5VMK
Crystal structure of a bifunctional GlmU UDP-N-acetylglucosamine diphosphorylase/glucosamine-1- phosphate N-acetyltransferase from Acinetobacter baumannii
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 | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000902 | biological_process | cell morphogenesis |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0000902 | biological_process | cell morphogenesis |
| C | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0009245 | biological_process | lipid A biosynthetic process |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CIT A 501 |
| Chain | Residue |
| A | ARG330 |
| A | LYS348 |
| A | TYR363 |
| A | ASN383 |
| A | TYR384 |
| A | LYS389 |
| C | ASN359 |
| C | HIS360 |
| C | ASN374 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 502 |
| Chain | Residue |
| A | GLY11 |
| A | LYS12 |
| A | GLY13 |
| A | ARG15 |
| A | LYS22 |
| A | ASN224 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue CIT B 501 |
| Chain | Residue |
| A | ASN359 |
| A | HIS360 |
| B | ARG330 |
| B | LYS348 |
| B | TYR363 |
| B | ASN383 |
| B | TYR384 |
| B | LYS389 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PG4 B 502 |
| Chain | Residue |
| A | ALA252 |
| A | ARG270 |
| A | ILE271 |
| A | ASP272 |
| A | GLU288 |
| B | ALA28 |
| B | GLY29 |
| B | GLU233 |
| B | ARG260 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue PG4 C 501 |
| Chain | Residue |
| A | PRO26 |
| A | ALA28 |
| A | GLY29 |
| A | GLU233 |
| C | ALA252 |
| C | ARG270 |
| C | ILE271 |
| C | GLU288 |
| C | ILE289 |
| C | HOH667 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue CIT C 502 |
| Chain | Residue |
| B | ASN359 |
| B | HIS360 |
| B | ASN374 |
| C | ARG330 |
| C | LYS348 |
| C | TYR363 |
| C | ASN383 |
| C | TYR384 |
| C | LYS389 |
| C | HOH640 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PG4 C 503 |
| Chain | Residue |
| B | ARG270 |
| B | GLU288 |
| C | ALA28 |
| C | GLY29 |
| C | GLU233 |
| C | ARG260 |
| C | HOH635 |
| C | HOH677 |
Functional Information from PROSITE/UniProt
| site_id | PS00101 |
| Number of Residues | 29 |
| Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. IGsnSsLvapVtIGngAtVGagSvItkdV |
| Chain | Residue | Details |
| A | ILE400-VAL428 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | HIS360 | |
| B | HIS360 | |
| C | HIS360 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 57 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | GLY137 | |
| A | GLU151 | |
| A | ASN166 | |
| A | ASN224 | |
| A | ARG330 | |
| A | LYS348 | |
| A | TYR363 | |
| A | ASN374 | |
| A | ALA377 | |
| A | ASN383 | |
| A | SER402 | |
| A | ALA420 | |
| A | ARG437 | |
| B | LEU8 | |
| B | LYS22 | |
| B | GLN73 | |
| B | GLY78 | |
| B | TYR100 | |
| B | ASP102 | |
| B | GLY137 | |
| B | GLU151 | |
| B | ASN166 | |
| B | ASN224 | |
| B | ARG330 | |
| B | LYS348 | |
| B | TYR363 | |
| B | ASN374 | |
| B | ALA377 | |
| B | ASN383 | |
| B | SER402 | |
| B | ALA420 | |
| B | ARG437 | |
| C | LEU8 | |
| C | LYS22 | |
| C | GLN73 | |
| C | GLY78 | |
| C | TYR100 | |
| C | ASP102 | |
| C | GLY137 | |
| C | GLU151 | |
| C | ASN166 | |
| C | ASN224 | |
| C | ARG330 | |
| C | LYS348 | |
| C | TYR363 | |
| C | ASN374 | |
| C | ALA377 | |
| C | ASN383 | |
| C | SER402 | |
| C | ALA420 | |
| C | ARG437 | |
| A | LEU8 | |
| A | LYS22 | |
| A | GLN73 | |
| A | GLY78 | |
| A | TYR100 | |
| A | ASP102 |
