4Q72
Crystal Structure of Bradyrhizobium japonicum Proline Utilization A (PutA) Mutant D779Y
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0006561 | biological_process | proline biosynthetic process |
| A | 0006562 | biological_process | proline catabolic process |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0010133 | biological_process | proline catabolic process to glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0006561 | biological_process | proline biosynthetic process |
| B | 0006562 | biological_process | proline catabolic process |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0010133 | biological_process | proline catabolic process to glutamate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 2001 |
| Chain | Residue |
| A | ASP278 |
| A | ALA344 |
| A | TYR345 |
| A | TRP346 |
| A | PHE364 |
| A | THR365 |
| A | ARG366 |
| A | LYS367 |
| A | THR370 |
| A | ALA393 |
| A | THR394 |
| A | ALA279 |
| A | HIS395 |
| A | ASN396 |
| A | TYR441 |
| A | SER466 |
| A | PHE467 |
| A | HOH2120 |
| A | HOH2149 |
| A | HOH2190 |
| A | ALA310 |
| A | GLN312 |
| A | TYR314 |
| A | ARG339 |
| A | VAL341 |
| A | LYS342 |
| A | GLY343 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 2002 |
| Chain | Residue |
| A | SER30 |
| A | PRO32 |
| A | ARG36 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 2003 |
| Chain | Residue |
| A | GLU256 |
| A | ALA297 |
| A | PRO299 |
| A | LYS302 |
| A | HIS332 |
| A | ARG334 |
| A | HOH2283 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 2004 |
| Chain | Residue |
| A | ASP359 |
| A | VAL517 |
| A | GLU518 |
| A | ALA524 |
| A | HOH2239 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2005 |
| Chain | Residue |
| A | ARG475 |
| A | ARG475 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2006 |
| Chain | Residue |
| A | ARG366 |
| A | LYS367 |
| A | ALA368 |
| A | HOH2124 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2007 |
| Chain | Residue |
| A | ARG791 |
| A | SER793 |
| A | ILE945 |
| A | GLY946 |
| A | ALA947 |
| A | HOH2152 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD B 1001 |
| Chain | Residue |
| B | ASP278 |
| B | ALA279 |
| B | ALA310 |
| B | GLN312 |
| B | TYR314 |
| B | ARG339 |
| B | VAL341 |
| B | LYS342 |
| B | GLY343 |
| B | ALA344 |
| B | TRP346 |
| B | PHE364 |
| B | THR365 |
| B | ARG366 |
| B | LYS367 |
| B | THR370 |
| B | ALA393 |
| B | THR394 |
| B | HIS395 |
| B | ASN396 |
| B | TYR441 |
| B | SER466 |
| B | PHE467 |
| B | HOH1131 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| B | PHE659 |
| B | ARG791 |
| B | SER793 |
| B | ILE945 |
| B | GLY946 |
| B | ALA947 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1003 |
| Chain | Residue |
| B | ARG475 |
| B | ARG475 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1004 |
| Chain | Residue |
| B | ARG366 |
| B | LYS367 |
| B | ALA368 |
| B | HOH1145 |
Functional Information from PROSITE/UniProt
