5KF6
Structure of proline utilization A from Sinorhizobium meliloti complexed with L-tetrahydrofuroic acid and NAD+ in space group P21
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 | 0003824 | molecular_function | catalytic 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 | 0006560 | biological_process | proline metabolic process |
| A | 0006561 | biological_process | obsolete proline biosynthetic process |
| 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 | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0003824 | molecular_function | catalytic 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 | 0006560 | biological_process | proline metabolic process |
| B | 0006561 | biological_process | obsolete proline biosynthetic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue FAD A 2001 |
| Chain | Residue |
| A | ASP306 |
| A | ALA372 |
| A | TYR373 |
| A | TRP374 |
| A | PHE392 |
| A | THR393 |
| A | ARG394 |
| A | LYS395 |
| A | THR398 |
| A | ALA421 |
| A | THR422 |
| A | ALA307 |
| A | HIS423 |
| A | ASN424 |
| A | GLN447 |
| A | CYS448 |
| A | LEU449 |
| A | TYR473 |
| A | ARG489 |
| A | GLU492 |
| A | SER497 |
| A | SER498 |
| A | VAL338 |
| A | PHE499 |
| A | TFB2003 |
| A | HOH2128 |
| A | HOH2304 |
| A | HOH2364 |
| A | HOH2532 |
| A | GLN340 |
| A | TYR342 |
| A | ARG367 |
| A | VAL369 |
| A | LYS370 |
| A | GLY371 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue NAD A 2002 |
| Chain | Residue |
| A | ILE703 |
| A | SER704 |
| A | PRO705 |
| A | TRP706 |
| A | ASN707 |
| A | ILE712 |
| A | LYS730 |
| A | ALA732 |
| A | GLU733 |
| A | ASP762 |
| A | GLY763 |
| A | GLY766 |
| A | ALA767 |
| A | PHE780 |
| A | THR781 |
| A | GLY782 |
| A | SER783 |
| A | VAL786 |
| A | GLU810 |
| A | THR811 |
| A | GLY812 |
| A | CYS844 |
| A | GLU940 |
| A | PHE942 |
| A | PHE1010 |
| A | MG2004 |
| A | HOH2188 |
| A | HOH2221 |
| A | HOH2264 |
| A | HOH2268 |
| A | HOH2549 |
| A | HOH2603 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue TFB A 2003 |
| Chain | Residue |
| A | LYS265 |
| A | ASP306 |
| A | TYR473 |
| A | TYR485 |
| A | ARG488 |
| A | ARG489 |
| A | FAD2001 |
| A | HOH2338 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 2004 |
| Chain | Residue |
| A | NAD2002 |
| A | HOH2221 |
| A | HOH2276 |
| A | HOH2549 |
| A | HOH2651 |
| B | HOH2678 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PGE A 2005 |
| Chain | Residue |
| A | HIS1045 |
| A | GLY1079 |
| A | HIS1097 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue PGE A 2006 |
| Chain | Residue |
| A | ALA670 |
| A | GLU671 |
| A | GLU674 |
| A | ALA711 |
| A | ARG843 |
| A | HOH2400 |
| A | HOH2569 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PGE A 2007 |
| Chain | Residue |
| A | LYS379 |
| A | LEU383 |
| A | GLU1090 |
| A | ASN1219 |
| A | HOH2537 |
| A | HOH2562 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 2001 |
| Chain | Residue |
| B | VAL338 |
| B | GLN340 |
| B | TYR342 |
| B | ARG367 |
| B | VAL369 |
| B | LYS370 |
| B | GLY371 |
| B | ALA372 |
| B | TYR373 |
| B | TRP374 |
| B | PHE392 |
| B | THR393 |
| B | ARG394 |
| B | LYS395 |
| B | THR398 |
| B | ALA421 |
| B | THR422 |
| B | HIS423 |
| B | ASN424 |
| B | CYS448 |
| B | LEU449 |
| B | TYR473 |
| B | GLU492 |
| B | SER498 |
| B | PHE499 |
| B | TFB2003 |
| B | HOH2105 |
| B | HOH2120 |
| B | HOH2389 |
| B | ASP306 |
| B | ALA307 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | binding site for residue NAD B 2002 |
| Chain | Residue |
| B | ILE703 |
| B | SER704 |
| B | PRO705 |
| B | TRP706 |
| B | ASN707 |
| B | ILE712 |
| B | LYS730 |
| B | ALA732 |
| B | GLU733 |
| B | GLY763 |
| B | GLY766 |
| B | ALA767 |
| B | PHE780 |
| B | THR781 |
| B | GLY782 |
| B | SER783 |
| B | VAL786 |
| B | GLU810 |
| B | THR811 |
| B | GLY812 |
| B | CYS844 |
| B | GLU940 |
| B | PHE942 |
| B | PHE1010 |
| B | MG2004 |
| B | HOH2159 |
| B | HOH2251 |
| B | HOH2363 |
| B | HOH2563 |
| B | HOH2590 |
| B | HOH2597 |
| B | HOH2627 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue TFB B 2003 |
| Chain | Residue |
| B | LYS265 |
| B | ASP306 |
| B | TYR473 |
| B | ARG488 |
| B | FAD2001 |
| B | HOH2404 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 2004 |
| Chain | Residue |
| B | NAD2002 |
| B | HOH2251 |
| B | HOH2478 |
| B | HOH2590 |
| B | HOH2627 |
| B | HOH2668 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 2005 |
| Chain | Residue |
| B | ALA581 |
| B | THR582 |
| B | HOH2101 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue PGE B 2006 |
| Chain | Residue |
| B | GLU674 |
| B | ALA711 |
| B | ARG843 |
| B | HOH2260 |
| B | HOH2501 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue PGE B 2007 |
| Chain | Residue |
| B | HIS1045 |
| B | GLY1079 |
| B | LEU1096 |
| B | HIS1097 |
| B | HOH2140 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue PGE B 2008 |
| Chain | Residue |
| B | GLU73 |
| B | GLY77 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue PGE B 2009 |
| Chain | Residue |
| B | LYS379 |
| B | GLU1090 |
| B | ASN1219 |
| B | HOH2174 |
| B | HOH2536 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 B 2010 |
| Chain | Residue |
| A | HIS433 |
| A | MET434 |
| B | LYS897 |
| B | HOH2574 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FdSAGQRCSALR |
| Chain | Residue | Details |
| A | PHE837-ARG848 |
