DB code: D00107

CATH domain 3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
3.90.1150.10 : Aspartate Aminotransferase, domain 1
E.C. 2.6.1.52
CSA 1bjo
M-CSA 1bjo
MACiE

CATH domain Related DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00102 D00103 D00104 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00103 D00104 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
Q59196 Phosphoserine aminotransferase
EC 2.6.1.52
Phosphohydroxythreonine aminotransferase
PSAT
PF00266 (Aminotran_5)
[Graphical View]
P23721 Phosphoserine aminotransferase
EC 2.6.1.52
Phosphohydroxythreonine aminotransferase
PSAT
PF00266 (Aminotran_5)
[Graphical View] 		NP_415427.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489179.1 (Protein)
NC_007779.1 (DNA/RNA sequence)

KEGG enzyme name
phosphoserine transaminase
PSAT
phosphoserine aminotransferase
3-phosphoserine aminotransferase
hydroxypyruvic phosphate-glutamic transaminase
L-phosphoserine aminotransferase
phosphohydroxypyruvate transaminase
phosphohydroxypyruvic-glutamic transaminase
3-O-phospho-L-serine:2-oxoglutarate aminotransferase
SerC
PdxC
3PHP transaminase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q59196 SERC_BACCI O-phospho-L-serine + 2-oxoglutarate = 3- phosphonooxypyruvate + L-glutamate. 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. Homodimer. Cytoplasm (By similarity). Binds 1 pyridoxal phosphate per subunit.
P23721 SERC_ECOLI O-phospho-L-serine + 2-oxoglutarate = 3- phosphonooxypyruvate + L-glutamate. 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. Homodimer. Cytoplasm. Binds 1 pyridoxal phosphate per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00260 Glycine, serine and threonine metabolism
MAP00750 Vitamin B6 metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C01005 C00026 C03232 C00025
E.C.
Compound Pyridoxal phosphate O-Phospho-L-serine 2-Oxoglutarate 3-Phosphonooxypyruvate L-Glutamate
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,phosphate group/phosphate ion carbohydrate,carboxyl group carbohydrate,carboxyl group,phosphate group/phosphate ion amino acids,carboxyl group
ChEBI 18405
 18405
 		15811
 15811
 		30915
 30915
 		30933
 30933
 		16015
 16015
PubChem 1051
 1051
 		57689797
 68841
 57689797
 68841
 		51
 51
 		105
 105
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
1bjnA01 Bound:LLP Unbound Unbound Unbound Unbound Unbound
1bjnB01 Bound:LLP Unbound Unbound Unbound Unbound Unbound
1bjoA01 Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:PLP-GAM
1bjoB01 Bound:LLP Unbound Unbound Unbound Unbound Unbound
1bt4A01 Bound:PLP Unbound Unbound Unbound Unbound Unbound
1bjnA02 Unbound Unbound Unbound Unbound Unbound Unbound
1bjnB02 Unbound Unbound Unbound Unbound Unbound Unbound
1bjoA02 Unbound Unbound Unbound Unbound Unbound Unbound
1bjoB02 Unbound Unbound Unbound Unbound Unbound Unbound
1bt4A02 Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1bjn, 1bjo & 1bt4

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bjnA01 LLP 198 LLP 198(Pyridoxal-phosphorylation)
1bjnB01 LLP 198 LLP 198(Pyridoxal-phosphorylation)
1bjoA01 LYS 198 LYS 198(PLP binding)
1bjoB01 LLP 198 LYS 198(PLP binding)
1bt4A01 LYS 197 LYS 197(PLP binding)
1bjnA02
1bjnB02
1bjoA02
1bjoB02
1bt4A02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.842-843

References
[1]
Resource
Comments
Medline ID
PubMed ID 10715213
Journal J Mol Biol
Year 2000
Volume 297
Pages 451-64
Authors Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R
Title Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 10637769
Journal IUBMB Life
Year 1999
Volume 48
Pages 525-9
Authors Basurko MJ, Marche M, Darriet M, Cassaigne A
Title Phosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 99150428
PubMed ID 10024454
Journal J Mol Biol
Year 1999
Volume 286
Pages 829-50
Authors Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN
Title Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate.
Related PDB
Related UniProtKB P23721
[4]
Resource
Comments CRYSTALLIZATION
Medline ID 96416269
PubMed ID 8819175
Journal Protein Sci
Year 1996
Volume 5
Pages 1426-8
Authors Moser M, Muller R, Battchikova N, Koivulehto M, Korpela T, Jansonius JN
Title Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus.
Related PDB
Related UniProtKB Q59196

Comments

Created Updated
2004-03-18 2009-02-26