2HOX
alliinase from allium sativum (garlic)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005773 | cellular_component | vacuole |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031404 | molecular_function | chloride ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047654 | molecular_function | alliin lyase activity |
| B | 0005773 | cellular_component | vacuole |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031404 | molecular_function | chloride ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047654 | molecular_function | alliin lyase activity |
| C | 0005773 | cellular_component | vacuole |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0031404 | molecular_function | chloride ion binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0047654 | molecular_function | alliin lyase activity |
| D | 0005773 | cellular_component | vacuole |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0031404 | molecular_function | chloride ion binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0047654 | molecular_function | alliin lyase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CeCntCytGPdC |
| Chain | Residue | Details |
| A | CYS39-CYS50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9 |
| Chain | Residue | Details |
| A | TYR92 | |
| B | TYR92 | |
| C | TYR92 | |
| D | TYR92 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12235163, ECO:0007744|PDB:1LK9 |
| Chain | Residue | Details |
| A | LYS251 | |
| B | LYS251 | |
| C | LYS251 | |
| D | LYS251 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | ASN19 | |
| B | ASN19 | |
| C | ASN19 | |
| D | ASN19 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:12235163, ECO:0000269|PubMed:17174334, ECO:0007744|PDB:1LK9, ECO:0007744|PDB:2HOX |
| Chain | Residue | Details |
| A | ASN146 | |
| A | ASN328 | |
| B | ASN146 | |
| B | ASN328 | |
| C | ASN146 | |
| C | ASN328 | |
| D | ASN146 | |
| D | ASN328 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:17174334, ECO:0007744|PDB:2HOX |
| Chain | Residue | Details |
| A | ASN191 | |
| B | ASN191 | |
| C | ASN191 | |
| D | ASN191 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP225 | |
| A | TYR165 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | PRO96 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | PRO96 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | PRO96 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP225 | |
| B | TYR165 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PRO96 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | ASP225 | |
| C | TYR165 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | ASP225 | |
| D | TYR165 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS251 | |
| A | ASP225 | |
| A | TYR165 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS251 | |
| B | ASP225 | |
| B | TYR165 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | LYS251 | |
| C | ASP225 | |
| C | TYR165 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | LYS251 | |
| D | ASP225 | |
| D | TYR165 |
