HAMAP rule MF_00160

General rule information [?]

Accession	MF_00160
Dates	1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 45)

Name	SerC_aminotrans_5

Scope

Bacteria

Archaea

Templates

P23721 (SERC_ECOLI); Q59196 (SERC_NIACI); P52878 (SERC_METBF); Q9RME2 (SERC_ALKAL); P80862 (SERC_BACSU): [Recover all]

Triggered by

HAMAP; MF_00160 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier

SERC

Protein name

RecName:		Full=Phosphoserine aminotransferase;
		EC 2.6.1.52;
AltName:		Full=Phosphohydroxythreonine aminotransferase;
		Short=PSAT;

Gene name

serC

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 EC 2.6.1.52
	RHEA:16573: 2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate EC 2.6.1.52
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 [?]

Cytoplasm
Amino-acid biosynthesis
Serine biosynthesis

case not <OC:Bacillota>

Pyridoxine biosynthesis

end case

Transferase
Aminotransferase
Pyridoxal phosphate

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;
PROSITE	PS00595; AA_TRANSFER_CLASS_5; 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.

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