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P62676 (SERC_SALGL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 52. 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
OrganismSalmonella gallinarum
Taxonomic identifier594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length362 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.

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.

Subcellular location

Cytoplasm By similarity.

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 – 362362Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150205

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region239 – 2402Pyridoxal phosphate binding By similarity

Sites

Binding site91L-glutamate By similarity
Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1531Pyridoxal phosphate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site1971Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1981N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P62676 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 8A8ED1A74D313507

FASTA36239,855
        10         20         30         40         50         60 
MAQVFNFSSG PAMLPAEVLK LAQQELRDWH GLGTSVMEIS HRGKEFIQVA EEAEQDFRDL 

        70         80         90        100        110        120 
LNIPSNYKVL FCHGGGRGQF AGVPLNLLGD KTTADYVDAG YWAASAIKEA KKYCAPQIID 

       130        140        150        160        170        180 
AKITVDGKRA VKPMREWQLS DNAAYLHYCP NETIDGIAID ETPDFGPEVV VTADFSSTIL 

       190        200        210        220        230        240 
SAPLDVSRYG VIYAGAQKNI GPAGLTLVIV REDLLGKAHE SCPSILDYTV LNDNDSMFNT 

       250        260        270        280        290        300 
PPTFAWYLSG LVFKWLKAQG GVAAMHKINQ QKAELLYGVI DNSDFYRNDV AQANRSRMNV 

       310        320        330        340        350        360 
PFQLADNALD KVFLEESFAA GLHALKGHRV VGGMRASIYN AMPIEGVKAL TDFMIDFERR 


HG 

« Hide

References

[1]"Nucleotide sequence of the Salmonella serC gene."
Griffin H.G.
Nucleic Acids Res. 18:4260-4260(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 9.
[2]"Cloning and DNA sequence analysis of the serC-aroA operon from Salmonella gallinarum; evolutionary relationships between the prokaryotic and eukaryotic aroA-encoded enzymes."
Griffin H.G., Griffin A.M.
J. Gen. Microbiol. 137:113-121(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53381 Genomic DNA. Translation: CAA37461.1.
M62801 Genomic DNA. Translation: AAA27222.1.
PIRS10512.

3D structure databases

ProteinModelPortalP62676.
SMRP62676. Positions 3-362.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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. 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_SALGL
AccessionPrimary (citable) accession number: P62676
Secondary accession number(s): P17902
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 3, 2013
This is version 52 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