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Q99K85 (SERC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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

Short name=PSAT
EC=2.6.1.52
Alternative name(s):
Endometrial progesterone-induced protein
Short name=EPIP
Phosphohydroxythreonine aminotransferase
Gene names
Name:Psat1
Synonyms:Psa, Psat
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

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 – 370370Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150136

Regions

Region79 – 802Pyridoxal phosphate binding By similarity
Region241 – 2422Pyridoxal phosphate binding By similarity

Sites

Binding site451L-glutamate By similarity
Binding site1071Pyridoxal phosphate By similarity
Binding site1561Pyridoxal phosphate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site1991Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue511N6-acetyllysine By similarity
Modified residue1271N6-acetyllysine Ref.4
Modified residue2001N6-(pyridoxal phosphate)lysine By similarity
Modified residue2691N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine By similarity
Modified residue3231N6-acetyllysine By similarity
Modified residue3331N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99K85 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6CF6B80CFDA1974B

FASTA37040,473
        10         20         30         40         50         60 
MEATKQVVNF GPGPAKLPHS VLLEIQKQLL DYRGLGISVL EMSHRSSDFA KIIGNTENLV 

        70         80         90        100        110        120 
RELLAVPNNY KVIFVQGGGS GQFSAVPLNL IGLKAGRSAD YVVTGAWSAK AAEEAKKFGT 

       130        140        150        160        170        180 
VNIVHPKLGS YTKIPDPSTW NLNPDASYVY FCANETVHGV EFDFVPDVKG AVLVCDMSSN 

       190        200        210        220        230        240 
FLSRPVDVSK FGVIFAGAQK NVGSAGVTVV IVRDDLLGFS LRECPSVLDY KVQAGNNSLY 

       250        260        270        280        290        300 
NTPPCFSIYV MGMVLEWIKN NGGAAAMEKL SSIKSQMIYE IIDNSQGFYV CPVERQNRSR 

       310        320        330        340        350        360 
MNIPFRIGNA KGDEALEKRF LDKAVELNMI SLKGHRSVGG IRASLYNAVT TEDVEKLAAF 

       370 
MKNFLEMHQL 

« Hide

References

« Hide 'large scale' references
[1]Sato M., Oguma T., Tsujimoto K., Tadakuma T.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 17-27; 52-94; 191-200; 223-231 AND 343-356, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF259674 mRNA. Translation: AAK69389.1.
BC004827 mRNA. Translation: AAH04827.1.
RefSeqNP_803155.1. NM_177420.2.
UniGeneMm.289936.

3D structure databases

ProteinModelPortalQ99K85.
SMRQ99K85. Positions 17-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99K85. 2 interactions.
MINTMINT-4134236.

PTM databases

PhosphoSiteQ99K85.

Proteomic databases

PaxDbQ99K85.
PRIDEQ99K85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025542; ENSMUSP00000025542; ENSMUSG00000024640.
GeneID107272.
KEGGmmu:107272.
UCSCuc008gwp.2. mouse.

Organism-specific databases

CTD29968.
MGIMGI:2183441. Psat1.

Phylogenomic databases

eggNOGCOG1932.
GeneTreeENSGT00390000015177.
HOGENOMHOG000088965.
HOVERGENHBG001218.
InParanoidQ99K85.
KOK00831.
OMANNTIFGT.
OrthoDBEOG7KQ220.
PhylomeDBQ99K85.
TreeFamTF312975.

Enzyme and pathway databases

UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

Gene expression databases

ArrayExpressQ99K85.
BgeeQ99K85.
CleanExMM_PSAT1.
GenevestigatorQ99K85.

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...

Other

ChiTaRSPSAT1. mouse.
NextBio358656.
PROQ99K85.
SOURCESearch...

Entry information

Entry nameSERC_MOUSE
AccessionPrimary (citable) accession number: Q99K85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot