Q54NU9
Gene name |
tpsB (DDB_G0284975) |
Protein name |
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] B |
Names |
Trehalose-6-phosphate synthase B, UDP-glucose-glucosephosphate glucosyltransferase B |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0284975 |
EC number |
2.4.1.15: 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 Q54NU9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q54NU9-F1 | Predicted | AlphaFoldDB |
No variants for Q54NU9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q54NU9 | |||||
No associated diseases with Q54NU9
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.15 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) | A protein complex that possesses alpha,alpha-trehalose-phosphate synthase (UDP-forming) and trehalose-phosphatase activities, and thus catalyzes two reactions in trehalose biosynthesis. In the complex identified in Saccharomyces, Tps1p has alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity, Tps2p has trehalose 6-phosphate phosphatase activity; Tps3p is a regulatory subunit, and an additional subunit, Tsl1p, may be present. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity | Catalysis of the reaction: UDP-glucose + D-glucose-6-phosphate = UDP + alpha,alpha-trehalose-6-phosphate. |
| trehalose-phosphatase activity | Catalysis of the reaction: trehalose 6-phosphate + H2O = trehalose + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| trehalose biosynthetic process | The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi. |
| trehalose metabolism in response to stress | The chemical reactions and pathways involving trehalose that occur as a result of a stimulus indicating the organism is under stress. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTIIQRSTSL | NNIINEKLGK | IIVASNTLPI | TVTKFNETPL | FGSPLSASRE | SITSSFGMSE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PSRDRESKIQ | IQINGHPFPT | QSALETLKAK | DEIEDWLWIG | WSHCEVNEDE | EPMLNQAIKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FSPHFEHVFL | NPRQFENYYK | GYCKNGLWLL | LHYQMNFIRM | QSEWWEEYVG | VNQMFAEKIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SVWRPSDIIW | IHDYHLMLVP | QMLRQLLPPE | ASIGFFFHAP | FPSYELFRIL | PNRKELLKGI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSSNLIGFQS | FEYVRHFKSS | CARLLDLEVH | PKGLEIFEDG | STHFTKLQVY | PIGVDYNDFA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KNLNLPEVSS | RVESLRKIFK | GKKVVVARDR | LDQIEGVPRK | LEVFEQLLND | HPEYIGKLVF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IQIYEPTVEE | GDETDEQKIL | HKTVNEMVGR | INGKFGKLSF | NPIEYINKKI | SYEELSALYK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LADIALITPI | RDGMNLTSHE | YVVCQKDNFG | VLILSEFAGA | ARCLGGSIIV | NPFSKKEIME |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AIIEALNMSM | HDRKLKHQIN | YNYVLANTSS | FWGKRFLCDL | NEATQKEIME | TSVPRANFQE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IEDSYKKAKV | RVFFLDYDGT | LTPLVRLPSQ | AMPSKQLIDV | LSKLTEDRRN | EVYVISGRDR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SSLEKWLGHL | PIGMSCEHGV | FTRQPGENQP | WTESPNAEVQ | WKDTVLSIMQ | DFEDRTPGSM |
| 670 | 680 | 690 | 700 | 710 | 720 |
| TETKQVNITW | HYRNADPDFG | QFQAKELIAQ | LRSVANKYPL | DILSGKKAIE | VKPIGINKGE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IVKMILQKID | ADFILCIGDD | KTDEDMFKAL | YNVPSFTIRV | CGDLEESTKA | RGVVESSSEV |
| LTLLNRLSLS |