Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0K5L8 (SERC_BURCH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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:Bcen2424_1042
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length360 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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000058203

Regions

Region237 – 2382Pyridoxal 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
A0K5L8 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 4EE7A5902D6117F1

FASTA36039,289
        10         20         30         40         50         60 
MRVFNFSAGP AAMPEEVLRQ AADEMLDWHG SGMSVMEMSH RGKEFMSIHE AALTDLRDLL 

        70         80         90        100        110        120 
GVPASHRILF LQGGGIAENA IVPMNLLGAR KTADFVVTGS WSQKSFGEAK KFCAPHLAAS 

       130        140        150        160        170        180 
GKTEAGFTRA PARAEWQLSD DPAYVHLCTN ETIDGVETFE IPDLGDVPLV ADVSSHILSR 

       190        200        210        220        230        240 
PMDVAKYGVL FGGAQKNIGM AGVTVVIVRE DLLDRALSIC PSAFEWKTIA ANNSLYNTPP 

       250        260        270        280        290        300 
TYAIYIAGLV FQWLKRQGGL EAIEARNIEK SKLLYDTIDA SSFYLNKVEP AARSRMNVPF 

       310        320        330        340        350        360 
FLADETRNED FLAGAKARGL LQLKGHKSVG GMRASIYNAV PLEGVKALVE YMKDFEQRGA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI2424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000458 Genomic DNA. Translation: ABK07795.1.
RefSeqYP_834688.1. NC_008542.1.

3D structure databases

ProteinModelPortalA0K5L8.
SMRA0K5L8. Positions 2-359.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0K5L8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4451087.
GenomeReviewsGene locus Bcen2424_1042 in contig CP000458_GR.
KEGGbch:Bcen2424_1042.
PATRIC19059318. VBIBurCen15205_1042.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHBG289982.
OMAYEVLFLQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycBCEN331272:BCEN2424_1042-MONOMER.

Family and domain databases

HAMAPMF_00160. SerC_aminotrans_5.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_BURCH
AccessionPrimary (citable) accession number: A0K5L8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 41 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