| General Information |
| MoonProt ID | 207 |
| First appeared in release | 1.0 |
| Name(s) | Bifunctional protein PutA
Proline oxidase
Delta-1-pyrroline-5-carboxylate dehydrogenase
P5C dehydrogenase
L-glutamate gamma-semialdehyde dehydrogenase
Proline utilization A
Transcriptional repressor Proline dehydrogenase
Gene Name: putA
***This protein has two different enzyme functions at the C-terminal and N-terminal ends, which is probably due to gene fusion during evolution. We consider it to be a Moonlighting Protein because it has a transcription repressor function in addition to the enzyme functions.**** |
| UniProt ID | P09546 (PUTA_ECOLI), Reviewed |
| GO terms | GO:0006351 transcription, DNA-templated
GO:0006355 regulation of transcription, DNA-templated
GO:0006537 glutamate biosynthetic process
GO:0006560 proline metabolic process
GO:0006561 proline biosynthetic process
GO:0006562 proline catabolic process
GO:0008152 metabolic process
GO:0010133 proline catabolic process to glutamate
GO:0045892 negative regulation of transcription, DNA-templated
GO:0055114 oxidation-reduction process
GO:0000986 bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding
GO:0001141 bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription
GO:0003677 DNA binding
GO:0003700 sequence-specific DNA binding transcription factor activity
GO:0003824 catalytic activity
GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
GO:0004657 proline dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0043565 sequence-specific DNA binding
GO:0050660 flavin adenine dinucleotide binding
GO:0009898 cytoplasmic side of plasma membrane |
| Organisms for which functions have been demonstrated | Escherichia coli (Gram negative bacterium) |
| Sequence length | 1320 |
| FASTA sequence | >sp|P09546|PUTA_ECOLI Bifunctional protein PutA OS=Escherichia coli (strain K12) GN=putA PE=1 SV=3
MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPELPALLSGAANESDEAPTPAEEPHQPFLDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRNQKNASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEASLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEESDRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGYVREATPREVEQALESAVNNAPIWFATPPAERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRSKGRPVFQAVRENSEDAREWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPESALAVTLARQDAKYPVDAQLKAALTQPLNALREWAANRPELQALCTQYGELAQAGTQRLLPGPTGERNTWTLLPRERVLCIADDEQDALTQLAAVLAVGSQVLWPDDALHRQLVKALPSAVSERIQLAKAENITAQPFDAVIFHGDSDQLRALCEAVAARDGTIVSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG
|
| Structure Information |
| PDB ID | 4O8A
1TIW
1TJ0
1TJ1
2FZM
2FZN
4JNZ
1TJ2
3ITG
4JNY
3E2Q
3EWR
3E2S |
| Quaternary structure | |
| SCOP | N-terminal domain of bifunctional PutA protein, TIM beta/alpha-barrel |
| CATH | 3.20.20.220 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | 4.47%, 611 - 669 |
| Predicted Disorder Regions | 1-12, 22, 48-83, 136-148, 196-200, 315-318, 590-602, 614-628, 638-639, 650-657, 989-990, 1091-1096, 1119-1137 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Proline dehydrogenase / Proline oxidase, enzyme
L-proline + a quinone => (S)-1-pyrroline-5-carboxylate + a quinol
L-glutamate 5-semialdehyde + NAD+ + H2O => L-glutamate + NADH
Amino-acid degradation, L-proline degradation into L-glutamate |
| References for function | RC Scarpulla and RL Soffer. (1978) Membrane-bound Proline Dehydrogenase from Escherichia coli, solubilization, purification and characterization. J. Biol. Chem. 253, 5997-6001.
JM Wood. (1981) Genetics of L-Proline Utilization in Escherichia coli. J. Bacte. 146, 895-901.
|
| E.C. number | 1.5.5.2 and 1.2.1.88 |
| Location of functional site(s) | |
| Cellular location of function | Cytoplasmic side of membrane, peripheral membrane protein |
| Comments | |
| Function 2 |
| Function description | transcriptional repressor of the put operon
|
| References for function | JM Wood. (1981) Genetics of L-Proline Utilization in Escherichia coli. J. Bacte. 146, 895-901. PMID: 7016835 |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | Cytoplasm, bound to DNA |
| Comments | |