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InterPro: IPR015659 Proline oxidase

Protein matchesHelp
UniProtKB
Matches:
262 proteins
AccessionHelp IPR015659 Proline_oxidase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR002872 Proline dehydrogenase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

In bacterial proline degradation, proline is converted to glutamate. Proline oxidase (PutA) is a flavin containing bifunctional enzyme (EC:1.5.99.8) that catalyzes the oxidation of proline to pyrroline-5-carboxylate and is a transcriptional repressor of the genes in the proline biosynthetic pathway. Its human homologue is involved in p53 mediated apoptosis. The structure of PutA is a dimer with each subunit containing three domains 1) a helical dimerisation arm, 2) a three helix bundle similar to the DNA-binding helix-turn-helix domain and 3) a beta/alpha barrel domain with [1] proline oxidase activity.

Database linksHelp
Enzyme: EC:1.5.99.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR015659 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O43272 Proline dehydrogenase, mitochondrial

O45228 Proline dehydrogenase, mitochondrial

P09368 Proline dehydrogenase, mitochondrial

Q04499 Proline dehydrogenase, mitochondrial

Q8VCZ9 Probable proline dehydrogenase 2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002872 Proline dehydrogenase
IPR011992 EF-hand-like domain
IPR015659 Proline oxidase
SWISS-MODEL
ModBase

PublicationsHelp
1. Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ.
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein.
Nat. Struct. Biol. 10 109-14 2003 [PubMed: 12514740]
http://dx.doi.org/10.1038/nsb885

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InterPro 23.1