ExPASy Proteomics Server

Accession	MF_00160
Dates	1-JUN-2001 (Created) 25-NOV-2009 (Last updated, Version 35)

Data class

Protein

Predictors

HAMAP; MF_00160; [distribution of match scores in UniProtKB];[seed alignment for MF_00160]

Names

SerC_aminotrans_5

Identifier

SERC

Protein name

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

Gene name

serC

FUNCTION: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).

CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate.

CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.

COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).

PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.

PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.

SUBUNIT: Homodimer (By similarity).

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Pfam	PF00266; Aminotran_5; 1;
TIGRFAMs	TIGR01364; serC_1; 1;
PROSITE	PS00595; AA_TRANSFER_CLASS_5; 1;

Cytoplasm, Amino-acid biosynthesis, Serine biosynthesis.

Pyridoxine biosynthesis.

Transferase, Aminotransferase, Pyridoxal phosphate.

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.

GO:0008615; Biological process: pyridoxine biosynthetic process.

GO:0005737; Cellular component: cytoplasm.

From: SERC_ECOLI (P23721)
Key		From		To		Description		Condition		FTGroup
REGION (Optional)		76		77		Pyridoxal phosphate binding (By similarity)		[GA]-[RST]
REGION (Optional)		239		240		Pyridoxal phosphate binding (By similarity)		N-T
BINDING (Optional)		9		9		L-glutamate (By similarity)		S
BINDING (Optional)		42		42		L-glutamate (By similarity)		R
BINDING		102		102		Pyridoxal phosphate (By similarity)		[WF]
BINDING		153		153		Pyridoxal phosphate (By similarity)		T
BINDING (Optional)		174		174		Pyridoxal phosphate (By similarity)		D
BINDING		197		197		Pyridoxal phosphate (By similarity)		Q
MOD_RES		198		198		N6-(pyridoxal phosphate)lysine (By similarity)		K

Size range:	355-378 amino acids
Related UniRules:	None
Template:	P23721 (SERC_ECOLI); Q59196 (SERC_BACCI); P52878 (SERC_METBF); Q9RME2 (SERC_BACAO); P80862 (SERC_BACSU): [Recover all]
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	None
Plasmid encoded:	None
Comments:	SerC is not involved in pyridoxine biosynthesis in B.subtilis, and probably also in other Firmicutes. 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.