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CAZyme Information: MGYG000002109_00150
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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 | UBA1232 sp900544815 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; UBA1232; UBA1232 sp900544815 | |||||||||||
| CAZyme ID | MGYG000002109_00150 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | 1,4-alpha-glucan branching enzyme GlgB | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 159421; End: 161400 Strand: + | |||||||||||
Full Sequence Download help
| MIYDNDEYLL PYKREIDRRL ERFLIKRGEL AGYNGKLTHA ANNHLYYGIH RDKNGYWFRE | 60 |
| FAPAAKGLVL VGDFNDWLPD KNYLAHTEWS FTNIGGGNWE LFVPVEKIKE EDLFKWMVQF | 120 |
| STGEWGERIP AYATTCVQDR QTKLFSAQID FSKREYEWKH KFSRKITSPL IYEVHIGMSS | 180 |
| EQETVSTFNE FRENVLPRVI EDGYNVLQIM ALQEHPYYGS FGYQVSNFFA LSSRFGTPAE | 240 |
| FKNLVDEAHA HGIAVVMDLV HSHAVKNDLE GLSTIDGSRD LYFHSGAAGD HPAWGTRCFN | 300 |
| YGKEETIRFL LSNCKFWLQE YHLDGFRFDG ITSMLYKDHG LERNFTGYND YFTSNTDTDA | 360 |
| YTYLSLANSL IKEIKPHAIT IAEDMSGMPG LAAPVAEGGT GFDYRLAMGV PDHWIKWIKE | 420 |
| LPDECWNVGE MWYQLTNKRA DEKTISYAES HDQALVGDKT IIFRLLDSLM YTEMEKSSTD | 480 |
| MRIDRGVALH KMIRLVTLAT CGGGYLTFMG NEFGHPEWID FPRQGNGWSY KYATRKWSLA | 540 |
| DNNLLRYSSL LQFEKNMIKL FKENDILKYR PVSIYNDVEK QVMAFKRGDY IFVFNFSPLK | 600 |
| SYTDYTLYGI KDGDYRVVLD TDWKEFGGFE RNNRDFKYKV SNGKFEIYVP SRCGLVYKM | 659 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 220 | 511 | 3.1e-143 | 0.9965870307167235 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11321 | AmyAc_bac_euk_BE | 0.0 | 156 | 555 | 5 | 406 | Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. |
| PLN02447 | PLN02447 | 0.0 | 1 | 657 | 61 | 728 | 1,4-alpha-glucan-branching enzyme |
| PLN02960 | PLN02960 | 2.42e-163 | 115 | 659 | 339 | 891 | alpha-amylase |
| PLN03244 | PLN03244 | 9.08e-135 | 115 | 659 | 344 | 866 | alpha-amylase; Provisional |
| COG0296 | GlgB | 7.84e-103 | 36 | 659 | 12 | 628 | 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGY53206.1 | 1.80e-291 | 2 | 658 | 6 | 657 |
| ACM90989.1 | 4.38e-271 | 2 | 658 | 4 | 663 |
| AZS28218.1 | 8.72e-260 | 2 | 658 | 5 | 658 |
| ADY31393.1 | 6.63e-259 | 5 | 659 | 8 | 659 |
| SNV25929.1 | 6.63e-259 | 5 | 659 | 8 | 659 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4BZY_A | 1.90e-193 | 6 | 656 | 35 | 694 | Crystalstructure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens] |
| 5CLT_A | 4.05e-192 | 9 | 656 | 6 | 662 | Crystalstructure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens] |
| 3AMK_A | 3.67e-185 | 2 | 641 | 13 | 659 | Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group] |
| 7ML5_A | 7.10e-185 | 2 | 641 | 12 | 658 | ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group] |
| 3VU2_A | 1.04e-184 | 2 | 641 | 13 | 659 | Structureof the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group],3VU2_B Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q6CCT1 | 4.77e-199 | 5 | 657 | 8 | 682 | 1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1 |
| Q6T308 | 4.98e-198 | 6 | 656 | 32 | 691 | 1,4-alpha-glucan-branching enzyme OS=Felis catus OX=9685 GN=GBE1 PE=2 SV=1 |
| Q6EAS5 | 5.17e-195 | 6 | 656 | 32 | 691 | 1,4-alpha-glucan-branching enzyme OS=Equus caballus OX=9796 GN=GBE1 PE=1 SV=1 |
| Q555Q9 | 2.09e-194 | 2 | 658 | 13 | 675 | 1,4-alpha-glucan-branching enzyme OS=Dictyostelium discoideum OX=44689 GN=glgB PE=3 SV=1 |
| Q04446 | 3.67e-193 | 6 | 656 | 35 | 694 | 1,4-alpha-glucan-branching enzyme OS=Homo sapiens OX=9606 GN=GBE1 PE=1 SV=3 |
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 |
|---|---|---|---|---|---|
| 1.000081 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |