Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6WNN5 (SERC_SHEB8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Shew185_2286
OrganismShewanella baltica (strain OS185) [Complete proteome] [HAMAP]
Taxonomic identifier402882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length363 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Pyridoxine 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: UniProtKB-HAMAP

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionO-phospho-L-serine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_1000203564

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region240 – 2412Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1561Pyridoxal phosphate By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site1981Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6WNN5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 11AE5917C9F11260

FASTA36339,932
        10         20         30         40         50         60 
MSAIYNFCAG PAMLPAAVMK KAQQELLDWN GQGVSVMEIS HRSKEFIALT QQAESDLREL 

        70         80         90        100        110        120 
MQIPTNYHVL FMHGGGRGQF SAVVNNFLGN HGRALYLVSG QWSSAALAEA QKLVGEAQID 

       130        140        150        160        170        180 
SLNIVEKHNG LNAVVLPDLH KIDADYRYVH YCPNETVDGI EIFDELDSPW PIVADLSSTI 

       190        200        210        220        230        240 
MSREIDVSRY GLIYAGAQKN IGPSGLSIVI VRDDMLKLPS LPQSSIMDYR LAVEHDSMFN 

       250        260        270        280        290        300 
TPPTFAWYLA AEVFAWLKST GGISSIAKIN QQKAQMLYQC IDGNAFYRNG VVAANRSQMN 

       310        320        330        340        350        360 
VTFQLVNEAL DGEFLKQAQI AGLVALKGHR IVGGMRASLY NAMPLDGIVA LVKFMNEFAA 


KHS 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS185."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS185.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000753 Genomic DNA. Translation: ABS08424.1.
RefSeqYP_001366487.1. NC_009665.1.

3D structure databases

ProteinModelPortalA6WNN5.
SMRA6WNN5. Positions 3-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402882.Shew185_2286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS08424; ABS08424; Shew185_2286.
GeneID5372307.
KEGGsbm:Shew185_2286.
PATRIC23461383. VBISheBal127872_2495.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHOG000088965.
KOK00831.
OMANNTIFGT.
OrthoDBEOG60CWP3.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycSBAL402882:GJ99-2349-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. SSF53383. 1 hit.
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_SHEB8
AccessionPrimary (citable) accession number: A6WNN5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways