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Q87QA3 (SERC_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:VP1247
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length364 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-Rule MF_00160

Catalytic activity

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP-Rule MF_00160

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP-Rule 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-Rule MF_00160

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP-Rule 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 caution

The sequence BAC59510.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150216

Regions

Region80 – 812Pyridoxal phosphate binding By similarity
Region241 – 2422Pyridoxal phosphate binding By similarity

Sites

Binding site461L-glutamate By similarity
Binding site1061Pyridoxal phosphate By similarity
Binding site1571Pyridoxal phosphate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site1991Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2001N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87QA3 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 617969D78437F489

FASTA36440,201
        10         20         30         40         50         60 
MEQNTDNVFN FSAGPAALPK AVMQQAQQEL IDWQGLGTSV MEISHRSKEF IKVAQEAEQD 

        70         80         90        100        110        120 
LRDLLNIPDN YKVLFCQGGA RAQFAAVPLN LLGDAETATY IDGGYWAESA VEEAKKYCEP 

       130        140        150        160        170        180 
DVFDAKTEID GKVAVLPASE WKIAPEAAYV HFCPNETIDG IEINDLPITD KPIVADMSST 

       190        200        210        220        230        240 
ILSREIDVSK YGVIYAGAQK NIGPSGIAIA IVRDDLLGMA KQVLPSILDY KVLAEKESMF 

       250        260        270        280        290        300 
NTPPTFAWYL SGLVFKWLKA QGGVKSIETV NREKAKLLYD YIDQSDFYRN GVHPSNRSLM 

       310        320        330        340        350        360 
NVPFQLAKPE LDATFLELAD AKGLKALKGH RVVGGMRASI YNAMPLEGVQ ALVDFMKEFE 


QNYA 

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References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC59510.1. Different initiation.
RefSeqNP_797626.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87QA3.
SMRQ87QA3. Positions 8-364.
ModBaseSearch...

Protein-protein interaction databases

STRING223926.VP1247.

Proteomic databases

PRIDEQ87QA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC59510; BAC59510; BAC59510.
GeneID1188752.
KEGGvpa:VP1247.
PATRIC20140698. VBIVibPar50997_1186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHOG000088965.
KOK00831.
OMAMSIMEMS.
ProtClustDBPRK05355.

Enzyme and pathway databases

UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00160. SerC_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR21152:SF1. PTHR21152:SF1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_VIBPA
AccessionPrimary (citable) accession number: Q87QA3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families