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P81435 (SERC_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_302
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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-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 – 361361Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150159

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region238 – 2392Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1531Pyridoxal phosphate By similarity
Binding site1731Pyridoxal phosphate By similarity
Binding site1961Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1971N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P81435 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: F30153652525047D

FASTA36141,261
        10         20         30         40         50         60 
MNLIYNFSAG PAMIPKDVLY QAKKELQNWN QIGCSIMEIS HRSKEFIQVA LEAEQDLRDL 

        70         80         90        100        110        120 
LNISNSYEIL FCQGGARGQF AAVPMNLLGN FKETDYINSG YWSNCALIEA KKYCIPKNIS 

       130        140        150        160        170        180 
VRQKKNGKSF LLKPSQWNIS DNSAYIHYCP NETIDGMSIY EEPNFKNKII VGDFSSFILS 

       190        200        210        220        230        240 
RRINIENYGL IYAGAQKNIG PSGITIILIR KDLIGYASKI SPSIFNYYII SKYNSMFNTP 

       250        260        270        280        290        300 
PTFSWYLSGL VFKWLKKQGG IKKIEQLNQK KSNLLYQIID NSNFYINDID KRNRSQMNVV 

       310        320        330        340        350        360 
FHLYNSKLDN LFLKEAKNAG LNALKGHNVI GGMRASIYNA MPLEGVQSLA KFMLYFEKKY 


G 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a DNA fragment from Buchnera aphidicola (Aphid endosymbiont) containing the genes aspS-trxB-serS-serC-aroA-rpsA-himD-tpiA."
Thao M.L., Baumann P.
Curr. Microbiol. 35:68-69(1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43549 Genomic DNA. Translation: AAC05435.1.
AE013218 Genomic DNA. Translation: AAM67856.1.
RefSeqNP_660645.1. NC_004061.1.

3D structure databases

ProteinModelPortalP81435.
SMRP81435. Positions 4-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg302.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67856; AAM67856; BUsg_302.
GeneID1005506.
KEGGbas:BUsg302.
PATRIC21247411. VBIBucAph100086_0315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
KOK00831.
OMAFAAIPMN.
OrthoDBEOG60CWP3.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-316-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]
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_BUCAP
AccessionPrimary (citable) accession number: P81435
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 100 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names