5UX5
Structure of Proline Utilization A (PutA) from Corynebacterium freiburgense
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006562 | biological_process | L-proline catabolic process |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0010133 | biological_process | L-proline catabolic process to L-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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006562 | biological_process | L-proline catabolic process |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0010133 | biological_process | L-proline catabolic process to L-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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| C | 0004657 | molecular_function | proline dehydrogenase activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006562 | biological_process | L-proline catabolic process |
| C | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| C | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| D | 0004657 | molecular_function | proline dehydrogenase activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006562 | biological_process | L-proline catabolic process |
| D | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| D | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue FAD A 2001 |
| Chain | Residue |
| A | ASP230 |
| A | ALA299 |
| A | LEU301 |
| A | TYR318 |
| A | THR320 |
| A | LYS321 |
| A | VAL324 |
| A | SER349 |
| A | HIS350 |
| A | ASN351 |
| A | GLU374 |
| A | MET231 |
| A | MET375 |
| A | ASN420 |
| A | VAL261 |
| A | GLN263 |
| A | TYR265 |
| A | ARG294 |
| A | VAL296 |
| A | LYS297 |
| A | GLY298 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue NAD A 2002 |
| Chain | Residue |
| A | SER590 |
| A | TRP592 |
| A | LYS616 |
| A | PRO617 |
| A | ALA618 |
| A | PRO619 |
| A | ASP648 |
| A | GLU649 |
| A | GLY653 |
| A | GLY669 |
| A | ALA670 |
| A | THR673 |
| A | PHE677 |
| A | TRP680 |
| A | GLU817 |
| A | PHE819 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 2003 |
| Chain | Residue |
| A | SER724 |
| A | GLY877 |
| A | ALA878 |
| A | PHE885 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue FAD B 2001 |
| Chain | Residue |
| B | MET231 |
| B | VAL261 |
| B | GLN263 |
| B | TYR265 |
| B | ARG294 |
| B | VAL296 |
| B | LYS297 |
| B | GLY298 |
| B | ALA299 |
| B | LEU301 |
| B | TYR318 |
| B | ALA319 |
| B | THR320 |
| B | LYS321 |
| B | VAL324 |
| B | SER349 |
| B | HIS350 |
| B | ASN351 |
| B | LEU376 |
| B | ASN420 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue NAD B 2002 |
| Chain | Residue |
| B | SER590 |
| B | TRP592 |
| B | LYS616 |
| B | ALA618 |
| B | PRO619 |
| B | ASP648 |
| B | GLU649 |
| B | MET657 |
| B | GLY669 |
| B | ALA670 |
| B | THR673 |
| B | PHE677 |
| B | TRP680 |
| B | PHE819 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 2003 |
| Chain | Residue |
| B | SER724 |
| B | GLY877 |
| B | ALA878 |
| B | PHE885 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue FAD C 2001 |
| Chain | Residue |
| C | MET231 |
| C | VAL261 |
| C | GLN263 |
| C | ARG294 |
| C | VAL296 |
| C | LYS297 |
| C | GLY298 |
| C | ALA299 |
| C | LEU301 |
| C | TYR318 |
| C | ALA319 |
| C | THR320 |
| C | LYS321 |
| C | VAL324 |
| C | SER349 |
| C | HIS350 |
| C | ASN351 |
| C | MET375 |
| C | LEU376 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue NAD C 2002 |
| Chain | Residue |
| C | TRP592 |
| C | LYS616 |
| C | ALA618 |
| C | PRO619 |
| C | GLU649 |
| C | GLY653 |
| C | THR668 |
| C | GLY669 |
| C | ALA670 |
| C | THR673 |
| C | LEU676 |
| C | PHE677 |
| C | GLU817 |
| C | PHE819 |
| C | SER590 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 2003 |
| Chain | Residue |
| C | SER724 |
| C | GLY877 |
| C | ALA878 |
| C | PHE885 |
| site_id | AD1 |
| Number of Residues | 18 |
| Details | binding site for residue FAD D 2001 |
| Chain | Residue |
| D | MET231 |
| D | VAL261 |
| D | GLN263 |
| D | ARG294 |
| D | VAL296 |
| D | LYS297 |
| D | GLY298 |
| D | ALA299 |
| D | LEU301 |
| D | THR320 |
| D | LYS321 |
| D | VAL324 |
| D | SER349 |
| D | HIS350 |
| D | ASN351 |
| D | GLU374 |
| D | MET375 |
| D | ASN420 |
| site_id | AD2 |
| Number of Residues | 15 |
| Details | binding site for residue NAD D 2002 |
| Chain | Residue |
| D | SER590 |
| D | TRP592 |
| D | LYS616 |
| D | ALA618 |
| D | PRO619 |
| D | ASP648 |
| D | GLU649 |
| D | GLY653 |
| D | MET657 |
| D | THR668 |
| D | GLY669 |
| D | ALA670 |
| D | THR673 |
| D | PHE677 |
| D | TRP680 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 2003 |
| Chain | Residue |
| D | SER724 |
| D | GLY877 |
| D | ALA878 |
| D | PHE885 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgHAGQKCSAAS |
| Chain | Residue | Details |
| A | PHE716-SER727 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. AETSGKNA |
| Chain | Residue | Details |
| A | ALA688-ALA695 |
