Q1N7J3 · Q1N7J3_SPHSS

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 site791
Active site825

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

    • ORF names
      SKA58_11258

Organism names

  • Taxonomic identifier
  • Strain
    • SKA58
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas

Accessions

  • Primary accession
    Q1N7J3

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain17-64Proline utilization A proline dehydrogenase N-terminal
Domain72-183Proline dehydrogenase PutA
Domain192-490Proline dehydrogenase
Domain573-1009Aldehyde dehydrogenase

Sequence similarities

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
    1,199
  • Mass (Da)
    127,900
  • Last updated
    2006-05-30 v1
  • Checksum
    F84EEC1CF432A81D
MTDKPFAQFAPAIRQPTPLRQAITAAYRRDEAEALEPLIAAATVPDAMRDAIADTTRKLVTALRANRKGSGVEGLVQEYALSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGDWGAHLGGEKSLFVNAATWGLVVTGKLVGSVDDRGLGAALTRLVARAGEPVIRRGVDLAMRMMGEQFVTGETIQQALKRAKEMEAKGFAYSYDMLGEAATTAADARRYFADYERAIHAIGKASAGRGIYAGPGISIKLSALHPRYVRAQADRVMGELLPAVKQLALLSKRYDIGFNIDAEEADRLELSLDLLESLAGDPDLAGWNGLGFVVQGYGKRCPFVIDWIIDLARRSDRRIMVRLVKGAYWDAEIKRAQVDGLPDFPVYTRKVHTDVAYIACARKLVAARDVVFPQFATHNAQTLSSIYHLAGPDFSVGDYEFQCLHGMGEPLYEQVVGAEKLNRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIADPAVSIDDLIADPAEVVKAMPHPGARHHQIALPADLYPDRRNSDGLDLSDEAELARLGDALRESAQIAWTAAPEKASGPARTVFNPADHRDVVGRVTDATEADARAAVIRAAESRWPNSAVSDRAAMLEAAADAMQARMPILLGLIVREAGKSLPNAIAEVREAIDFLRYYARQAHATFGAQQQSLGPVVCISPWNFPLAIFTGQVAAALMAGNPVLAKPAEETPLIAAESVRLLHDAGVPADALQLLPGDGGIGAALVAAPETAAVMFTGSTEVARLIQRQLAPRLSRAGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALAELRIGRTDALSVDIGPVITAEARDGIIAHIDAMRAKGRGVEQSVLPPETAHGTFVAPTIIEIDGIADLEREVFGPVLHVLRFKREGLDALVDQINATGYGLTFGLHTRLDETIARVTSRAKVGNIYVNRNVIGAIVGVQPFGGRGLSGTGPKAGGPLYLGRLTTTPPVFAERVTHLRSPLHGFADWLDRQGEGEAAAQARRTGDASALGVELSLPGPVGERNLYALHPRGRVLMRPATRQGLFRQMAAILATGNHGVVQGMTLPADLPQDVAACFSTNESGPFAAALVEGDSAKIAATAQCVADMPGPIVPVHVDEHGQGYCLDWLLEEVSTSINTTAAGGNASLMMIG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAQG01000029
EMBL· GenBank· DDBJ
EAT06973.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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