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Q66CI9 (SERC_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:YPTB1414
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length361 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-Rule MF_00160

Catalytic activity

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

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

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_00160

Pathway

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

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP-Rule MF_00160

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00160

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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 – 361361Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150228

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region238 – 2392Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1531Pyridoxal phosphate By similarity
Binding site1731Pyridoxal phosphate By similarity
Binding site1961Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1971N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66CI9 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 4A55EE9512240F38

FASTA36139,991
        10         20         30         40         50         60 
MTQVYNFSAG PAMLPVEVLR RAEQELRNWH GLGTSVMEIS HRSKEFMQVA EESEKDLRDL 

        70         80         90        100        110        120 
LQIPANYKVL FCHGGARAQF AAVPLNLLGD SNSADYIDGG YWAHSAVKEA QKYCTPHVID 

       130        140        150        160        170        180 
VTTHDNGLTG IQPMKQWKLS DNAAYVHYCP NETIDGVAIN EQPDFGNKVV VADYSSAILS 

       190        200        210        220        230        240 
RPIDISRYGV IYAGAQKNIG PAGLTLVIVR EDLLGKAHTA LPSILDYKVL ADNDSMFNTP 

       250        260        270        280        290        300 
PTFAWYLSGL VFKWLKEQGG LGEMEKRNQA KAELLYGAID RTGFYRNQVA IANRSWMNVP 

       310        320        330        340        350        360 
FQMAEASLDK LFLSEAEAQG LQALKGHRVA GGMRASIYNA MPIEGVKALT DFMADFERRH 


G 

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References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH20654.1.
RefSeqYP_069945.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66CI9.
SMRQ66CI9. Positions 3-361.
ModBaseSearch...

Protein-protein interaction databases

STRING273123.YPTB1414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH20654; CAH20654; YPTB1414.
GeneID2956596.
KEGGyps:YPTB1414.
PATRIC18641415. VBIYerPse22266_1775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHOG000088965.
KOK00831.
OMAKPMKEWQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-1485-MONOMER.
UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00160. SerC_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
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_YERPS
AccessionPrimary (citable) accession number: Q66CI9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 11, 2004
Last modified: May 29, 2013
This is version 67 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