5KF7
Structure of proline utilization A from Sinorhizobium meliloti complexed with L-tetrahydrofuroic acid and NAD+ in space group P3121
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| 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 | SER498 |
| A | PHE499 |
| A | VAL338 |
| A | TFB2003 |
| A | HOH2115 |
| A | HOH2219 |
| A | GLN340 |
| A | TYR342 |
| A | ARG367 |
| A | VAL369 |
| A | LYS370 |
| A | GLY371 |
| site_id | AC2 |
| Number of Residues | 31 |
| 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 | 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 | MG2009 |
| A | HOH2112 |
| A | HOH2163 |
| A | HOH2227 |
| A | HOH2246 |
| A | HOH2291 |
| A | HOH2302 |
| A | HOH2585 |
| 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 | HOH2156 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 2004 |
| Chain | Residue |
| A | HIS1045 |
| A | GLY1079 |
| A | LEU1096 |
| A | HIS1097 |
| A | HOH2258 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue PG4 A 2005 |
| Chain | Residue |
| A | ALA670 |
| A | GLU671 |
| A | GLU674 |
| A | PHE708 |
| A | ALA711 |
| A | ARG843 |
| A | ILE1001 |
| A | HOH2353 |
| A | HOH2492 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE A 2006 |
| Chain | Residue |
| A | ALA570 |
| A | ALA571 |
| A | LYS573 |
| A | VAL601 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue 1PE A 2007 |
| Chain | Residue |
| A | LYS379 |
| A | LEU383 |
| A | GLU1090 |
| A | ASN1219 |
| A | ALA1221 |
| A | HOH2300 |
| A | HOH2432 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 2008 |
| Chain | Residue |
| A | ARG688 |
| A | PRO1039 |
| A | GLN1040 |
| A | HOH2141 |
| A | HOH2263 |
| A | HOH2571 |
| A | SER94 |
| A | GLN96 |
| A | ARG170 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 2009 |
| Chain | Residue |
| A | NAD2002 |
| A | HOH2239 |
| A | HOH2246 |
| A | HOH2302 |
| A | HOH2623 |
| A | HOH2647 |
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 |
