AC   MF_00160;
DC   Protein; auto
TR   HAMAP; MF_00160; -; 1; level=0
XX
Names: SerC_aminotrans_5
XX
ID   SERC
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
DE            Short=PSAT;
GN   Name=serC;
XX
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC         L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC         oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC         ChEBI:CHEBI:58538; EC=2.6.1.52;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC       Note=Binds 1 pyridoxal phosphate per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3.
case not <OC:Bacillota>
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
XX
DR   Pfam; PF00266; Aminotran_5; 1; trigger=no
DR   NCBIfam; TIGR01364; SerC_1; 1; trigger=no
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Serine biosynthesis
case not <OC:Bacillota>
KW   Pyridoxine biosynthesis
end case
KW   Transferase
KW   Aminotransferase
KW   Pyridoxal phosphate
XX
GO   GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity
GO   GO:0030170; F:pyridoxal phosphate binding
GO   GO:0006564; P:L-serine biosynthetic process
case not <OC:Bacillota>
GO   GO:0008615; P:pyridoxine biosynthetic process
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: SERC_ECOLI (P23721)
FT   BINDING         76..77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: [GA]-[RST]
FT   BINDING         239..240
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: N-T
FT   BINDING         9
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: S
FT   BINDING         42
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   Optional; Condition: R
FT   BINDING         102
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [WF]
FT   BINDING         153
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: T
FT   BINDING         174
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: D
FT   BINDING         197
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Q
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 355-378;
Related: None;
Template: P23721; Q59196; P52878; Q9RME2; P80862;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.45 2023/06/01
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