A2RAL4
Gene name |
bglA (bgl1, An18g03570) |
Protein name |
Probable beta-glucosidase A |
Names |
Beta-D-glucoside glucohydrolase A, Cellobiase A, Gentiobiase A |
Species |
Aspergillus niger (strain CBS 51388 / FGSC A1513) |
KEGG Pathway |
ang:ANI_1_456164 |
EC number |
3.2.1.21: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
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 A2RAL4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2RAL4-F1 | Predicted | AlphaFoldDB |
No variants for A2RAL4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2RAL4 | |||||
No associated diseases with A2RAL4
4 regional properties for A2RAL4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glycoside hydrolase, family 3, N-terminal | 82 - 338 | IPR001764 |
| domain | Glycoside hydrolase family 3 C-terminal domain | 400 - 654 | IPR002772 |
| active_site | Glycoside hydrolase, family 3, active site | 266 - 283 | IPR019800 |
| domain | Fibronectin type III-like domain | 779 - 847 | IPR026891 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.2.1.21 | Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| beta-glucosidase activity | Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose. |
| glucosidase activity | Catalysis of the hydrolysis of glucosyl compounds, substances containing a group derived from a cyclic form of glucose or a glucose derivative. |
| scopolin beta-glucosidase activity | Catalysis of the reaction: H2O + scopolin <=> beta-D-glucose + scopoletin. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular carbohydrate catabolic process | The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y, as carried out by individual cells. |
| cellulose catabolic process | The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRFTSIEAVA | LTAVSLASAD | ELAYSPPYYP | SPWANGQGDW | AEAYQRAVDI | VSQMTLAEKV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NLTTGTGWEL | ELCVGQTGGV | PRLGIPGMCA | QDSPLGVRDS | DYNSAFPAGV | NVAATWDKNL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AYLRGQAMGQ | EFSDKGADIQ | LGPAAGPLGR | SPDGGRNWEG | FSPDPALSGV | LFAETIKGIQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DAGVVATAKH | YIAYEQEHFR | QAPEAQGYGF | NITESGSANL | DDKTMHELYL | WPFADAIRAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AGAVMCSYNQ | INNSYGCQNS | YTLNKLLKAE | LGFQGFVMSD | WAAHHAGVSG | ALAGLDMSMP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GDVDYDSGTS | YWGTNLTISV | LNGTVPQWRV | DDMAVRIMAA | YYKVGRDRLW | TPPNFSSWTR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DEYGFKYYYV | SEGPYEKVNQ | FVNVQRNHSE | LIRRIGADST | VLLKNDGALP | LTGKERLVAL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IGEDAGSNPY | GANGCSDRGC | DNGTLAMGWG | SGTANFPYLV | TPEQAISNEV | LKNKNGVFTA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TDNWAIDQIE | ALAKTASVSL | VFVNADSGEG | YINVDGNLGD | RRNLTLWRNG | DNVIKAAASN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CNNTIVIIHS | VGPVLVNEWY | DNPNVTAILW | GGLPGQESGN | SLADVLYGRV | NPGAKSPFTW |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GKTREAYQDY | LYTEPNNGNG | APQEDFVEGV | FIDYRGFDKR | NETPIYEFGY | GLSYTTFNYS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NLQVEVLSAP | AYEPASGETE | AAPTFGEVGN | ASDYLYPDGL | QRITKFIYPW | LNSTDLEASS |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GDASYGQDAS | DYLPEGATDG | SAQPILPAGG | GAGGNPRLYD | ELIRVSVTIK | NTGKVAGDEV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PQLYVSLGGP | NEPKIVLRQF | ERITLQPSKE | TQWSTTLTRR | DLANWNVETQ | DWEITSYPKM |
| 850 | |||||
| VFAGSSSRKL | PLRASLPTVH |