A0A2S3X785 · A0A2S3X785_PSEPU

Function

function

Oxidizes proline to glutamate for use as a carbon and nitrogen source.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site881
Active site915

GO annotations

AspectTerm
Cellular Componentcytoplasmic side of plasma membrane
Molecular Function1-pyrroline-5-carboxylate dehydrogenase activity
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionproline dehydrogenase activity
Biological Processproline biosynthetic process
Biological Processproline catabolic process to glutamate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional protein PutA

Including 2 domains:

  • Recommended name
    Proline dehydrogenase
  • EC number
  • Alternative names
    • Proline oxidase
  • Recommended name
    Delta-1-pyrroline-5-carboxylate dehydrogenase
  • EC number
  • Short names
    P5C dehydrogenase
  • Alternative names
    • L-glutamate gamma-semialdehyde dehydrogenase

Gene names

    • Name
      putA
    • ORF names
      BGP84_14960

Organism names

Accessions

  • Primary accession
    A0A2S3X785

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain11-43PutA RHH
Domain87-134Proline utilization A proline dehydrogenase N-terminal
Domain146-257Proline dehydrogenase PutA
Domain267-567Proline dehydrogenase
Compositional bias642-660Polar residues
Region642-664Disordered
Domain657-1101Aldehyde dehydrogenase

Sequence similarities

Belongs to the aldehyde dehydrogenase family.
In the C-terminal section; belongs to the aldehyde dehydrogenase family.
In the N-terminal section; belongs to the proline dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,311
  • Mass (Da)
    142,580
  • Last updated
    2018-07-18 v1
  • Checksum
    0A4D2F7E090FAB7A
MATTTLGVKLDDAIRERLKQAAQHIAQTPHWMIKQAIFNYLEQIESGVTPAQQSGLAAVAGDEQPEHLDERALQVFLDFAESILPQSVLRAAITAAYRRPEADAIPMLLEQARQPAEMAKASHQLAYSIAQKLRNQKSAGGRQGLVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKIANGNWSQHLGRSPSTFVNAASWGLLITGKLVSTHNETGLSSSLNRIISKRGEPLIRKGVDMAMRLMGEQFVTGETIGEALANAARREAKGFRYSYDMLGEAALTEHDAQNYLAAYEQAIHAIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYVIDYVIDLAKRSRHRLMIRLVKGAYWDSEIKRAQIDGLEGYPVYTRKVYTDLSYIACARKLLSVPEAIYPQFATHNAHSLAAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVDNVADGKLNRPCRIYAPVGSHETLLAYLVRRLLENGANTSFVNRIADRSISLDELVEDPVLQVEKMAAQEGALGLPHPRIALARNLYGGTRLNSSGLDLSNEHRLGSLASALLASANQPYTAGPTASNDSSHPRTVSAVRNPADHRDLIGQVYEANESDVRNAILCAQASGPIWQSTLPAERAAILERAADLMESEMQQLMGLLVRESGKTFSNAIAEVREAVDFLRYYGAQAASFSNDSHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILHQAGVPTSVVQLLPGRGETVGASLVGDSRIRGVMFTGSTEVAGILSRNLAGRLDGQGQTLPLIAETGGMNAMIVDSSALAEQVVVDVISSAFDSAGQRCSALRVLCVQADVADHVCQMLRGAMAEYRVGSPERLDTDIGPVIDREARDNIVNHIEHMRRKGRSVFQAARADGQLLQRGTFVLPTLIELDSLDELEREIFGPVLHVVRYQRSQLNELLEQINASGYGLTLGVHTRIDETIAQVVETARVGNLYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPHDAVAQALADGDGHAVAAPTDLQNARKAFAAWAEQTEPGIANLFARYLQQSQSYTTHLLAGPTGERNSYTLLPREVVLNLAENRLDLLAQLAACLAVGSRVLWLDSHNTLRAQLPAAVQARIDSISDWTDPQARFDAILHHGDSDQLRYVSQLSARRRGAIVGVHGLGRADTDIPLERLLIEHALSVNTAAAGGNANLMTIC

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias642-660Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MINH01000019
EMBL· GenBank· DDBJ
POG10968.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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