Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide 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 | 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 | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 901 |
| Chain | Residue |
| B | LYS221 |
| B | ARG238 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 902 |
| Chain | Residue |
| A | LYS221 |
| A | ARG238 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 903 |
| Chain | Residue |
| B | HOH2180 |
| B | VAL537 |
| B | HIS539 |
| B | ILE542 |
| B | HOH1893 |
| B | HOH2179 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 904 |
| Chain | Residue |
| A | VAL537 |
| A | HIS539 |
| A | ILE542 |
| A | HOH1877 |
| A | HOH1910 |
| A | HOH2208 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE COA A 990 |
| Chain | Residue |
| A | PHE163 |
| A | GLY165 |
| A | ARG191 |
| A | TRP309 |
| A | ALA357 |
| A | THR359 |
| A | VAL386 |
| A | SER523 |
| A | GLY524 |
| A | ARG584 |
| A | PRO589 |
| A | HOH1854 |
| A | HOH1883 |
| A | HOH1923 |
| A | HOH2133 |
| A | HOH2162 |
| A | HOH2163 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COA B 991 |
| Chain | Residue |
| B | PHE163 |
| B | GLY165 |
| B | ARG191 |
| B | ILE196 |
| B | TRP309 |
| B | ALA357 |
| B | THR359 |
| B | VAL386 |
| B | SER523 |
| B | GLY524 |
| B | ARG584 |
| B | PRO589 |
| B | HOH1883 |
| B | HOH2010 |
| B | HOH2014 |
| B | HOH2060 |
| B | HOH2092 |
| B | HOH2093 |
| B | HOH2110 |
| B | HOH2131 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PRX A 999 |
| Chain | Residue |
| A | THR311 |
| A | GLY387 |
| A | GLU388 |
| A | PRO389 |
| A | ASP411 |
| A | THR412 |
| A | TRP413 |
| A | TRP414 |
| A | GLN415 |
| A | THR416 |
| A | ASP500 |
| A | ILE512 |
| A | ARG515 |
| A | ARG526 |
| A | HOH1887 |
| A | HOH2054 |
| A | HOH2056 |
| A | HOH2078 |
| A | HOH2201 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PRX B 998 |
| Chain | Residue |
| B | THR311 |
| 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 | HOH2005 |
| B | HOH2023 |
| B | HOH2030 |
| B | HOH2104 |
| B | HOH2111 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1800 |
| Chain | Residue |
| B | VAL161 |
| B | ILE162 |
| B | PHE163 |
| B | PHE166 |
| B | TYR263 |
| B | GLY308 |
| B | HOH1834 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1801 |
| Chain | Residue |
| A | ILE162 |
| A | PHE163 |
| A | PHE166 |
| A | TYR263 |
| A | GLY308 |
| A | VAL161 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1802 |
| Chain | Residue |
| A | GLU41 |
| A | GLN42 |
| A | ILE45 |
| A | HOH1891 |
| A | HOH1996 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1803 |
| Chain | Residue |
| A | GLY164 |
| A | GLY165 |
| A | PHE166 |
| A | SER167 |
| A | ILE196 |
| A | ASN201 |
| A | PRO589 |
| A | HOH2035 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1804 |
| Chain | Residue |
| B | VAL190 |
| B | GLY193 |
| B | ARG194 |
| B | SER195 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01123","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12627952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17497934","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Hinge residue important for conformational flexibility"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; by Pat","evidences":[{"source":"HAMAP-Rule","id":"MF_01123","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12493915","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15236963","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
