| IED ID | IndEnz0002005033 |
| Enzyme Type ID | protease005033 |
| Protein Name |
3-deoxy-D-manno-octulosonic acid transferase Kdo transferase EC 2.4.99.12 EC 2.4.99.13 Bifunctional Kdo transferase Kdo-lipid IV A 3-deoxy-D-manno-octulosonic acid transferase Lipid IV A 3-deoxy-D-manno-octulosonic acid transferase |
| Gene Name | waaA kdtA b3633 JW3608 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGETLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNKVDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLIAAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATSTHEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTSTQVVVGDTMGELMLLYGIADLAFVGGSLVERGGHNPLEAAAHAIPVLMGPHTFNFKDICARLEQASGLITVTDATTLAKEVSSLLTDADYRSFYGRHAVEVLYQNQGALQRLLQLLEPYLPPKTH |
| Enzyme Length | 425 |
| Uniprot Accession Number | P0AC75 |
| Absorption | |
| Active Site | ACT_SITE 60; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Catalytic activity is inhibited by the antibiotic polymixin B and by Re endotoxin. {ECO:0000269|PubMed:1577828}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}; CATALYTIC ACTIVITY: Reaction=alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28062, ChEBI:CHEBI:15378, ChEBI:CHEBI:60364, ChEBI:CHEBI:60365, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.13; Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}; |
| DNA Binding | |
| EC Number | 2.4.99.12; 2.4.99.13 |
| Enzyme Function | FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:1577828}; |
| Pathway | PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step 1/4. {ECO:0000269|PubMed:1577828}.; PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step 2/4. {ECO:0000269|PubMed:1577828}.; PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis. {ECO:0000269|PubMed:1577828}. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Region (3); Site (2); Transmembrane (1) |
| Keywords | Cell inner membrane;Cell membrane;Lipopolysaccharide biosynthesis;Membrane;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:1577828}; Single-pass membrane protein {ECO:0000305|PubMed:1577828}; Cytoplasmic side {ECO:0000305|PubMed:1577828}. |
| Modified Residue | |
| Post Translational Modification | PTM: Degraded by the protease FtsH; therefore FtsH regulates the addition of the sugar moiety to the LPS and thus the maturation of the LPS precursor. {ECO:0000269|PubMed:18776015}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15690043; 20706981; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,291 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52 uM for lipid IV(A) (at pH 8) {ECO:0000269|PubMed:1577828}; KM=88 uM for CMP-Kdo (at pH 8) {ECO:0000269|PubMed:1577828}; Vmax=18 umol/min/mg enzyme (at pH 8) {ECO:0000269|PubMed:1577828}; |
| Metal Binding | |
| Rhea ID | RHEA:28066; RHEA:28062 |
| Cross Reference Brenda | 2.4.99.12;2.4.99.13; |