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Reviewed, UniProtKB/Swiss-Prot B6J1E0 (SERC_COXB2)

Last modified October 13, 2009. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: CbuG_1469
OrganismCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP]
Taxonomic identifier434923 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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.

Subcellular location

Cytoplasm By similarity.

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_1000097211

Regions

Region237 – 2382Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1521Pyridoxal phosphate By similarity
Binding site1711Pyridoxal phosphate By similarity
Binding site1941Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1951N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J1E0-1 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 55E5E8CD3E321336

FASTA36040,645
        10         20         30         40         50         60 
MSRVYNFSAG PAAIPEEVLF TVRDELLDWH GIGMSIAEVS HRGEEFIGVA EEAERDLREL 

        70         80         90        100        110        120 
LAVPESYHIL FLQGGSRLQF AMVPMNLLAN HKKAVYIDSG VWSNLAIREA KNYCDPHLAT 

       130        140        150        160        170        180 
NAKELNYTGI PDQATWDMPN EAAYFYYVDN ETVNGIEFPF IPDTDLTLVC DMSSNLLSRP 

       190        200        210        220        230        240 
FDVSRYGLIF ACAQKNMGLA GLTIVIVHDD LLKRSPLPTT PSYLQYALHA KERSFINTPP 

       250        260        270        280        290        300 
TFAWYLAGLI FKWVKNQGGV AVLAERNQRK AAKLYKFIDK SNFFDNPINP TYRSRMNVIF 

       310        320        330        340        350        360 
RLADERLNSL FLKEATENGL ANLKGHRLLG GMRASIYNAM TEEGVDALIN FMGQFEKRHG 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed: 19047403] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001019 Genomic DNA. Translation: ACJ18768.1.
RefSeqYP_002303913.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7013885.
GenomeReviewsGene locus CbuG_1469 in contig CP001019_GR.
KEGGcbg:CbuG_1469.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00160.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR003248. Pser_amintransf.
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.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_COXB2
AccessionPrimary (citable) accession number: B6J1E0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: October 13, 2009
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents