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A8YW78 (SERC_LACH4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoserine aminotransferase

EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT
Gene names
Name:serC
Ordered Locus Names:lhv_0048
OrganismLactobacillus helveticus (strain DPC 4571) [Complete proteome] [HAMAP]
Taxonomic identifier405566 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP MF_00160

Catalytic activity

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP MF_00160

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP MF_00160

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_00160

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160

Subunit structure

Homodimer By similarity. HAMAP MF_00160

Subcellular location

Cytoplasm By similarity HAMAP MF_00160.

Sequence similarities

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Serine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-serine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000071543

Regions

Region75 – 762Pyridoxal phosphate binding By similarity
Region236 – 2372Pyridoxal phosphate binding By similarity

Sites

Binding site411L-glutamate By similarity
Binding site1011Pyridoxal phosphate By similarity
Binding site1521Pyridoxal phosphate By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site1951Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1961N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8YW78 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 9090F84548F80786

FASTA37341,162
        10         20         30         40         50         60 
MTVYNFAAGP ATLPDPVIKQ IQEELPSLQG SGMSILEISH RSQMFDKIID TAKQDIKDLM 

        70         80         90        100        110        120 
HVPDNYHILF FQGGGTGQFA AVPMNLATKH KRIALLDSGH WATRAGDEAA NLGVTVDVLD 

       130        140        150        160        170        180 
STKDKHYQEL PHMPHAISAS DYDYLHITTN NTIEGTAYHT LPEHGDVTLV GDLSSNFMAE 

       190        200        210        220        230        240 
EYQVSDFGLI FGGVQKNLGP AGVTVVIVRD DLVNHVDHIP SILNYELFVK KNSMFNTPPV 

       250        260        270        280        290        300 
FAIYATGLVL KWLKQQGGIA GIEALNKKKS ALLYDFLDQS TLFHNDIKKT DRSLTNIPFK 

       310        320        330        340        350        360 
TTDPVLDKQV IAEADQAGLK NLKGHRSVGG LRASLYNAMP LAGVQALVDF LYNFEKQHKN 

       370 
NTMGKRYVSS KNI 

« Hide

References

[1]"Genome sequence of Lactobacillus helveticus: an organism distinguished by selective gene loss and IS element expansion."
Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K., McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F., Beresford T., Ross R.P.
J. Bacteriol. 190:727-735(2008) [PubMed: 17993529] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DPC 4571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000517 Genomic DNA. Translation: ABX26333.1.
RefSeqYP_001576620.1. NC_010080.1.

3D structure databases

ProteinModelPortalA8YW78.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8YW78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5772750.
GenomeReviewsGene locus lhv_0048 in contig CP000517_GR.
KEGGlhe:lhv_0048.
PATRIC22232068. VBILacHel91643_0051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289982.
OMAYEVLFLQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycLHEL405566:LHV_0048-MONOMER.

Family and domain databases

HAMAPMF_00160. SerC_aminotrans_5.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00831.
PANTHERPTHR21152:SF1. PTHR21152:SF1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01364. SerC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_LACH4
AccessionPrimary (citable) accession number: A8YW78
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families