P0A759 · NAGB_ECOLI
- ProteinGlucosamine-6-phosphate deaminase
- GenenagB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids266 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Miscellaneous
Disulfide bonds seem not to be essential for the stability of the oligomer under physiological conditions.
Catalytic activity
- alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4+
Activity regulation
Allosterically activated by N-acetylglucosamine 6-phosphate (GlcNAc6P). Competitively inhibited by 2-amino-2-deoxy-D-glucitol-6-phosphate (GlcN-ol-6P).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.5 mM | GlcN6P |
Pathway
Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 72 | Proton acceptor; for enolization step | ||||
Sequence: D | ||||||
Active site | 141 | For ring-opening step | ||||
Sequence: D | ||||||
Active site | 143 | Proton acceptor; for ring-opening step | ||||
Sequence: H | ||||||
Active site | 148 | For ring-opening step | ||||
Sequence: E | ||||||
Site | 151 | Part of the allosteric site | ||||
Sequence: S | ||||||
Site | 158 | Part of the allosteric site | ||||
Sequence: R | ||||||
Site | 160 | Part of the allosteric site | ||||
Sequence: K | ||||||
Site | 161 | Part of the allosteric site | ||||
Sequence: T | ||||||
Site | 254 | Part of the allosteric site | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | glucosamine-6-phosphate deaminase activity | |
Molecular Function | identical protein binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | glucosamine catabolic process | |
Biological Process | N-acetylglucosamine catabolic process | |
Biological Process | N-acetylneuraminate catabolic process | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlucosamine-6-phosphate deaminase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A759
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 118 | 50% of wild-type activity, but 2-fold decrease in substrate affinity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 141 | Large decrease in activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 143 | Loss of activity for the deamination reaction but not for the reverse reaction; complete loss of the homotropic cooperativity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 148 | Large decrease in activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 174 | Loss of activity in the absence of the allosteric activator. | ||||
Sequence: F → A | ||||||
Mutagenesis | 239 | 50% of wild-type activity, but 2-fold decrease in substrate affinity; decrease in allosteric interaction energy. | ||||
Sequence: C → S |
Chemistry
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000160143 | 1-266 | Glucosamine-6-phosphate deaminase | |||
Sequence: MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQVSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCDEPSTMELKVKTLRYFNELEAENIKGL | ||||||
Disulfide bond | 219 | Interchain | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length266
- Mass (Da)29,774
- Last updated2005-06-07 v1
- ChecksumD1443A40E74AC08E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 70 | in Ref. 2; AAC09324 | ||||
Sequence: N → NM | ||||||
Sequence conflict | 91 | in Ref. 2; AAC09324 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M19284 EMBL· GenBank· DDBJ | AAA24191.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF052007 EMBL· GenBank· DDBJ | AAC09324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73772.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA35321.1 EMBL· GenBank· DDBJ | Genomic DNA |