2P2Q
Acetyl-CoA Synthetase, R584E mutation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003987 | molecular_function | acetate-CoA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006085 | biological_process | acetyl-CoA biosynthetic process |
A | 0006935 | biological_process | chemotaxis |
A | 0016208 | molecular_function | AMP binding |
A | 0016874 | molecular_function | ligase activity |
A | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
A | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
A | 0046872 | molecular_function | metal ion binding |
B | 0003987 | molecular_function | acetate-CoA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006085 | biological_process | acetyl-CoA biosynthetic process |
B | 0006935 | biological_process | chemotaxis |
B | 0016208 | molecular_function | AMP binding |
B | 0016874 | molecular_function | ligase activity |
B | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
B | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PRX A 999 |
Chain | Residue |
A | THR311 |
A | THR416 |
A | ASP500 |
A | ILE512 |
A | ARG515 |
A | ARG526 |
A | HOH1110 |
A | GLY387 |
A | GLU388 |
A | PRO389 |
A | ASP411 |
A | THR412 |
A | TRP413 |
A | TRP414 |
A | GLN415 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PRX B 998 |
Chain | Residue |
B | THR311 |
B | VAL386 |
B | GLY387 |
B | GLU388 |
B | PRO389 |
B | ASP411 |
B | THR412 |
B | TRP413 |
B | TRP414 |
B | GLN415 |
B | THR416 |
B | ASP500 |
B | ILE512 |
B | ARG515 |
B | ARG526 |
B | HOH1112 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG191 | |
B | ARG191 | |
B | GLY387 | |
B | ASP411 | |
B | ASP500 | |
B | ARG515 | |
B | ARG526 | |
B | VAL537 | |
B | HIS539 | |
B | ILE542 | |
A | GLY387 | |
A | ASP411 | |
A | ASP500 | |
A | ARG515 | |
A | ARG526 | |
A | VAL537 | |
A | HIS539 | |
A | ILE542 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01123, ECO:0000269|PubMed:12627952, ECO:0000269|PubMed:17497934 |
Chain | Residue | Details |
A | THR311 | |
A | ASN335 | |
A | SER523 | |
A | GLU584 | |
B | THR311 | |
B | ASN335 | |
B | SER523 | |
B | GLU584 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Hinge residue important for conformational flexibility |
Chain | Residue | Details |
A | ASP517 | |
B | ASP517 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; by Pat => ECO:0000255|HAMAP-Rule:MF_01123, ECO:0000269|PubMed:12493915, ECO:0000269|PubMed:15236963 |
Chain | Residue | Details |
A | LYS609 | |
B | LYS609 |