P31119
Gene name |
aas |
Protein name |
Bifunctional protein Aas |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b2836 |
EC number |
2.3.1.40: Transferring groups other than amino-acyl groups |
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 P31119
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P31119-F1 | Predicted | AlphaFoldDB |
No variants for P31119
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P31119 | |||||
No associated diseases with P31119
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.40 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity | Catalysis of the reaction: acyl- + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| long-chain fatty acid [acyl-carrier-protein] ligase activity | Catalysis of the reaction: ATP + an acid |
| long-chain fatty acid-CoA ligase activity | +Catalysis of the reaction: ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; a long-chain fatty acid is a fatty acid with a chain length between C13 and C22. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid metabolic process | The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| phospholipid biosynthetic process | The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O60488 | ACSL4 | Long-chain-fatty-acid--CoA ligase 4 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLFSFFRNLC | RVLYRVRVTG | DTQALKGERV | LITPNHVSFI | DGILLGLFLP | VRPVFAVYTS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ISQQWYMRWL | KSFIDFVPLD | PTQPMAIKHL | VRLVEQGRPV | VIFPEGRITT | TGSLMKIYDG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AGFVAAKSGA | TVIPVRIEGA | ELTHFSRLKG | LVKRRLFPQI | TLHILPPTQV | AMPDAPRARD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RRKIAGEMLH | QIMMEARMAV | RPRETLYESL | LSAMYRFGAG | KKCVEDVNFT | PDSYRKLLTK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TLFVGRILEK | YSVEGERIGL | MLPNAGISAA | VIFGAIARRR | MPAMMNYTAG | VKGLTSAITA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AEIKTIFTSR | QFLDKGKLWH | LPEQLTQVRW | VYLEDLKADV | TTADKVWIFA | HLLMPRLAQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KQQPEEEALI | LFTSGSEGHP | KGVVHSHKSI | LANVEQIKTI | ADFTTNDRFM | SALPLFHSFG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LTVGLFTPLL | TGAEVFLYPS | PLHYRIVPEL | VYDRSCTVLF | GTSTFLGHYA | RFANPYDFYR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LRYVVAGAEK | LQESTKQLWQ | DKFGLRILEG | YGVTECAPVV | SINVPMAAKP | GTVGRILPGM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DARLLSVPGI | EEGGRLQLKG | PNIMNGYLRV | EKPGVLEVPT | AENVRGEMER | GWYDTGDIVR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FDEQGFVQIQ | GRAKRFAKIA | GEMVSLEMVE | QLALGVSPDK | VHATAIKSDA | SKGEALVLFT |
| 670 | 680 | 690 | 700 | 710 | |
| TDNELTRDKL | QQYAREHGVP | ELAVPRDIRY | LKQMPLLGSG | KPDFVTLKSW | VDEAEQHDE |