Alternative representations: 1 /
| Protein length | 1779 aa |
|---|---|
| Source database | UniProt |
| Identifiers | A1TTJ2_ACIAC, A1TTJ2 |
| 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. |
A1TTJ2_ACIAC is shown as
Aave_3733 in the network
Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.
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 A1TTJ2_ACIAC is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
| Pathway | Description | |
|---|---|---|
| map01053 | Biosynthesis of siderophore group nonribosomal peptides | iPath3 |
| map00071 | Fatty acid degradation | iPath3 |
| KO | Name | Description | |
|---|---|---|---|
| K04780 | dhbF | glyine---[glycyl-carrier protein] ligase [EC:6.2.1.66] | |
| K08227 | lplT | MFS transporter, LPLT family, lysophospholipid transporter | |
| K03367 | dltA | D-alanine--poly(phosphoribitol) ligase subunit 1 [EC:6.1.1.13] | |
| K01897 | ACSL, fadD | long-chain-fatty-acid---CoA ligase [EC:6.2.1.3] | iPath3 |
| K00635 | tgs, wax-dgat | diacylglycerol O-acyltransferase / wax synthase [EC:2.3.1.20 2.3.1.75] | iPath3 |
| K12444 | ppsE | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292] |
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 397945.Aave_3733 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| 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] |
| LCOG1020 | All organisms (root) | D-alanine--poly(phosphoribitol) ligase subunit 1 [EC:6.1.1.13],acyl-CoA synthetase [EC:6.2.1.-],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72] |
| LCOG4908 | All organisms (root) | diacylglycerol O-acyltransferase / wax synthase [EC:2.3.1.20 2.3.1.75],phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase [EC:2.3.1.282],mxaD protein |
| 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] |
| COG4908 | Bacteria (superkingdom) | diacylglycerol O-acyltransferase / wax synthase [EC:2.3.1.20 2.3.1.75],phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase [EC:2.3.1.282],mxaD protein |
| COG1020 | Bacteria (superkingdom) | D-alanine--poly(phosphoribitol) ligase subunit 1 [EC:6.1.1.13],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72],mycolipenoyl-CoA---2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase / long-chain-acyl-CoA---trehalose acyltransferase [EC:2.3.1.278 2.3.1.279] |
| 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] |
| 8VCRG | Betaproteobacteria (class) | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292],phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase C [EC:2.3.1.292],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72] |
| GI7UW | Burkholderiales (order) | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72],L-cysteine---[L-cysteinyl-carrier protein] ligase PchF [EC:6.2.1.69] |
| BI47U | Comamonadaceae (family) | glyine---[glycyl-carrier protein] ligase [EC:6.2.1.66] |
| GW152 | Acidovorax (genus) | AMP-binding,PP-binding,Condensation |
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.