F1RQM2 · AGM1_PIG
- ProteinPhosphoacetylglucosamine mutase
- GenePGM3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids542 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
Catalytic activity
- N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Activity regulation
Inhibited by Mn2+, Cd2+, Zn2+, Cu2+ and Be2+.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.29 mM | D-glucosamine 1-phosphate | |||||
0.39 mM | D-glucose 1-phosphate | |||||
0.018 mM | fructose 1,6-diphosphate | |||||
0.016 mM | galactose 1,6-diphosphate | |||||
0.005 mM | mannose 1,6-diphosphate | |||||
0.002 mM | glucose 1,6-diphosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
39.4 μmol/min/mg | for D-glucosamine 1-phosphate | ||||
28.9 μmol/min/mg | for D-glucose 1-phosphate | ||||
10.1 μmol/min/mg | for fructose 1,6-diphosphate | ||||
14.3 μmol/min/mg | for galactose 1,6-diphosphate | ||||
26.7 μmol/min/mg | for mannose 1,6-diphosphate | ||||
34.4 μmol/min/mg | for glucose 1,6-diphosphate |
pH Dependence
Optimum pH is 7-7.5.
Pathway
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 64 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 64 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 276 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 278 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 280 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 370-372 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 496-500 | substrate | ||||
Sequence: RPSGT | ||||||
Binding site | 505 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoacetylglucosamine mutase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | hemopoiesis | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoacetylglucosamine mutase
- EC number
- Short namesPAGM ; PGlcNAc mutase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionF1RQM2
Proteomes
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000431296 | 1-542 | Phosphoacetylglucosamine mutase | |||
Sequence: MDLDAITKHSASHAKPDGLILQYGTAGFRTKADRLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEDDNGVKLVDPLGEMLAPSWEEHATHLANAEEQDLARALVAISEEAAVNLHQDAFVVIGRDTRPSSEKLSESVIDGVTVLGGQFHDYGLLTTPQLHYMVCCRNTGGQYGEATIDGYYHKLSTAFVELSKQASCSGDDHRTLKVDCANGIGALKLKEMKHYLPQGLSVQLFNDGTKGKLNHFCGADFVKSHQKPPEGIEMKANERCCSFDGDADRIIYYYCDVDGHFHLIDGDKIATLISSFLKELLLEIGESLTVGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDLGVYFEANGHGTVLFSKAAEAKIRQLAKELEDKKGKAAKMLENVIDLFNQATGDAISDMLVIEAILALKGLTIQQWDALYTDLPNRQLKVKVADRQVISTTDAERQVVKPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQENADSLAYEVSLAVFQQAGGVGERPQPGF | ||||||
Modified residue | 62 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 64 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length542
- Mass (Da)59,474
- Last updated2012-07-11 v2
- ChecksumA5C7A8492751E150
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AEMK01179872 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CU463150 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
GACC01000082 EMBL· GenBank· DDBJ | JAA53725.1 EMBL· GenBank· DDBJ | mRNA |