Domains within Escherichia coli UMN026 protein AAS_ECOLU (B7N768)
Bifunctional protein Aas
Alternative representations: 1 /
| Protein length | 719 aa |
|---|---|
| Source database | UniProt |
| Identifiers | A0A135PSI5_ECOLX, A0A135PSI5, U9ZH05_ECOLX, U9ZH05, D7X6N5_ECOLX, D7X6N5, AAS_ECOLU, B7N768 |
Domain architecture analysis
Display all proteins with similar:
| Domain organisation | Proteins having all the domains as the query in the same order. Additional domains are allowed. |
|---|---|
| Domain composition | Proteins with the same domain composition have at least one copy of each of the domains of the query. |
This domain architecture was probably invented with the emergence of cellular organisms
Predicted functional partners
AAS_ECOLU is shown as 
aas in the network
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The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.
Protein AAS_ECOLU is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
KEGG pathways
| Pathway | Description | |
|---|---|---|
| map00071 | Fatty acid degradation | iPath3 |
| map00564 | Glycerophospholipid metabolism | iPath3 |
KEGG orthologous groups
| KO | Name | Description | |
|---|---|---|---|
| K00655 | plsC | 1-acyl-sn-glycerol-3-phosphate acyltransferase [EC:2.3.1.51] | iPath3 |
| K08227 | lplT | MFS transporter, LPLT family, lysophospholipid transporter | |
| K05939 | aas | acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20] | |
| K01897 | ACSL, fadD | long-chain-fatty-acid---CoA ligase [EC:6.2.1.3] | iPath3 |
Orthologous groups
Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 585056.ECUMN_3163 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG0204 | All organisms (root) | 1-acyl-sn-glycerol-3-phosphate acyltransferase [EC:2.3.1.51],lysophosphatidylcholine acyltransferase / lyso-PAF acetyltransferase [EC:2.3.1.23 2.3.1.67],lysophosphatidate acyltransferase [EC:2.3.1.51] |
| LCOG0318 | All organisms (root) | long-chain acyl-CoA synthetase [EC:6.2.1.3],fatty-acyl-CoA synthase [EC:6.2.1.-],4-coumarate--CoA ligase [EC:6.2.1.12] |
| COG0318 | Bacteria (superkingdom) | long-chain acyl-CoA synthetase [EC:6.2.1.3],fatty-acyl-CoA synthase [EC:6.2.1.-],o-succinylbenzoate---CoA ligase [EC:6.2.1.26] |
| COG0204 | Bacteria (superkingdom) | 1-acyl-sn-glycerol-3-phosphate acyltransferase [EC:2.3.1.51],lyso-ornithine lipid O-acyltransferase [EC:2.3.1.270],acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20] |
| 633R2 | Proteobacteria (phylum) | MFS transporter, LPLT family, lysophospholipid transporter,acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72] |
| ER2BD | Gammaproteobacteria (class) | acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20],MFS transporter, LPLT family, lysophospholipid transporter |
| AUHND | Enterobacterales (order) | acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20] |
| 7FJ16 | Enterobacteriaceae (family) | acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20] |
| GBR3J | Escherichia coli (species) | acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20] |
The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.