A0A6N3IN21 · SDSL_RAT

  • Protein
    Serine dehydratase-like
  • Gene
    Sdsl
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha-ketobutyrate and pyruvate, respectively (PubMed:33079132).
Also exhibits racemase activity towards L-glutamate and D-glutamate (PubMed:33079132).

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Activity regulation

Serine dehydratase activity is inhibited by manganese chloride, ferrous chloride, cobalt chloride, cupric chloride, nickel chloride and zinc chloride. Glutamate racemase activity is inhibited by manganese chloride, ferrous chloride, cupric chloride and zinc chloride.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
27.6 mML-serine
6.13 mML-threonine
111 mML-glutamate
147 mMD-glutamate
kcat is 844 min-1 for L-serine and 152 min-1 for L-threonine.

pH Dependence

Optimum pH is 9.0 for serine dehydratase activity and 8.0 for glutamate racemase activity.

Temperature Dependence

Optimum temperature is 45 degrees Celsius at pH 8.3 for serine dehydratase and glutamate racemase activities.

GO annotations

AspectTerm
Molecular Functionglutamate racemase activity
Molecular Functionidentical protein binding
Molecular FunctionL-serine ammonia-lyase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionthreonine deaminase activity
Biological Processisoleucine biosynthetic process
Biological ProcessL-serine catabolic process
Biological Processlipid metabolic process
Biological Processthreonine catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Serine dehydratase-like
  • Alternative names
    • Glutamate racemase (EC:5.1.1.3
      ) . EC:5.1.1.3 (UniProtKB | ENZYME | Rhea)
    • L-serine deaminase (EC:4.3.1.17
      ) . EC:4.3.1.17 (UniProtKB | ENZYME | Rhea)
    • L-serine dehydratase/L-threonine deaminase
    • L-threonine dehydratase (TDH) (EC:4.3.1.19
      ) . EC:4.3.1.19 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      Sdsl
    • Synonyms
      Sdhl
      , Stdhgr

Organism names

  • Taxonomic identifier
  • Strain
    • Brown Norway
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    A0A6N3IN21
  • Secondary accessions
    • D3ZHV7

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00004605981-329Serine dehydratase-like
Modified residue48N6-(pyridoxal phosphate)lysine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Monomer (PubMed:33079132).
Homodimer (By similarity).

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    329
  • Mass (Da)
    34,953
  • Last updated
    2022-05-25 v1
  • Checksum
    1D73C02088ACD1BA
MEGASAECVRAEPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAKTVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEGRLSPALDSVVVIVCGGNNISSQQLQELKTQLNCS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LC552948
EMBL· GenBank· DDBJ
BCG52828.1
EMBL· GenBank· DDBJ
mRNA
CH473973
EMBL· GenBank· DDBJ
EDM13784.1
EMBL· GenBank· DDBJ
Genomic DNA
AABR07036392
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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