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putA fused DNA-binding transcriptional repressor/proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase PutA [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945600, updated on 30-Jul-2025
Official Symbol
putA
Official Full Name
fused DNA-binding transcriptional repressor/proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase PutA
Primary source
ECOCYC:EG10801
Locus tag
b1014
See related
ASAP:ABE-0003424
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1005; poaA; putC
Summary
PutA is a multifunctional membrane-associated flavoprotein involved in proline catabolism: the central proline dehydrogenese domain feeds its product to the C-terminal Delta(1)-pyrroline-5-carboxylate dehydrogenese domain, to produce glutamate. [More information is available at EcoGene: EG10801]. The PutA protein is a bifunctional enzyme and a transcriptional repressor of the put (proline utilization) regulon and belongs to the PutA family. [More information is available at EcoCyc: EG10801].
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Sequence:
NC_000913.3 (1074920..1078882, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ureidoacrylate amidohydrolase Neighboring gene pyrimidine monooxygenase RutA Neighboring gene DNA-binding transcriptional regulator RutR Neighboring gene protein YmdG Neighboring gene proline:Na(+) symporter

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline. Brown ED, et al. J Biol Chem, 1993 Apr 25. PMID 8473341
  2. Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA. Baban BA, et al. Biochim Biophys Acta, 2004 Sep 1. PMID 15450175
  3. Detection of L-lactate in polyethylene glycol solutions confirms the identity of the active-site ligand in a proline dehydrogenase structure. Zhang M, et al. Acta Crystallogr D Biol Crystallogr, 2004 May. PMID 15103160, Free PMC Article
  4. Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli. Zhu W, et al. Biochemistry, 2003 May 13. PMID 12731889
  5. Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Lee YH, et al. Nat Struct Biol, 2003 Feb. PMID 12514740, Free PMC Article

See all (54) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Deletion of the C-terminal motif (CCM) or replacement of hydrophobic residues with negatively charged residues within the CCM impairs EcPutA functional and physical membrane association
    Title: Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A.
  2. crystal structures of the proline dehydrogenase domain mutants PutA86-630D370N and PutA86-630D370A complexed with the proline analogue show that the mutations cause only minor perturbations to the active site but no major structural changes
    Title: Involvement of the β3-α3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A.
  3. Data show that PutA is a symmetric V-shaped dimer having dimensions of 205 x 85 x 55 A. The particle consists of two large lobes connected by a 30-A diameter cylinder
    Title: Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli.
  4. kinetic data, along with analysis of crystal structure data for the PRODH domain, suggest that the proline:ubiquinone oxidoreductase reaction occurs via a rapid equilibrium ping-pong mechanism with proline and ubiquinone binding at two distinct sites
    Title: Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli.
  5. analysis of metabolism and gene expression in the proline utilization A protein from Escherichia coli [review]
    Title: Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli.
  6. From this study it is clear that reduction of flavin adenine dinucleotide bound to the proline dehydrogenase active site of PutA elicits global conforamtional changes that direct PutA-membrane associations.
    Title: Regulation of PutA-membrane associations by flavin adenine dinucleotide reduction.
  7. identify molecular interactions in the PutA active site that underlie redox-dependent functional switching of PutA
    Title: Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding.
  8. The proline dehydrogenase (PRODH)/L-tetrahydro-2-furoic acid complex is the first structure of PRODH with a five-membered ring proline analogue bound in the active site.
    Title: Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables DNA-binding transcription factor activity IEA
Inferred from Electronic Annotation
more info
  
enables DNA-binding transcription repressor activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA-binding transcription repressor activity IEA
Inferred from Electronic Annotation
more info
  
enables L-glutamate gamma-semialdehyde dehydrogenase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables L-glutamate gamma-semialdehyde dehydrogenase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables L-glutamate gamma-semialdehyde dehydrogenase activity IEA
Inferred from Electronic Annotation
more info
  
enables anion binding IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables cis-regulatory region sequence-specific DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables flavin adenine dinucleotide binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables heterocyclic compound binding IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables proline dehydrogenase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables proline dehydrogenase activity IEA
Inferred from Electronic Annotation
more info
  
enables proline dehydrogenase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables sequence-specific DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables transcription cis-regulatory region binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in L-proline catabolic process to L-glutamate IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in L-proline catabolic process to L-glutamate IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within L-proline catabolic process to L-glutamate IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within negative regulation of DNA-templated transcription IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proline metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of DNA-templated transcription IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within response to oxidative stress IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasmic side of membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytoplasmic side of plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasmic side of plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
fused DNA-binding transcriptional repressor/proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase PutA
NP_415534.1

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1074920..1078882 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415534.1 fused DNA-binding transcriptional repressor/proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase PutA

    See identical proteins and their annotated locations for NP_415534.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A6N8QZP8, A0A8T5ZYY9
    Conserved Domains (1) summary
    PRK11809
    Location:1 → 1320
    putA; trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Nucleotide Protein
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