ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry A8FKB5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SERC_CAMJ8
Primary accession number A8FKB5
Secondary accession numbers None
Integrated into Swiss-Prot on February 26, 2008
Sequence was last modified on November 13, 2007 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 11)
Name and origin of the protein
Protein name Phosphoserine aminotransferase
Synonyms EC 2.6.1.52
Phosphohydroxythreonine aminotransferase
PSAT
Gene name
Name: serC
OrderedLocusNames: C8J_0303
From
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [TaxID: 407148] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01404-07; PubMed=17873037 [NCBI, ExPASy, EBI, Israel, Japan]
Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M.;
"The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828).";
J. Bacteriol. 189:8402-8403(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000814; ABV51902.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001481879.1; -.
3D structure databases
ModBase A8FKB5.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004648; Molecular function: phosphoserine transaminase activity (inferred from electronic annotation from HAMAP).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from HAMAP).
GO:0006564; Biological process: L-serine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008615; Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00160; -; 1.
PBIL [Tree]
InterPro IPR000192; Aminotrans_V/Cys_dSase.
IPR003248; Pser_amintransf.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
IPR015422; PyrdxlP-dep_Trfase_major_sub2.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
Pfam PF00266; Aminotran_5; 1.
Pfam graphical view of domain structure.
ProDom PD001544; Pser_amintransf; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01364; serC_1; 1.
PROSITE PS00595; AA_TRANSFER_CLASS_5; FALSE_NEG.
ProtoNet A8FKB5.
Genome annotation databases
GeneID 5618480; -.
GenomeReviews CP000814_GR; C8J_0303.
KEGG cju:C8J_0303; -.
CMR A8FKB5; C8J_0303.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis; Serine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   358  358     Phosphoserine aminotransferase. PRO_1000071542
REGION   75    76  2     Pyridoxal phosphate binding (By similarity). 
REGION   233   234  2     Pyridoxal phosphate binding (By similarity). 
BINDING   41    41        L-glutamate (By similarity). 
BINDING   100   100        Pyridoxal phosphate (By similarity). 
BINDING   148   148        Pyridoxal phosphate (By similarity). 
BINDING   167   167        Pyridoxal phosphate (By similarity). 
BINDING   190   190        Pyridoxal phosphate (By similarity). 
BINDING   191   191        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 40441 Da [This is the MW of the unprocessed precursor] CRC64: 39BD4191ACCA9BC6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRKINFSAGP STLPLEILEQ AQKELCDYQG RGYSIMEISH RTKVFEEVHF GAQEKAKKLY 

        70         80         90        100        110        120 
GLNDDYEVLF LQGGASLQFA MIPMNLSLNG VCEYANTGVW TKKAIKEAQI LGVNVKTVAS 

       130        140        150        160        170        180 
SEESNFNHIP RVEFSDNADY AYICSNNTIY GTQYQNYPKT KAPLIVDASS DFFSRKVDFS 

       190        200        210        220        230        240 
NIALFYGGVQ KNAGISGLSC IFIRKDMLER SKNKQIPSML NYLTHAENQS LFNTPPTFAI 

       250        260        270        280        290        300 
YMFNLEMDWL LNQGELDKVH EKNSQKAAML YECIDLSNGF YKGHADKKDR SLMNVSFNIA 

       310        320        330        340        350 
KNKDLEPLFV KEAEEAGMIG LKGHRILGGI RASIYNALNL DQVKTLCEFM KEFQGKYA
A8FKB5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!