2G5F
The structure of MbtI from Mycobacterium Tuberculosis, the first enzyme in the synthesis of Mycobactin, reveals it to be a salicylate synthase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | tryptophan biosynthetic process |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004106 | molecular_function | chorismate mutase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0008909 | molecular_function | isochorismate synthase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009697 | biological_process | salicylic acid biosynthetic process |
A | 0010106 | biological_process | cellular response to iron ion starvation |
A | 0016829 | molecular_function | lyase activity |
A | 0016833 | molecular_function | oxo-acid-lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
A | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0052572 | biological_process | response to host immune response |
B | 0000162 | biological_process | tryptophan biosynthetic process |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004106 | molecular_function | chorismate mutase activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0008909 | molecular_function | isochorismate synthase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0009697 | biological_process | salicylic acid biosynthetic process |
B | 0010106 | biological_process | cellular response to iron ion starvation |
B | 0016829 | molecular_function | lyase activity |
B | 0016833 | molecular_function | oxo-acid-lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
B | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0052572 | biological_process | response to host immune response |
C | 0000162 | biological_process | tryptophan biosynthetic process |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004106 | molecular_function | chorismate mutase activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0008909 | molecular_function | isochorismate synthase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0009697 | biological_process | salicylic acid biosynthetic process |
C | 0010106 | biological_process | cellular response to iron ion starvation |
C | 0016829 | molecular_function | lyase activity |
C | 0016833 | molecular_function | oxo-acid-lyase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
C | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0052572 | biological_process | response to host immune response |
D | 0000162 | biological_process | tryptophan biosynthetic process |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004106 | molecular_function | chorismate mutase activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0008909 | molecular_function | isochorismate synthase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0009697 | biological_process | salicylic acid biosynthetic process |
D | 0010106 | biological_process | cellular response to iron ion starvation |
D | 0016829 | molecular_function | lyase activity |
D | 0016833 | molecular_function | oxo-acid-lyase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
D | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0052572 | biological_process | response to host immune response |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYR A 2001 |
Chain | Residue |
A | ILE207 |
A | TYR385 |
A | LEU404 |
A | ARG405 |
A | GLY419 |
A | ALA420 |
A | LYS438 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PYR B 2002 |
Chain | Residue |
B | TYR385 |
B | LEU404 |
B | ARG405 |
B | GLY419 |
B | ALA420 |
B | LYS438 |
B | ILE207 |
B | ALA362 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IMD A 3001 |
Chain | Residue |
A | ARG303 |
A | GLU307 |
D | GLU289 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IMD C 3002 |
Chain | Residue |
B | ARG303 |
B | GLU307 |
C | GLN123 |
C | GLU289 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IMD C 3003 |
Chain | Residue |
B | GLU289 |
C | ARG303 |
C | GLU307 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IMD D 3004 |
Chain | Residue |
A | GLU289 |
D | ARG303 |
D | GLU307 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 4001 |
Chain | Residue |
C | LEU268 |
C | THR271 |
C | ARG405 |
C | ALA418 |
C | LYS438 |
C | HOH4044 |
C | HOH4108 |
C | HOH4157 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 4002 |
Chain | Residue |
D | ARG405 |
D | LYS438 |
D | THR441 |
D | HOH4069 |
D | HOH4175 |
D | HOH4187 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 4003 |
Chain | Residue |
A | ASP322 |
A | THR325 |
A | ARG327 |
A | HIS334 |
A | LEU335 |
A | GLY336 |
A | SER337 |
A | THR338 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 4004 |
Chain | Residue |
B | ASP322 |
B | THR325 |
B | ARG327 |
B | HIS334 |
B | LEU335 |
B | GLY336 |
B | SER337 |
B | THR338 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL C 4005 |
Chain | Residue |
C | GLU266 |
C | ASP322 |
C | THR325 |
C | ARG327 |
C | HIS334 |
C | LEU335 |
C | GLY336 |
C | SER337 |
C | THR338 |
C | HOH4246 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 4006 |
Chain | Residue |
D | GLU266 |
D | ASP322 |
D | THR325 |
D | ARG327 |
D | HIS334 |
D | LEU335 |
D | GLY336 |
D | SER337 |
D | THR338 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9X9I8 |
Chain | Residue | Details |
A | GLU252 | |
B | GLU252 | |
C | GLU252 | |
D | GLU252 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697 |
Chain | Residue | Details |
A | GLY270 | |
B | GLY270 | |
C | GLY270 | |
D | GLY270 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20512795 |
Chain | Residue | Details |
A | GLU297 | |
D | GLU297 | |
D | GLU431 | |
D | GLU434 | |
A | GLU431 | |
A | GLU434 | |
B | GLU297 | |
B | GLU431 | |
B | GLU434 | |
C | GLU297 | |
C | GLU431 | |
C | GLU434 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697 |
Chain | Residue | Details |
A | TYR385 | |
C | ARG405 | |
C | GLY419 | |
C | LYS438 | |
D | TYR385 | |
D | ARG405 | |
D | GLY419 | |
D | LYS438 | |
A | ARG405 | |
A | GLY419 | |
A | LYS438 | |
B | TYR385 | |
B | ARG405 | |
B | GLY419 | |
B | LYS438 | |
C | TYR385 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl => ECO:0000269|PubMed:17240979 |
Chain | Residue | Details |
A | LEU268 | |
B | LEU268 | |
C | LEU268 | |
D | LEU268 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1i7q |
Chain | Residue | Details |
A | HIS334 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1i7q |
Chain | Residue | Details |
B | HIS334 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1i7q |
Chain | Residue | Details |
C | HIS334 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1i7q |
Chain | Residue | Details |
D | HIS334 |