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A9A0A5 (SERC_DESOH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Dole_3221
OrganismDesulfococcus oleovorans (strain DSM 6200 / Hxd3) [Complete proteome] [HAMAP]
Taxonomic identifier96561 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfococcus

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 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 – 361361Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000097213

Regions

Region77 – 782Pyridoxal phosphate binding By similarity
Region237 – 2382Pyridoxal phosphate binding By similarity

Sites

Binding site431L-glutamate By similarity
Binding site1031Pyridoxal 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
A9A0A5 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 3B94FD99417DBB95

FASTA36139,461
        10         20         30         40         50         60 
MSKRIYNFNP GPAALPLSVL EEIQATFLDF AGTGMSITEV SHRSKPFDAI INDAVTRVKR 

        70         80         90        100        110        120 
LLGIGDDFKV LFVQGGASMQ FAMVPMNLLP DGKSADYVNT GTWSTKAIKE TKILGKTVNV 

       130        140        150        160        170        180 
AASSEDRNFA YIPKELSLDP NAAYVHITSN NTIKGTQWAD FPDTKGVPIV SDMSSDILSR 

       190        200        210        220        230        240 
PLDMSKFGLI YAGAQKNIGP AGVCMVIVKN DLLEKANTGL PSMLAYKTYA DSNSLYNTPP 

       250        260        270        280        290        300 
CFTIYAIDLV LKWLEETIGG LEKMDAVNRE KAALLYDLFD ASSFYNGTAD ADSRSLMNVT 

       310        320        330        340        350        360 
FRLPSEDLEK RFVEEATKND LGGLKGHRSV GGCRASIYNA MSMEGIQALV DFMKEFERTN 


G 

« Hide

References

[1]"Complete sequence of Desulfococcus oleovorans Hxd3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Wawrik B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6200 / Hxd3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000859 Genomic DNA. Translation: ABW69024.1.
RefSeqYP_001531101.1. NC_009943.1.

3D structure databases

ProteinModelPortalA9A0A5.
SMRA9A0A5. Positions 2-361.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9A0A5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5696083.
GenomeReviewsGene locus Dole_3221 in contig CP000859_GR.
KEGGdol:Dole_3221.
PATRIC21696681. VBIDesOle35880_3334.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289982.
OMAYEVLFLQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycDOLE96561:DOLE_3221-MONOMER.

Family and domain databases

HAMAPMF_00160. SerC_aminotrans_5.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_DESOH
AccessionPrimary (citable) accession number: A9A0A5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 35 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