7K47
Crystal Structure of Glucosamine-1-phosphate N-acetyltransferase from Stenotrophomonas maltophilia K279a
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | HIS362 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | LEU10 | |
| A | ASN226 | |
| A | ARG332 | |
| A | LYS350 | |
| A | TYR365 | |
| A | ASN376 | |
| A | ALA379 | |
| A | ASN385 | |
| A | SER404 | |
| A | ALA422 | |
| A | ARG439 | |
| A | LYS24 | |
| A | GLN76 | |
| A | GLY81 | |
| A | TYR103 | |
| A | ASP105 | |
| A | GLY138 | |
| A | GLU153 | |
| A | ASN168 |
