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Reviewed, UniProtKB/Swiss-Prot Q8A8L4 (SERC_BACTN)

Last modified November 3, 2009. Version 51. 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: BT_1153
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length355 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 – 355355Phosphoserine aminotransferase HAMAP MF_00160
PRO_0000150154

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

Sequences

Sequence LengthMass (Da)Tools
Q8A8L4-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D6FE0762EF14968F

FASTA35539,434
        10         20         30         40         50         60 
MKKHNFNAGP SILPREVIED TAKAILDFNG SGLSLMEISH RAKDFQPVVD EAEALFKELL 

        70         80         90        100        110        120 
NIPEGYSVLF LGGGASMEFC MVPFNFLEKK AAYLNTGVWA KKAMKEAKGF GEVVEVASSA 

       130        140        150        160        170        180 
EATYTYIPKD YTIPADADYF HITTNNTIYG TELKEDLNSP VPMVADMSSD IFSRPIDVSK 

       190        200        210        220        230        240 
YICIYGGAQK NLAPAGVTFV IVKNDAVGKV SRYIPSMLNY QTHIDNGSMF NTPPVVPIYA 

       250        260        270        280        290        300 
ALLNLRWIKA QGGVKEMERR AIEKADMLYA EIDRNKLFVG TAAKEDRSRM NICFVMAPEY 

       310        320        330        340        350 
KDLEADFMKF ATEKGMVGIK GHRSVGGFRA SCYNALPKES VQALIDCMQE FEKLH 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO76260.1.
RefSeqNP_810066.1.

3D structure databases

HSSPHSSP built from PDB template 1BT4 based on UniProtKB Q59196.
ModBaseSearch...

Genome annotation databases

GeneID1073773.
GenomeReviewsGene locus BT_1153 in contig AE015928_GR.
KEGGbth:BT_1153.
NMPDRfig|226186.1.peg.1153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A8L4.
OMASMYNTPP.

Enzyme and pathway databases

BioCycBTHE226186:BT_1153-MON.
BRENDA2.6.1.52. 21018.

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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_BACTN
AccessionPrimary (citable) accession number: Q8A8L4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 51 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