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 | 1-pyrroline-5-carboxylate dehydrogenase activity |
A | 0004657 | molecular_function | proline dehydrogenase activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
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 |
B | 0000166 | molecular_function | nucleotide 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 | 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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003700 | molecular_function | DNA-binding transcription factor activity |
C | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
C | 0004657 | molecular_function | proline dehydrogenase activity |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0006562 | biological_process | proline catabolic process |
C | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
C | 0010133 | biological_process | proline catabolic process to 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 | 1-pyrroline-5-carboxylate dehydrogenase activity |
D | 0004657 | molecular_function | proline dehydrogenase activity |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0006562 | biological_process | proline catabolic process |
D | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
D | 0010133 | biological_process | proline catabolic process to 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 |