P53536
Gene name |
PHO1 |
Protein name |
Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic |
Names |
Starch phosphorylase L |
Species |
Vicia faba (Broad bean) (Faba vulgaris) |
KEGG Pathway |
|
EC number |
2.4.1.1: 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 P53536
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P53536-F1 | Predicted | AlphaFoldDB |
No variants for P53536
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P53536 | |||||
No associated diseases with P53536
1 regional properties for P53536
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Phosphorylase pyridoxal-phosphate attachment site | 841 - 853 | IPR035090 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.1 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| amyloplast | A plastid whose main function is to synthesize and store starch. |
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| glycogen phosphorylase activity | Catalysis of the reaction: glycogen + phosphate = maltodextrin + alpha-D-glucose 1-phosphate. |
| linear malto-oligosaccharide phosphorylase activity | Catalysis of the reaction: hydrogenphosphate + a linear malto-oligosaccharide = alpha-D-glucose 1-phosphate + a linear malto-oligosaccharide. |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
| SHG alpha-glucan phosphorylase activity | Catalysis of the reaction: hydrogenphosphate + a plant soluble heteroglycan = alpha-D-glucose 1-phosphate + a plant soluble heteroglycan. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASMTMRFHP | NSTAVTESVP | RRGSVYGFIG | YRSSSLFVRT | NVIKYRSVKR | NLEFRRRSAF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SVKCGSGNEA | KQKVKDQEVQ | QEAKTSPSSF | APDTTSIVSS | IKYHAEFTPL | FSPEKFELPQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AFIATAQSVR | DALIINWNAT | YDYYEKLNVK | QAYYLSMEFL | QGRALLNAIG | NLELTGPYAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ALSQLSYKLE | DVAHQEPDAA | LGNGGLGRLA | SCFLDSLATL | NYPAWGYGLR | YKYGLFKQRI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TKDGQEEVAE | DWLEMGNPWE | IVRNDVSYPV | RFYGKVVSGS | DGKKHWVGGE | DIKAVAHDVP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IPGYKTRSTI | NLRLWSTKAA | SEEFDLNAFN | SGRHTEASEA | LANAEKICYI | LYPGDESIEG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KTLRLKQQYT | LCSASLQDII | ARFERRSGAS | VNWEDFPEKV | AVQMNDTHPT | LCIPELMRIL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IDIKGLSWKD | AWNITQRTVA | YTNHTVLPEA | LEKWSMDLME | KLLPRHVEII | EMIDEELIRT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IIAEYGTADS | DLLDKKLKEM | RILENVELPA | EFADILVKTK | EATDISSEEV | QISKEGGEEE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ETSKEGGEEE | EEKEVGGGRE | EGDDGKEDEV | EKAIAEKDGT | VKSSIGDKKK | KLPEPVPVPP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KLVRMANLCV | VGGHAVNGVA | EIHSEIVKDD | VFNAFYKLWP | EKFQNKTNGV | TPRRWIRFCN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PDLSKIITQW | IGTEDWILNT | EKLAELRKFA | DNEDLQTQWR | EAKRNNKVKV | AAFLRERTGY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SVSPDSMFDI | QVKRIHEYKR | QLLNIFGIVY | RYKKMKEMNA | AERKENFVPR | VCIFGGKAFA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TYVQAKRIVK | FITDVGATVN | HDPEIGDLLK | VIFVPDYNVS | VAEMLIPASE | LSQHISTAGM |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EASGTSNMKF | AMNGCLQIGT | LDGANVEIRE | EVGADNFFLF | GAKAREIVGL | RKERARGKFV |
| 910 | 920 | 930 | 940 | 950 | 960 |
| PDPRFEEVKK | FVRSGVFGSY | NYDELIGSLE | GNEGFGRADY | FLVGQDFPSY | LECQEEVDKA |
| 970 | 980 | 990 | 1000 | ||
| YRDQKKWTRM | SILNTAGSSK | FSSDRTIHEY | AREIWNIEPV | KLE |