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Reviewed, UniProtKB/Swiss-Prot Q9X4H1 (SERC_EDWI9)

Last modified February 9, 2010. Version 62. 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: NT01EI_2459
OrganismEdwardsiella ictaluri (strain 93-146) [Complete proteome] [HAMAP]
Taxonomic identifier634503 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
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. HAMAP MF_00160

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. HAMAP MF_00160

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. HAMAP MF_00160

Subcellular location

Cytoplasm By similarity HAMAP 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 – 363363Phosphoserine aminotransferase HAMAP MF_00160
PRO_0000150170

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region240 – 2412Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1041Pyridoxal phosphate By similarity
Binding site1551Pyridoxal phosphate By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site1981Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X4H1-1 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 945229E9EE3F65FB

FASTA36340,210
        10         20         30         40         50         60 
MTQVYNFCAG PAMLPVEVLR RAEQELCNWH GLGTSVMEIS HRGEAFMQVA AEAEQDLRDL 

        70         80         90        100        110        120 
LKVPADYRIL FCHGGARGQF AAVPLNLLGS ERTARADYAV GGYWAQSAAK EAQRYCNPHA 

       130        140        150        160        170        180 
IDIAQRVDGK LSMKPMAQWD LLEESAYLHY CPNETIDGVT IDEEPDFGDR VVVADMSSTI 

       190        200        210        220        230        240 
LSRPIDVSRY GLIYAGAQKN VGPAGITLVI VREDLLGRAR REIPSILDYQ VLVESDSMFN 

       250        260        270        280        290        300 
TPPTFAWYLS GMVFKWLKEQ GGVSEMARRN QAKADLLYQA IDGGEFYRND VAPANRSRMN 

       310        320        330        340        350        360 
VPFQMVDSAL DPLFWDEARK AGLHALKGHK VAGGMRASIY NAMPLAGVQA LVAFMADFAR 


RHG 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Edwardsiella ictaluri 93-146."
Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"An aroA mutant of Edwardsiella ictaluri is safe and efficacious as a live, attenuated vaccine."
Thune R.L., Fernandez D.H., Battista J.R.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-363.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001600 Genomic DNA. Translation: ACR69629.1.
AF110153 Genomic DNA. Translation: AAD28374.1.
RefSeqYP_002933864.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7959191.
GenomeReviewsGene locus NT01EI_2459 in contig CP001600_GR.
KEGGeic:NT01EI_2459.

Organism-specific databases

CMRSearch...

Enzyme and pathway databases

BRENDA2.6.1.52. 279047.

Family and domain databases

HAMAPMF_00160. SerC_aminotrans_5.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR003248. Pser_amintransf.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
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...

Entry information

Entry nameSERC_EDWI9
AccessionPrimary (citable) accession number: Q9X4H1
Secondary accession number(s): C5BBS4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 1, 2009
Last modified: February 9, 2010
This is version 62 of the entry and version 2 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