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A5FH28 (SERC_FLAJ1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Fjoh_2462
OrganismFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]
Taxonomic identifier376686 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium ›

Protein attributes

Sequence length356 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_1000076906

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region234 – 2352Pyridoxal phosphate binding By similarity

Sites

Binding site411L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1501Pyridoxal phosphate By similarity
Binding site1691Pyridoxal phosphate By similarity
Binding site1921Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1931N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FH28 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 001013680A26430E

FASTA35638,871
        10         20         30         40         50         60 
MKKHNYSAGP SILPQEVFEK ASKAVLNFND SGLSILEISH RSKDFVAVMD EARSLALELL 

        70         80         90        100        110        120 
GLQGKGYQAL FLQGGASTAF LMAPYNLMKE NGKAAYLDSG TWATAAIKEA KLFGETVIVG 

       130        140        150        160        170        180 
SSKDDNYTYI PKGYEIPADA DYFHCTSNNT IFGTQIQEFP STNIPVVCDM SSDIFSRELD 

       190        200        210        220        230        240 
FSKFDLIYAG AQKNMGPAGT TLVVVKEEIL GKNGRTIPSM LDYAKHIKAE SMYNTPSVFA 

       250        260        270        280        290        300 
VYVSLLTLQW IKAKGGIAAV EKLNNAKADL LYAEIDRNPL FKGAANVEDR SKMNVTFLLN 

       310        320        330        340        350 
NPEHTETFDA LWKAAGISGL PGHRSVGGYR ASIYNAMPIE SVQVLVDVMK ALESKV

« Hide

References

[1]"Complete sequence of Flavobacterium johnsoniae UW101."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000685 Genomic DNA. Translation: ABQ05489.1.
RefSeqYP_001194808.1. NC_009441.1.

3D structure databases

ProteinModelPortalA5FH28.
ModBaseSearch...

Protein-protein interaction databases

STRING376686.Fjoh_2462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ05489; ABQ05489; Fjoh_2462.
GeneID5090319.
KEGGfjo:Fjoh_2462.
PATRIC21899361. VBIFlaJoh53613_2532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHOG000088965.
KOK00831.
OMAMSIMEMS.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycFJOH376686:GIXN-2519-MONOMER.
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.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_FLAJ1
AccessionPrimary (citable) accession number: A5FH28
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 1, 2013
This is version 45 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

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