Q816G6
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 |
Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) |
KEGG Pathway |
bce:BC4867 |
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 Q816G6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q816G6-F1 | Predicted | AlphaFoldDB |
No variants for Q816G6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q816G6 | |||||
No associated diseases with Q816G6
5 regional properties for Q816G6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Alpha-D-phosphohexomutase, C-terminal | 373 - 443 | IPR005843 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain I | 3 - 136 | IPR005844 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain II | 166 - 253 | IPR005845 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain III | 257 - 365 | IPR005846 |
| conserved_site | Alpha-D-phosphohexomutase, conserved site | 95 - 104 | IPR016066 |
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 | |
2 GO annotations of 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| 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 |
| MNVINCEEVK | RDEFHTEKYY | ESYNIFGAHV | VTEDEIQGVR | FTVWAPHAKA | MSVVGDFNEW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DYEQHKMLQV | TEEGIWSLFI | PHIEEGEIYK | YAIETLAGDV | ILKADPYAVY | AEVRPNTASV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VFDIKGYEWN | DKNWNRKKKK | KSIYKEAMTV | YELHFGSWKK | KEDGTLYSYR | EMVEELIPYV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VEHQFTHIEI | MPLVEHPYDR | SWGYQGTGYY | AATSRFGTPH | DLMHFVDECH | KYGIGVILDW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VPGHFCKDAH | GLYLFDGTPT | YEYKDKDVQE | NPVWGTVNFD | LGKREVRNFL | ISNALFWMRY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FHIDGFRVDA | VANMLYWNKE | GQEQSNEHAV | SFLRELNEAV | FAEDEDFLMT | AEDSTAWPLV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TTPTYEGGLG | FNYKWNMGWM | NDVLKYMECA | PEYRKHIHEK | MTFSLLYAYS | ENFILPLSHD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EVVHGKKSLL | NKMPGDYWDK | FAQLRLLYGY | FFTHPGKKLL | FMGGEFGQFD | EWKDLEDLDW |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NLHDFEMHRY | MHDYFKELIA | LYKRSKPLWQ | LDHSPEGFQW | IDANNNEQSI | FSFIRQGDKQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EDALVIVCNF | TKATYENYKV | GVPDFEYYNE | ILNSDAQQYG | GSGQVNKKRL | KTILEPYHNQ |
| 610 | 620 | 630 | 640 | ||
| AAHVEITIPP | FGVSILRPVK | TRKGSKKQDG | SKTKVRSNVT | SRGKR |