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Literature summary extracted from

  • Lee, Y.H.; Nadaraia, S.; Gu, D.; Becker, D.F.; Tanner, J.J.
    Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein (2003), Nat. Struct. Biol., 10, 109-114.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.5.2 hanging drop method Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.5.2 L-proline + acceptor + H2O Escherichia coli PutA flavoprotein plays multiple roles in proline catabolism by functioning as a membrane-associated bi-functional enzyme and a transcriptional repressor of proline utilization genes (S)-1-pyrroline-5-carboxylate + reduced acceptor
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.5.2 Escherichia coli P09546 PutA669, corresponding to the N-terminal 669 residues of the 1320-amino acid PutA polypeptide chain
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.5.2 L-proline + acceptor + H2O PutA flavoprotein plays multiple roles in proline catabolism by functioning as a membrane-associated bi-functional enzyme and a transcriptional repressor of proline utilization genes Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
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 ?

Subunits

EC Number Subunits Comment Organism
1.5.5.2 dimer domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a beta/alpha-barrel PRODH domain with a bound lactate inhibitor Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.5.5.2 PutA flavoprotein
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 Escherichia coli