EzCatDB: D00107
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DB codeD00107
CATH domainDomain 13.40.640.10 : Aspartate Aminotransferase; domain 2Catalytic domain
Domain 23.90.1150.10 : Aspartate Aminotransferase, domain 1
E.C.2.6.1.52
CSA1bjo

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

Enzyme Name
UniProtKBKEGG

Q59196P23721
Protein namePhosphoserine aminotransferasePhosphoserine aminotransferasephosphoserine 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
SynonymsEC 2.6.1.52
Phosphohydroxythreonine aminotransferase
PSAT
EC 2.6.1.52
Phosphohydroxythreonine aminotransferase
PSAT
RefSeq
NP_415427.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489179.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF00266 (Aminotran_5)
[Graphical view]
PF00266 (Aminotran_5)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism
MAP00750Vitamin B6 metabolism

UniProtKB:Accession NumberQ59196P23721
Entry nameSERC_BACCISERC_ECOLI
ActivityO-phospho-L-serine + 2-oxoglutarate = 3- phosphonooxypyruvate + L-glutamate.,4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.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.
SubunitHomodimer.Homodimer.
Subcellular locationCytoplasm (By similarity).Cytoplasm.
CofactorBinds 1 pyridoxal phosphate per subunit.Binds 1 pyridoxal phosphate per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00018C01005C00026C03232C00025
CompoundPyridoxal phosphateO-Phospho-L-serine2-Oxoglutarate3-PhosphonooxypyruvateL-Glutamate
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,phosphate group/phosphate ioncarbohydrate,carboxyl groupcarbohydrate,carboxyl group,phosphate group/phosphate ionamino acids,carboxyl group
ChEBI18405
15811
30915
30933
16015

PubChem1051
68841
57689797
51
105
88747398
44272391
33032

              
1bjnA01Bound:LLPUnboundUnboundUnboundUnboundUnbound
1bjnB01Bound:LLPUnboundUnboundUnboundUnboundUnbound
1bjoA01Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-GAM
1bjoB01Bound:LLPUnboundUnboundUnboundUnboundUnbound
1bt4A01Bound:PLPUnboundUnboundUnboundUnboundUnbound
1bjnA02UnboundUnboundUnboundUnboundUnboundUnbound
1bjnB02UnboundUnboundUnboundUnboundUnboundUnbound
1bjoA02UnboundUnboundUnboundUnboundUnboundUnbound
1bjoB02UnboundUnboundUnboundUnboundUnboundUnbound
1bt4A02UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1bjn, 1bjo & 1bt4
pdbCatalytic residuesCofactor-binding residuesModified residues
           
1bjnA01LLP 198
 
LLP 198(Pyridoxal-phosphorylation)
1bjnB01LLP 198
 
LLP 198(Pyridoxal-phosphorylation)
1bjoA01LYS 198
LYS 198(PLP binding)
 
1bjoB01LLP 198
LYS 198(PLP binding)
 
1bt4A01LYS 197
LYS 197(PLP binding)
 
1bjnA02 
 
 
1bjnB02 
 
 
1bjoA02 
 
 
1bjoB02 
 
 
1bt4A02 
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.842-843

references
[1]
PubMed ID10715213
JournalJ Mol Biol
Year2000
Volume297
Pages451-64
AuthorsKaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R
TitleCrystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly.
[2]
PubMed ID10637769
JournalIUBMB Life
Year1999
Volume48
Pages525-9
AuthorsBasurko MJ, Marche M, Darriet M, Cassaigne A
TitlePhosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID99150428
PubMed ID10024454
JournalJ Mol Biol
Year1999
Volume286
Pages829-50
AuthorsHester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN
TitleCrystal 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 UniProtKBP23721
[4]
CommentsCRYSTALLIZATION
Medline ID96416269
PubMed ID8819175
JournalProtein Sci
Year1996
Volume5
Pages1426-8
AuthorsMoser M, Muller R, Battchikova N, Koivulehto M, Korpela T, Jansonius JN
TitleCrystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus.
Related UniProtKBQ59196


createdupdated
2004-03-182009-02-26


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