Protein Information

General Information
MoonProt ID136
First appeared in release1.0
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 IDP10503 (PUTA_SALTY), Reviewed
GO termsGO: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 GO:0003677 DNA binding GO:0006355 regulation of transcription, DNA-templated
Organisms for which functions have been demonstratedSalmonella typhimurium
Sequence length1320
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
Quaternary structure
Function 1
Function descriptionProline dehydrogenase / Proline oxidase pyrroline-5-carboxylic acid dehydrogenase activity
References for functionR 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. number1.5.5.2 and 1.2.1.88
Location of functional site(s)Active site:883,917
Cellular location of functionCytoplasmic side of membrane, peripheral membrane protein
CommentsDNA 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 descriptiontranscriptional repressor of the put operon
References for functionOstrovsky 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. numberN/A
Location of functional site(s)
Cellular location of functioncytoplasm
Comments