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06202 GDE_C 1.21e-74 1044 1427 5 374
Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
cd11313 AmyAc_arch_bac_AmyA 5.47e-50 128 496 6 336
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. 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.
COG3408 GDB1 4.55e-34 935 1420 156 594
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551 AmyAc_family 6.86e-26 172 444 22 247
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.
pfam12439 GDE_N 2.56e-23 794 1003 19 209
Glycogen debranching enzyme N terminal. This domain family is found in bacteria and archaea, and is typically between 218 and 229 amino acids in length. The family is found in association with pfam06202. Glycogen debranching enzyme catalyzes the debranching of amylopectin in glycogen. This is done by transferring three glucose subunits of glycogen from one parallel chain to another. This has the effect of enabling the glucose residues to become more accessible for glycolysis.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQV01271.1 0.0 2 1432 5 1432
AOY59008.1 0.0 2 1432 5 1432
ABC78593.1 0.0 4 1432 5 1420
CBX27385.1 0.0 6 1432 9 1428
ABW66661.1 0.0 4 1432 14 1431

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4U33_A 1.32e-14 169 530 273 651
Structureof Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_B Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_C Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_D Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_E Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U33_F Structure of Mtb GlgE bound to maltose [Mycobacterium tuberculosis CDC1551],4U3C_A Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_B Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_C Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_D Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_E Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551],4U3C_F Docking Site of Maltohexaose in the Mtb GlgE [Mycobacterium tuberculosis CDC1551]
5CGM_A 5.02e-14 169 561 248 662
Structureof Mycobacterium thermoresistibile GlgE in complex with maltose at 1.95A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CGM_B Structure of Mycobacterium thermoresistibile GlgE in complex with maltose at 1.95A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CIM_A Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CIM_B Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CJ5_A Structure of Mycobacterium thermoresistibile GlgE APO form at 3.13A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CJ5_B Structure of Mycobacterium thermoresistibile GlgE APO form at 3.13A resolution [Mycolicibacterium thermoresistibile ATCC 19527]
1WZA_A 6.19e-12 158 339 14 206
Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
1CYG_A 6.02e-11 237 578 111 482
CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
5H2T_A 2.15e-10 171 359 44 259
Structureof trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_B Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_C Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_D Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_E Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_F Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_G Structure of trehalose synthase [Thermomonospora curvata DSM 43183],5H2T_H Structure of trehalose synthase [Thermomonospora curvata DSM 43183]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q3J3M8 1.38e-24 172 560 230 638
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) OX=272943 GN=glgE PE=3 SV=3
Q9JN46 3.71e-23 172 530 212 585
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q2RTZ1 4.20e-23 172 568 255 671
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE PE=3 SV=1
Q63T93 4.83e-17 172 530 676 1050
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q1D651 1.58e-16 173 530 222 594
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1

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
1.000057 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001812_00509.