Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q734W9 (SERC_BACC1)

Last modified November 3, 2009. Version 46. 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: BCE_3285
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Phosphoserine aminotransferase HAMAP MF_00160
PRO_0000150144

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region237 – 2382Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal 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
Q734W9-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: AFFE549F454CA691

FASTA36040,330
        10         20         30         40         50         60 
MERVYNFSAG PSILPLPVLE KVQKELVNYN GTGMSIMEMS HRSSYFQSII DEAGSLLREL 

        70         80         90        100        110        120 
MNIPDEYEVL FLQGGASLQF SMIPLNVMNT YKKAGYILTG SWSKKAMQEA EKVGEVQVIA 

       130        140        150        160        170        180 
SSENEKFTTI PRLDGLLGDE KLDYVHITTN NTIEGTKYVD IPHVDKVPLV ADMSSNILSE 

       190        200        210        220        230        240 
RYDVSKFGLI YAGAQKNLGP AGLTIAIIKR DLIGGADRSC PTMLNYETYS KNNSLYNTPP 

       250        260        270        280        290        300 
SFSIYVTKLV LEWLKEQGGV SAIEEQNRMK SSLLYNFLDE SKLFTSPVDP TYRSLMNIPF 

       310        320        330        340        350        360 
TTPSEELNSE FLQKAKERGL VTLKGHRSVG GMRASIYNAM PAEGVQQLVN YMKEFELENR 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017194 Genomic DNA. Translation: AAS42193.1.
RefSeqNP_979585.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ734W9.

Genome annotation databases

GeneID2748348.
GenomeReviewsGene locus BCE_3285 in contig AE017194_GR.
KEGGbca:BCE_3285.
NMPDRfig|222523.1.peg.3257.
TIGRBCE_3285.

Phylogenomic databases

HOGENOMQ734W9.
OMASMYNTPP.

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]
ProDomPD001544. Pser_amintransf. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_BACC1
AccessionPrimary (citable) accession number: Q734W9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 46 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