P54960
Gene name |
|
Protein name |
3-hydroxy-3-methylglutaryl-coenzyme A reductase |
Names |
HMG-CoA reductase |
Species |
Blattella germanica (German cockroach) (Blatta germanica) |
KEGG Pathway |
|
EC number |
1.1.1.34: With NAD(+) or NADP(+) as acceptor |
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 P54960
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P54960-F1 | Predicted | AlphaFoldDB |
No variants for P54960
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P54960 | |||||
No associated diseases with P54960
4 regional properties for P54960
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Sterol-sensing domain | 59 - 218 | IPR000731 |
| conserved_site | Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site | 614 - 628 | IPR023076-1 |
| conserved_site | Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site | 770 - 777 | IPR023076-2 |
| conserved_site | Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site | 824 - 837 | IPR023076-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.34 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| hydroxymethylglutaryl-CoA reductase (NADPH) activity | Catalysis of the reaction: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| coenzyme A metabolic process | The chemical reactions and pathways involving coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester. |
| isoprenoid biosynthetic process | The chemical reactions and pathways resulting in the formation of an isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVGRLFRAHG | QFCASHPWEV | IVATLTLTVC | MLTVDQRPLG | LPPGWGHNCI | TLEEYNAADM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IVMTLIRCVA | VLYSYYQFCH | LQKLGSKYIL | GIAGLFTVFS | SFVFSSSVIN | FLGSDVSDLK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DALFFFLLLI | DLSKATVLAQ | FALSSRSQDE | VKHNIARGIA | MLGPTITLDT | VVETLVIGVG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MLSGVRRLEV | LCCFACMSVI | VNYVVFMTFY | PACLSLILEL | SRSGESGRPA | WHDKSLIIKA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LHEEDQKPNP | VVQRVKVIMS | AGLMLVHAHR | WVRCLSIALW | PDLTSLRYFC | THCDTGVSYS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RWSFASEGEE | LPTVKLVTGD | SVVNSNSTDD | AQLHYYIMRW | LTVSADHIVI | LILLLALAVK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FVFFETRDEL | TTTRGMDGWV | EVSSPVEHKY | VQTEQPSCSA | PEQPLEEPPA | SNRSIDECLS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VCKSDVGAQA | LSDCEVMALV | TSGHIAGYQL | EKVVRNPERG | VGIRRQILTK | TADLKDALDN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LPYKNYDYLK | VMGACCENVI | GYMPVPVGVA | GPLNLDGRLV | HVPLATTEGC | LVASTNRGMR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALMRCGVTSR | IVADGMTRGP | VVRFPNIDRA | SEAMLWMQVP | YNFEQIKKNF | DSTSRFARLS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KIHIRVAGRH | LFIRFIATTG | DAMGMNMLSK | GTEVALAYVQ | QVYPDMEILS | LSGNFCTDKK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PAAVNWIEGR | GKSVVCEAIV | PADIIKSVLK | TSVQALMDVN | ITKNLIGSAV | AGSIGGFNAH |
| 730 | 740 | 750 | 760 | 770 | 780 |
| AANIVTAIFI | ATGQDPAQNV | GSSNCMTLME | PWGEDGKDLY | VSCTMPSIEI | GTIGGGTVLP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PQAACLDMLG | VRGANEMCPG | ENANTLARIV | CGTVLAGELS | LMSALAAGHL | VKSHMRHNRS |
| 850 | |||||
| SVSTSGSEPS | TPACKS |