A6VP15
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 |
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z) |
KEGG Pathway |
asu:Asuc_1352 |
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 A6VP15
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6VP15-F1 | Predicted | AlphaFoldDB |
No variants for A6VP15
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6VP15 | |||||
No associated diseases with A6VP15
4 regional properties for A6VP15
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glycoside hydrolase, family 13, N-terminal | 135 - 209 | IPR004193 |
| domain | Glycosyl hydrolase, family 13, catalytic domain | 253 - 604 | IPR006047 |
| domain | Alpha-amylase/branching enzyme, C-terminal all beta | 632 - 726 | IPR006048 |
| domain | Glycogen branching enzyme GlgB, N-terminal Early set domain | 120 - 224 | 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 |
| MTTFVTQDTI | NAFFDGRHAD | PFAVLGMHET | DNGIEIRALL | PDAGRVVVID | KETQDEVCEL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SRIDERGFFA | GIMPQRNSFF | NYQLQVSWGN | EVLRIEDPYR | FHPMIQELDN | WLLAEGSHLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PYEVLGAHFM | ECDHVSGVNF | RLWAPNAKRV | SVVGDFNYWD | GRRHPMRFHQ | ASGVWELFIP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KVALGDLYKF | ELLDNNNRLR | LKSDPYAFAA | QLRPDTASQI | SVLPEIQEMT | AARRKANQLD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QPISIYEVHL | GSWRRNLANN | FWLNYDEIAD | ELIPYVKEMG | FTHIELLPIS | EFPFDGSWGY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QPIGLYAPTS | RFGSPEGFKR | FVDKAHAAGI | NVILDWVPGH | FPSDTHGLAT | FDGTALYEHA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DPKEGYHQDW | NTLIYNYGRH | EVKNYLSGNA | LYWVERFGLD | GIRVDAVASM | IYRDYSRRDG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EWIPNQYGGR | ENLEAIEFLK | HTNYILGTEH | PGVMCVAEES | TAFAGVTLPP | ENGGLGFNFK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WNMGWMNDTL | SYMKLDPIYR | QYNHSKLTFG | MLYQYSENFV | LPLSHDEVVH | GKCSLLDKMP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GDTWQKFANL | RAYYGYMWAY | PGKKLLFMGN | EFAQGREWNY | QESLDWYLLD | EFHGGGWHSG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VQRLVKDLNK | TYQKQSALYQ | LDTKPEGFEW | LVVDDAQNSV | FVFERRNAKG | EPLIVVSNFT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PVPRENYRFG | VNVAGSYEEI | LNTDADIYKG | SGLNNGGVID | SEEIESHGKT | QSISITVPPL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ATVYFKLKSA | RKVASPRKVT | KKKTTADGAE | ATAKNASASK | ATKVSTKKTV | KSSEAKPVKA |
| 790 | 800 | 810 | 820 | ||
| ATKSSVTKVA | TKKSTDKPTA | KATRTKKATV | TKTAKASAKT | TAKKTKDNA |