General Information |
MoonProt ID | 136 |
First appeared in release | 1.0 |
Name(s) | Bifunctional protein PutA
Proline utilization A
Put A proline dehydrogenase
Transcriptional repressor
Proline dehydrogenase, Proline oxidase
Delta-1-pyrroline-5-carboxylate dehydrogenase, P5C dehydrogenase
L-glutamate gamma-semialdehyde 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 | P10503 (PUTA_SALTY), 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:0055114 oxidation-reduction process
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:0016020 membrane |
Organisms for which functions have been demonstrated | Salmonella typhimurium (and also E. coli) (Gram negative bacterium) |
Sequence length | 1320 |
FASTA sequence | >sp|P10503|PUTA_SALTY Bifunctional protein PutA OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=putA PE=2 SV=4
MGTTTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLENSDTLPELPALFVGAANESEEPVAPQDEPHQPFLEFAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLRNQKSASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLVDLASRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADATLPLDELVADPVEAVEKLAQQEGQAGIPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLSSALLSNAMQKWQAKPVLEQPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADARVRGVMFTGSTEVATLLQRNIATRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDAQEWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAHRPPNALNTTLTRQDARYPVDAQLKTTLLAPLTALTQWAADRPALQTLCRQFADLAQAGTQRLLPGPTGERNTWTLLPRERVLCLADDEQDALTQLAAVLAVGSQALWSDDAFHRDLAKRLPAAVAARVQFAKAETLMAQPFDAVIFHGDSDKLRTVCEAVAAREGAIVSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG |
Structure Information |
PDB ID | Closest homologue in PDB is from E.coli with 95.60% amino acid sequence identity; 41% query cover |
Quaternary structure | |
SCOP | NA |
CATH | NA |
TM Helix Prediction | no TM helices |
DisProt Annotation | Not in DisProt |
Predicted Disorder Regions | 1 to 11, 21-22, 48-81, 137-147, 314-320, 589-628, 639, 651-657, 989-991, 1092-1095, 1120-1137 |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | Proline dehydrogenase / Proline oxidase
pyrroline-5-carboxylic acid dehydrogenase activity |
References for function | R Menzel and J Roth. (1981) Purification of the putA Gene Product--a bifunctional membrane-bounded protein from Salmonella Typhimurium responsible for the two-step oxidation of proline to glutamate. J. Biol. Chem. 256, 9755-9761.
R Menzel and J Roth. (1981) Enzymatic Properties of the Purified putA Protein from Salmonella typhimurium. J. Biol. Chem. 256, 9762-9766.
|
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 | DNA binding residue: 87-1113aa.
R.K. Singh, J.D. Lawson, W Zhu, et al. (2011) Small-angle X-Ray Scattering Studies of the Oligomeric State and Quaternary Structure of of the Trifunctional Proline Utilization A (PutA) Flavoprotein from Escherichia coli. J. Biol. Chem. 286, 43144-43153.
DNA binding domains: residue 1-47. Enzyme active sites: Tyr437, Trp438, Tyr552, Arg555, Arg556, Glu559. FAD binding: Ala371, Ala436, Gln404. Acetate ion binding: Arg 555, Arg556, Lys329.
M Zhang, TA White, JP Schuermann, et al. (2004) Structures of the Escherichia coli PutA Proline Dehydrogenase Domain in Complex with Competitive Inhibitors. Biochemistry. 43, 12539-12548.
Carboxylate bound: Lys 329, Arg 555, Arg 556. Ion pair network: Glu 559, Glu 289, Asp 370, Arg 431. Flavin ribityl binding: Arg 556, Glu 559. NADH binding: Arg 431. Lactase Hydroxyl binding: Asp 370, Tyr 540.
YH Lee, S Nadaraia, D Gu, et al. (2003) Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Nat. Struct. Biol. 10, 109-114.
FAD binding: Arg 431, Arg 556, Lys 329, Arg 555.
W Zhang, M Zhang, W Zhu, et al. (2007) Redox-Induced Changed in Flavin Structire and Roles of Flavin N(5) and the Ribityl 2'-OH Group in Regulating PutA-Membrane Binding. Biochemistry 46, 483-491.
FAD binding: Lys 329, Arg 431, Asp 370. (2010) The structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N-Propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction. Biochemistry. 49, 560-569. |
Function 2 |
Function description | transcriptional repressor of the put operon |
References for function | Ostrovsky de, Maloy S. PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator. Proc Natl Acad Sci U S A. 1993 May 1. PMID: 8483946.
Ostrovsky de, OBrien K, Maloy S. Regulation of proline utilization in Salmonella typhimurium: a membrane-associated dehydrogenase binds DNA in vitro. J Bacteriol. 1991 Jan. PMID: 1987118. |
E.C. number | N/A |
Location of functional site(s) | |
Cellular location of function | cytoplasm |
Comments | |