Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033353 | biological_process | S-adenosylmethionine cycle |
| A | 0071269 | biological_process | L-homocysteine biosynthetic process |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033353 | biological_process | S-adenosylmethionine cycle |
| B | 0071269 | biological_process | L-homocysteine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | THR198 |
| A | VAL285 |
| A | ASP286 |
| A | THR317 |
| A | GLY318 |
| A | ASN319 |
| A | ILE322 |
| A | ILE340 |
| A | GLY341 |
| A | HIS342 |
| A | LEU383 |
| A | THR199 |
| A | ASN385 |
| A | HIS392 |
| A | ADE502 |
| A | HOH678 |
| A | HOH680 |
| A | HOH696 |
| A | HOH709 |
| A | HOH737 |
| A | HOH743 |
| B | GLN454 |
| A | THR200 |
| B | LYS467 |
| B | TYR471 |
| A | ASN232 |
| A | GLY263 |
| A | ASP264 |
| A | VAL265 |
| A | SER283 |
| A | GLU284 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue ADE A 502 |
| Chain | Residue |
| A | HIS58 |
| A | THR60 |
| A | GLN62 |
| A | THR63 |
| A | MET390 |
| A | GLY391 |
| A | HIS392 |
| A | MET397 |
| A | NAD501 |
| A | HOH753 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 503 |
| Chain | Residue |
| A | GLN62 |
| A | MET390 |
| A | HIS392 |
| A | HOH650 |
| A | HOH671 |
| A | HOH797 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 504 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | MET251 |
| A | SER253 |
| A | LYS255 |
| A | LYS442 |
| A | HOH673 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | SER468 |
| A | HIS470 |
| A | TYR471 |
| A | HOH620 |
| A | HOH764 |
| A | HOH803 |
| B | ASP223 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| A | LYS467 |
| A | TYR471 |
| B | THR198 |
| B | THR199 |
| B | THR200 |
| B | ASN232 |
| B | GLY263 |
| B | ASP264 |
| B | VAL265 |
| B | GLU284 |
| B | VAL285 |
| B | ASP286 |
| B | CYS289 |
| B | THR317 |
| B | GLY318 |
| B | ASN319 |
| B | ILE322 |
| B | ILE340 |
| B | GLY341 |
| B | HIS342 |
| B | LEU383 |
| B | ASN385 |
| B | HIS392 |
| B | ADE502 |
| B | HOH645 |
| B | HOH679 |
| B | HOH687 |
| B | HOH737 |
| B | HOH749 |
| B | HOH780 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue ADE B 502 |
| Chain | Residue |
| B | NAD501 |
| B | LEU57 |
| B | HIS58 |
| B | THR60 |
| B | GLN62 |
| B | THR63 |
| B | MET390 |
| B | GLY391 |
| B | HIS392 |
| B | MET397 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 503 |
| Chain | Residue |
| B | GLN62 |
| B | MET390 |
| B | HIS392 |
| B | HOH640 |
| B | HOH801 |
| B | HOH804 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue BR B 504 |
| Chain | Residue |
| A | LYS189 |
| B | ASP371 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | THR200 |
| B | HIS203 |
| B | GLY318 |
| B | HOH601 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | MET251 |
| B | SER253 |
| B | LYS255 |
| B | PHE395 |
| B | LYS442 |
| B | ILE443 |
| B | HOH733 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | PHE20 |
| B | LYS23 |
| B | ILE360 |
| B | LYS361 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiYSTQDhAAAAI |
| Chain | Residue | Details |
| A | SER81-ILE95 | |
| site_id | PS00739 |
| Number of Residues | 18 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvamVaGFGdVGKGsaA |
| Chain | Residue | Details |
| A | GLY254-ALA271 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26627650","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26627650","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26627650","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"26627650","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26627650","evidenceCode":"ECO:0000269"}]} |
