IED ID | IndEnz0005000366 |
Enzyme Type ID | lipase000366 |
Protein Name |
N-acylneuraminate cytidylyltransferase EC 2.7.7.43 CMP-N-acetylneuraminic acid synthase CMP-NeuNAc synthase |
Gene Name | neuA |
Organism | Escherichia coli |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli |
Enzyme Sequence | MRTKIIAIIPARSGSKGLRNKNALMLIDKPLLAYTIEAALQSEMFEKVIVTTDSEQYGAIAESYGADFLLRPEELATDKASSFEFIKHALSIYTDYESFALLQPTSPFRDSTHIIEAVKLYQTLEKYQCVVSVTRSNKPSQIIRPLDDYSTLSFFDLDYSKYNRNSIVEYHPNGAIFIANKQHYLHTKHFFGRYSLAYIMDKESSLDIDDRMDFELAITIQQKKNRQKIDLYQNIHNRINEKRNEFDSVSDITLIGHSLFDYWDVKKINDIEVNNLGIAGINSKEYYEYIIEKELIVNFGEFVFIFFGTNDIVVSDWKKEDTLWYLKKTCQYIKKKNAASKIYLLSVPPVFGRIDRDNRIINDLNSYLRENVDFAKFISLDHVLKDSYGNLNKMYTYDGLHFNSNGYTVLENEIAEIVK |
Enzyme Length | 419 |
Uniprot Accession Number | P13266 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by the CTP analogs 5-mercuri-CTP and CTP-2',3'-dialdehyde. {ECO:0000269|PubMed:2826425}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate + diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43; Evidence={ECO:0000269|PubMed:2826425}; |
DNA Binding | |
EC Number | 2.7.7.43 |
Enzyme Function | FUNCTION: Catalyzes the formation of CMP-N-acetylneuraminic acid (CMP-NeuNAc), which is essential for the formation of the capsule. {ECO:0000269|PubMed:2826425}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0-10.0. {ECO:0000269|PubMed:2826425}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1) |
Keywords | Capsule biogenesis/degradation;Cytoplasm;Direct protein sequencing;Magnesium;Manganese;Nucleotidyltransferase;Transferase |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2826425}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 48,736 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 mM for NeuNAc (at pH 9.0) {ECO:0000269|PubMed:2826425}; KM=0.31 mM for CTP (at pH 9.0) {ECO:0000269|PubMed:2826425}; |
Metal Binding | |
Rhea ID | RHEA:11344 |
Cross Reference Brenda |