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HAMAP rule MF_00160

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_00160
Accession MF_00160
Dates 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 46)
Name SerC_aminotrans_5
Scope(s) Bacteria
Archaea
Template(s) 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 Name=serC;

Comments [?]

FUNCTIONCatalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine.
CATALYTIC ACTIVITY Reaction=O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810, ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CATALYTIC ACTIVITY Reaction=4-(phosphooxy)-L-threonine + 2-oxoglutarate = (R)-3-hydroxy-2- oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452, ChEBI:CHEBI:58538; EC=2.6.1.52;
COFACTOR Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Note=Binds 1 pyridoxal phosphate per subunit.;
PATHWAYAmino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
case not <OC:Bacillota>
PATHWAYCofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
end case
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs 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 <OCellular component: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 76 77 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"		 [GA]-[RST]
BINDING 239 240 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"		 N-T
BINDING 9 9 /ligand="L-glutamate"
/ligand_id="ChEBI:CHEBI:29985"		 S
BINDING 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 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 /note="N6-(pyridoxal phosphate)lysine" K

Additional information [?]

Size range 355-378 amino acids
Related rules None
Fusion Nter: None Cter: 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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