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 | 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 |
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 |