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Reviewed, UniProtKB/Swiss-Prot B8FLC3 (SERC_DESAA)

Last modified October 13, 2009. Version 7. 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: Dalk_3380
OrganismDesulfatibacillum alkenivorans (strain AK-01) [Complete proteome] [HAMAP]
Taxonomic identifier439235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfatibacillum

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_1000118178

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 site1521Pyridoxal 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
B8FLC3-1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 732DB679C3D2AA59

FASTA36139,582
        10         20         30         40         50         60 
MKNRIHNFNA GPAALPLPVL EEIQAELLDF KGSGMSIMEV SHRSKWFDDV INETVERINR 

        70         80         90        100        110        120 
LMGLGDDFQV LFMQGGASTQ FALVPMNLLP EGQSADYVNT GTWSTKAIKE AQAMGKTVNV 

       130        140        150        160        170        180 
AASSEDRNFC YIPKDIPLDP NAAYVHITSN NTIKGTAYTD FPDAGNVPLI ADMSSDILSR 

       190        200        210        220        230        240 
PIDASKFGLI YAGAQKNMGP AGVCVAIIRK DMLERVPASL PSMFKYTTFA DKNSMYNTPP 

       250        260        270        280        290        300 
CFAIYTVGLV VKWIEETIGG LEKMEARNRK KADTLYSIFD SSDFYSGTAD KDSRSLMNVT 

       310        320        330        340        350        360 
FRLPSEDLEK AFVAQALENG LGGLKGHRSV GGCRASIYNP TSQEGIEALV DFMKEFEKKN 


G 

« Hide

References

[1]"Complete sequence of Desulfatibacillum alkenivorans AK-01."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Wawrik B., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001322 Genomic DNA. Translation: ACL05069.1.
RefSeqYP_002432537.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7167323.
GenomeReviewsGene locus Dalk_3380 in contig CP001322_GR.
KEGGdal:Dalk_3380.

Organism-specific databases

CMRSearch...

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]
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_DESAA
AccessionPrimary (citable) accession number: B8FLC3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 3, 2009
Last modified: October 13, 2009
This is version 7 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