P52979
Gene name |
glgB |
Protein name |
1,4-alpha-glucan branching enzyme GlgB |
Names |
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase, Alpha-(1->4)-glucan branching enzyme, Glycogen branching enzyme, BE |
Species |
Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) |
KEGG Pathway |
|
EC number |
2.4.1.18: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P52979
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P52979-F1 | Predicted | AlphaFoldDB |
No variants for P52979
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P52979 | |||||
No associated diseases with P52979
4 regional properties for P52979
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glycoside hydrolase, family 13, N-terminal | 145 - 216 | IPR004193 |
| domain | Glycosyl hydrolase, family 13, catalytic domain | 260 - 629 | IPR006047 |
| domain | Alpha-amylase/branching enzyme, C-terminal all beta | 638 - 732 | IPR006048 |
| domain | Glycogen branching enzyme GlgB, N-terminal Early set domain | 138 - 228 | IPR044143 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.18 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 1,4-alpha-glucan branching enzyme activity | Catalysis of the transfer of a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxyl group in a similar glucan chain. |
| 1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis) | Catalysis of the reaction: a glucosylated glycogenin = a glycogen. |
| cation binding | Binding to a cation, a charged atom or group of atoms with a net positive charge. |
| hydrolase activity, hydrolyzing O-glycosyl compounds | Catalysis of the hydrolysis of any O-glycosyl bond. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glycogen biosynthetic process | The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKKPLNSAEE | KKTGDITKAE | IEAIKSGLHS | NPFQIIPLHE | TPEGFSARCF | IPGAEEVSVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TLDGNFVGEL | KQIDPDGFFE | GRIDLSKRQP | VRYRACRDDA | EWAVTDPYSF | GPVLGPMDDY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FVREGSICGY | STGWARIPLK | LEGVEGFHFA | VWAPNGRRVS | VVGDFNNWDG | RRHVMRFRKD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TGIWEIFAPD | VYACAYKFEI | LGANGELLPL | KADPYARRGE | LRPKNASVTA | PELTQKWEDQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AHREHWAQVD | QRRQPISIYE | VHAGSWQRSE | DGTFLSWDEL | EAQLIPYCTD | MGFTHIEFLP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ITEHPYDPSW | GYQTTGLYAP | TARFGDPEGF | ARFVNGAHKV | GIGVLLDWVP | AHFPTDEHGL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RWFDGTALYE | HADPRQGFHP | DWNTAIYNFG | RIEVMSYLIN | NALYWAEKFH | LDGLRVDAVA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SMLYLDYSRK | EGEWIPNEYG | GRENLESVRF | LQKMNSLVYG | THPGVMTIAE | ESTSWPKVSQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PVHEGGLGFG | FKWNMGFMHD | TLSYFSREPV | HRKFHHQELT | FGLLYAFTEN | FVLPLSHDEV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VHGKGSLIAK | MSGDDWQKFA | NLRSYYGFMW | GYPGKKLLFM | GQEFAQWSEW | SEKGSLDWNL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RQYPMHEGMR | RLVRDLNLTY | RSKAALHARD | CEPDGFRWLV | VDDHENSVFA | WLRTAPGEKP |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VAVICNLTPV | YRENYYVPLG | VAGRWREILN | TDAEIYGGSG | KGNGGRVQAV | DAGGEIGAML |
| 730 | |||||
| VLPPLATIML | EPEN |