1G99
AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006082 | biological_process | organic acid metabolic process |
| A | 0006083 | biological_process | acetate metabolic process |
| A | 0006085 | biological_process | acetyl-CoA biosynthetic process |
| A | 0008776 | molecular_function | acetate kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016774 | molecular_function | phosphotransferase activity, carboxyl group as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006082 | biological_process | organic acid metabolic process |
| B | 0006083 | biological_process | acetate metabolic process |
| B | 0006085 | biological_process | acetyl-CoA biosynthetic process |
| B | 0008776 | molecular_function | acetate kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016774 | molecular_function | phosphotransferase activity, carboxyl group as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 409 |
| Chain | Residue |
| A | ARG91 |
| A | HIS123 |
| A | HIS180 |
| A | GLY212 |
| A | ARG241 |
| A | ADP410 |
| A | HOH446 |
| A | HOH453 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 409 |
| Chain | Residue |
| B | GLY212 |
| B | ARG241 |
| B | ADP410 |
| B | HIS180 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP A 410 |
| Chain | Residue |
| A | ASN211 |
| A | ASP283 |
| A | PHE284 |
| A | ARG285 |
| A | GLY331 |
| A | ILE332 |
| A | ASN335 |
| A | SER336 |
| A | SO4409 |
| A | HOH445 |
| A | HOH453 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP B 410 |
| Chain | Residue |
| B | HIS208 |
| B | GLY210 |
| B | ASN211 |
| B | GLY212 |
| B | ASN282 |
| B | ASP283 |
| B | PHE284 |
| B | ARG285 |
| B | GLY331 |
| B | ILE332 |
| B | ASN335 |
| B | SER336 |
| B | SO4409 |
Functional Information from PROSITE/UniProt
| site_id | PS01075 |
| Number of Residues | 12 |
| Details | ACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvINaGSSSlK |
| Chain | Residue | Details |
| A | VAL3-LYS14 |
| site_id | PS01076 |
| Number of Residues | 18 |
| Details | ACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. IItcHlGnGsSItAvegG |
| Chain | Residue | Details |
| A | ILE204-GLY221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11133963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15647264","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 11133963, 11562377 |
| Chain | Residue | Details |
| A | GLY212 | |
| A | SER10 | |
| A | ASP148 | |
| A | ARG91 | |
| A | ARG241 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 11133963, 11562377 |
| Chain | Residue | Details |
| B | GLY212 | |
| B | SER10 | |
| B | ASP148 | |
| B | ARG91 | |
| B | ARG241 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 643 |
| Chain | Residue | Details |
| A | ASN7 | metal ligand |
| A | ARG91 | electrostatic stabiliser, polar interaction |
| A | HIS180 | electrostatic stabiliser, polar interaction |
| A | ARG241 | electrostatic stabiliser, polar interaction |
| A | GLU384 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 643 |
| Chain | Residue | Details |
| B | ASN7 | metal ligand |
| B | ARG91 | electrostatic stabiliser, polar interaction |
| B | HIS180 | electrostatic stabiliser, polar interaction |
| B | ARG241 | electrostatic stabiliser, polar interaction |
| B | GLU384 | metal ligand |
