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Q2L2T1 (SERC_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:BAV1348
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length376 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 – 376376Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000058201

Regions

Region253 – 2542Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1041Pyridoxal phosphate By similarity
Binding site1631Pyridoxal phosphate By similarity
Binding site1881Pyridoxal phosphate By similarity
Binding site2111Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2121N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2L2T1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: CA1412033AF11B5F

FASTA37640,575
        10         20         30         40         50         60 
MARPWNFSAG PSALPESVLQ QAAAEMLDWH GSGMSVMEMS HRGRQFVQIC DEAEADLREL 

        70         80         90        100        110        120 
MNVPADYAIM FMQGGGLGEN AIVPMNLIGR RGLPAADFVV TGHWSTRSHK EAGRYGDAQI 

       130        140        150        160        170        180 
AASSAQAVNI DGHEQRPFTW VPPLSDWRVR PEAAYLHLCS NETIGGVEFT EWPDLAAFGA 

       190        200        210        220        230        240 
PDVPLVVDAS SHFLSRPLDV TRTGLLFAGA QKNAGPAGVT VVIARRDLLG KALSICPSAF 

       250        260        270        280        290        300 
DYANVAAEHS RYNTPPTFAI YVAGLVYKWV KAQGGVQGLE AANKAKADLL YGYLDASGFY 

       310        320        330        340        350        360 
RNPVHPAVRS RMNVPFVLHD ESLNDAFLKG AEAAGLLALK GHKSVGGMRA SIYNAMPLAG 

       370 
VQALVDYLKE FERLHG 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ48957.1.
RefSeqYP_785870.1. NC_010645.1.

3D structure databases

HSSPHSSP built from PDB template 2C0R based on UniProtKB Q59196.
ProteinModelPortalQ2L2T1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2L2T1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6267140.
GenomeReviewsGene locus BAV1348 in contig AM167904_GR.
KEGGbav:BAV1348.
NMPDRfig|521.1.peg.520.
PATRIC21128888. VBIBorAvi43433_1367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289982.
OMAVPENYKV.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycABAU360910:BAV1348-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_BORA1
AccessionPrimary (citable) accession number: Q2L2T1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 46 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