A0A7D5YCL4 · A0A7D5YCL4_9ACTN

Function

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Pathway

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

Features

Showing features for binding site.

130620406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site98substrate
Binding site133FAD (UniProtKB | ChEBI)
Binding site161FAD (UniProtKB | ChEBI)
Binding site185-187FAD (UniProtKB | ChEBI)
Binding site224-225FAD (UniProtKB | ChEBI)
Binding site286substrate
Binding site287substrate

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionnucleotide binding
Molecular Functionproline dehydrogenase activity
Biological Processproline catabolic process to glutamate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    proline dehydrogenase
  • EC number

Gene names

    • ORF names
      HZU44_25870

Organism names

  • Taxonomic identifier
  • Strain
    • Africana
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micromonosporales > Micromonosporaceae > Micromonospora

Accessions

  • Primary accession
    A0A7D5YCL4

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain42-297Proline dehydrogenase

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    306
  • Mass (Da)
    33,946
  • Last updated
    2020-12-02 v1
  • Checksum
    7593AB18F131B79A
MLRSVILAASRSSQVERLVATAPFTRDVVRRFVAGAGTDDALRATRELVADGLAVTLDNLGEDTVTGEQAIATRDEYLKLLTLLSDAGLTPAAEVSVKLSALGQRFDEQLAYDNARAICVAAEAAGTTVTLDMEDHTTTDSTLDTLARLRKDFPSTGAVLQAYLRRTESDCRELAYAGSRVRLCKGAYREPESVAYQAAREVDKSYVRCLNILMSGDGYPMLATHDPRLIAIGEDRARWFDRGPDRFEFQMLYGIRPEEQARLVGDGYTVRTYLPYGTDWYGYLMRRLAERPANLAFFGRALMSKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP058905
EMBL· GenBank· DDBJ
QLJ98113.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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