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Reviewed, UniProtKB/Swiss-Prot B6YQL2 (SERC_AZOPC)

Last modified October 13, 2009. Version 9. 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

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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
Ordered Locus Names: CFPG_221
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

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Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000097202

Regions

Region75 – 762Pyridoxal phosphate binding By similarity
Region231 – 2322Pyridoxal phosphate binding By similarity

Sites

Binding site411L-glutamate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1471Pyridoxal phosphate By similarity
Binding site1661Pyridoxal phosphate By similarity
Binding site1891Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1901N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
B6YQL2-1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 5B8AB0E88EA17AB0

FASTA35940,077
        10         20         30         40         50         60 
MKKYNFNPGP SILPQETVNN TARAITNFSN SGLSLMEISH RSKDFQLMIN ETIVLFKELL 

        70         80         90        100        110        120 
SIPEGYSVLF LGGGASLQFC MVPYNLLETK AAYLNSGAWA SKAIKEARLF GEIIEVASSR 

       130        140        150        160        170        180 
EANFSYIPKN YIVPSDSDYF HITTNNTIFG TEIHHDIESS VPLVADMSSD IFSRPINISK 

       190        200        210        220        230        240 
YGLIYGGAQK NLGPAGVTFV IVKDSLLGNV SRPIPSMLDY RIHIKNESMF NTPPVVPIYA 

       250        260        270        280        290        300 
SLQTLKWLKT LGGVEEVYKK NKEKATFLYE EIDRNRLFKG IAATEDRSLM NVCFIMNDEY 

       310        320        330        340        350 
KNLESAFQQF ASSKGMVGIK GHRSVGGFRA SIYNALPKES IKALVSVMRE FEKIHCKGI

« Hide

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References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AP010656 Genomic DNA. Translation: BAG83484.1.
RefSeqYP_002308895.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7039838.
GenomeReviewsGene locus CFPG_221 in contig AP010656_GR.
KEGGaps:CFPG_221.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSERC_AZOPC
AccessionPrimary (citable) accession number: B6YQL2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: October 13, 2009
This is version 9 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)

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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