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 | 5 |
Details | BINDING SITE FOR RESIDUE MG B 901 |
Chain | Residue |
B | VAL537 |
B | HIS539 |
B | ILE542 |
B | HOH1137 |
B | HOH1148 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 902 |
Chain | Residue |
A | HOH1198 |
A | HOH1200 |
A | VAL537 |
A | HIS539 |
A | ILE542 |
A | HOH1097 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE COA A 990 |
Chain | Residue |
A | PHE163 |
A | GLY164 |
A | GLY165 |
A | ARG191 |
A | ARG194 |
A | ILE196 |
A | SER523 |
A | HIS525 |
A | ARG584 |
A | PRO589 |
A | HOH1034 |
A | HOH1181 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE COA B 991 |
Chain | Residue |
B | PHE163 |
B | GLY164 |
B | GLY165 |
B | ARG191 |
B | ARG194 |
B | ILE196 |
B | ARG584 |
B | PRO589 |
B | HOH1172 |
site_id | AC5 |
Number of Residues | 14 |
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 | ARG515 |
A | ARG526 |
A | HOH1156 |
site_id | AC6 |
Number of Residues | 15 |
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 | HOH1168 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 800 |
Chain | Residue |
B | VAL161 |
B | ILE162 |
B | PHE163 |
B | PHE166 |
B | TYR263 |
B | GLY308 |
B | HOH1038 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 801 |
Chain | Residue |
A | VAL161 |
A | ILE162 |
A | PHE163 |
A | PHE166 |
A | TYR263 |
A | GLY308 |
A | HOH1037 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 802 |
Chain | Residue |
A | GLU41 |
A | GLN42 |
A | ILE45 |
A | HOH1009 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 803 |
Chain | Residue |
A | GLY164 |
A | GLY165 |
A | PHE166 |
A | SER167 |
A | ILE196 |
A | ASN201 |
A | ARG584 |
A | PRO589 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 804 |
Chain | Residue |
B | VAL190 |
B | GLY193 |
B | ARG194 |
B | SER195 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 805 |
Chain | Residue |
B | GLY164 |
B | GLY165 |
B | PHE166 |
B | SER167 |
B | ILE196 |
B | ASN201 |
B | ARG584 |
B | HOH1104 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DTSQSKHISyrEL |
Chain | Residue | Details |
A | ASP101-LEU113 | |
site_id | PS00455 |
Number of Residues | 12 |
Details | AMP_BINDING Putative AMP-binding domain signature. ILYTSGSTGkPK |
Chain | Residue | Details |
A | ILE261-LYS272 | |
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 | |
Chain | Residue | Details |
A | THR311 | |
A | ASN335 | |
A | SER523 | |
A | ARG584 | |
B | THR311 | |
B | ASN335 | |
B | SER523 | |
B | ARG584 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Hinge residue important for conformational flexibility |
Chain | Residue | Details |
A | ASP517 | |
B | ASP517 | |
Chain | Residue | Details |
A | LYS609 | |
B | LYS609 | |