P39371 · NANM_ECOLI
- ProteinN-acetylneuraminate epimerase
- GenenanM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids368 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses (PubMed:18063573).
Forms linear aceneuramate during interconversion of Neu5Ac anomers (PubMed:33895133).
Forms linear aceneuramate during interconversion of Neu5Ac anomers (PubMed:33895133).
Catalytic activity
- N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminateThis reaction proceeds in the forward and the backward directions.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 228 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | protein homodimerization activity | |
Molecular Function | racemase and epimerase activity, acting on carbohydrates and derivatives | |
Biological Process | N-acetylneuraminate catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylneuraminate epimerase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP39371
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30 | No effect on catalytic activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 228 | Great decrease in catalytic activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 234 | Decrease in catalytic activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 297 | No effect on catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 302 | No effect on catalytic activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 328 | No effect on catalytic activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 344 | No effect on catalytic activity. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MNKTITALAIMMASFAANA | ||||||
Chain | PRO_0000016655 | 20-368 | N-acetylneuraminate epimerase | |||
Sequence: SVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKKWTALAAFPGGPRDQATSAFIDGNLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAHYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVSSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSTDIHLWHNGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVTDSVLITVKDNKVTVQN |
Proteomic databases
Expression
Induction
Induced by N-acetylneuraminate and modulated by N-acetylglucosamine, via the NanR and NagC regulators.
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 40-84 | Kelch 1 | ||||
Sequence: TVYIGLGSAGTAWYKLDTQAKDKKWTALAAFPGGPRDQATSAFID | ||||||
Repeat | 86-137 | Kelch 2 | ||||
Sequence: NLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHN | ||||||
Repeat | 139-173 | Kelch 3 | ||||
Sequence: KAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINA | ||||||
Repeat | 174-219 | Kelch 4 | ||||
Sequence: HYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKG | ||||||
Repeat | 222-265 | Kelch 5 | ||||
Sequence: TWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVSSPDGVAGG | ||||||
Repeat | 287-336 | Kelch 6 | ||||
Sequence: ENYQNGKNYAHEGLKKSYSTDIHLWHNGKWDKSGELSQGRAYGVSLPWNN | ||||||
Repeat | 338-367 | Kelch 7 | ||||
Sequence: LLIIGGETAGGKAVTDSVLITVKDNKVTVQ |
Sequence similarities
Belongs to the NanM family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length368
- Mass (Da)39,572
- Last updated2000-05-30 v2
- Checksum1194F392C51EA204
Sequence caution
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U14003 EMBL· GenBank· DDBJ | AAA97206.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC77266.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE78303.1 EMBL· GenBank· DDBJ | Genomic DNA |