A0A6N3IN21 · SDSL_RAT
- ProteinSerine dehydratase-like
- GeneSdsl
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids329 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Also exhibits racemase activity towards L-glutamate and D-glutamate (PubMed:33079132).
Catalytic activity
- L-serine = NH4+ + pyruvate
Cofactor
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 mM | L-serine | |||||
6.13 mM | L-threonine | |||||
111 mM | L-glutamate | |||||
147 mM | D-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
Aspect | Term | |
---|---|---|
Molecular Function | glutamate racemase activity | |
Molecular Function | identical protein binding | |
Molecular Function | L-serine ammonia-lyase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | threonine deaminase activity | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | L-serine catabolic process | |
Biological Process | lipid metabolic process | |
Biological Process | threonine catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSerine dehydratase-like
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionA0A6N3IN21
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000460598 | 1-329 | Serine dehydratase-like | |||
Sequence: MEGASAECVRAEPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAKTVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEGRLSPALDSVVVIVCGGNNISSQQLQELKTQLNCS | ||||||
Modified residue | 48 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Monomer (PubMed:33079132).
Homodimer (By similarity).
Homodimer (By similarity).
Structure
Sequence
- Sequence statusComplete
- Length329
- Mass (Da)34,953
- Last updated2022-05-25 v1
- Checksum1D73C02088ACD1BA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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. |