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HAMAP rule MF_00160

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General rule information [?]

Accession MF_00160
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 45)
Name SerC_aminotrans_5
Templates P23721 (SERC_ECOLI); Q59196 (SERC_NIACI); P52878 (SERC_METBF); Q9RME2 (SERC_ALKAL); P80862 (SERC_BACSU): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Phosphoserine aminotransferase;
AltName: Full=Phosphohydroxythreonine aminotransferase;
Gene name

Comments [?]

Function Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic activity RHEA:14329: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
RHEA:16573: 2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
Cofactor pyridoxal 5'-phosphate
Note: Binds 1 pyridoxal phosphate per subunit.
Pathway Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
case not <OC:Bacillota>
Pathway Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
end case
Subunit Homodimer.
Subcellular location Cytoplasm.
Similarity Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Keywords [?]

case not <OC:Bacillota>
end case

Gene Ontology [?]

GO:0004648; Molecular function: O-phospho-L-serine:2-oxoglutarate aminotransferase activity.
GO:0030170; Molecular function: pyridoxal phosphate binding.
GO:0006564; Biological process: L-serine biosynthetic process.
case not <OC:Bacillota>
GO:0008615; Biological process: pyridoxine biosynthetic process.
end case
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF00266; Aminotran_5; 1;
NCBIfam TIGR01364; SerC_1; 1;

Features [?]

From: SERC_ECOLI (P23721)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING (Optional)     76     77       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326     [GA]-[RST]  
BINDING (Optional)     239     240       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326     N-T  
BINDING (Optional)     9     9       /ligand="L-glutamate" /ligand_id="ChEBI:CHEBI:29985     S  
BINDING (Optional)     42     42       /ligand="L-glutamate" /ligand_id="ChEBI:CHEBI:29985     R  
BINDING     102     102       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326     [WF]  
BINDING     153     153       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326     T  
BINDING (Optional)     174     174       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326     D  
BINDING     197     197       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326     Q  
MOD_RES     198     198       N6-(pyridoxal phosphate)lysine     K  

Additional information [?]

Size range 355-378 amino acids
Related rules None
Fusion None
Comments SerC is not involved in pyridoxine biosynthesis in B.subtilis, and probably also in other Bacillota. In these organisms, pyridoxal phosphate biosynthesis is achieved by an alternative pathway involving pdxS(yaaD) and pdxT(yaaE). SerC from Mycobacterium species are slightly divergent and could have a different activity.