Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6ALW3 (SERC_DESPS)

Last modified November 3, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: DP1933
OrganismDesulfotalea psychrophila [Complete proteome] [HAMAP]
Taxonomic identifier84980 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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.

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 – 361361Phosphoserine aminotransferase HAMAP MF_00160
PRO_0000150166

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 site1531Pyridoxal 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
Q6ALW3-1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 6E3CF8F9C3B7A8C0

FASTA36139,842
        10         20         30         40         50         60 
MADRVYNFSA GPATLPFEVL EQAGKDIVNF KETGSGLIEI SHRSPEFIEV IEKTESLVRE 

        70         80         90        100        110        120 
LLEVPDNYKV LFLQGGASSQ FFMVPMNLLG AGKKATYLNT GTWAKKAIKE AQLFGDIDVA 

       130        140        150        160        170        180 
YSSEESIFNH VPANDAYQVA EESEYLYFAS NNTIYGTQFE TMPQSKKMLV ADMSSDIFSR 

       190        200        210        220        230        240 
KVDVSKFGLI FAGAQKNLGP AGVTLVIIRD DLLEKTPAHT PTMLSYKTHA DKGSMFNTPP 

       250        260        270        280        290        300 
CFAIYVMGEV LAWLKNLGGV EKIEEINREK AALLYSQIDA SDYYRVHAQD GSRSLMNVTF 

       310        320        330        340        350        360 
NLPTAELEAK FIAEASALQM KGLKGHRSIG GCRASIYNAF PREGVVKLVE FMQVFAANNP 


A 

« Hide

References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed: 15305914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

CR522870 Genomic DNA. Translation: CAG36662.1.
RefSeqYP_065669.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2947300.
GenomeReviewsGene locus DP1933 in contig CR522870_GR.
KEGGdps:DP1933.
NMPDRfig|177439.1.peg.1933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6ALW3.
OMASMYNTPP.

Enzyme and pathway databases

BioCycDPSY177439:DP1933-MON.
BRENDA2.6.1.52. 280712.

Family and domain databases

HAMAPMF_00160.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR003248. Pser_amintransf.
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.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
ProDomPD001544. Pser_amintransf. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_DESPS
AccessionPrimary (citable) accession number: Q6ALW3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: September 13, 2004
Last modified: November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents