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UniProtKB/Swiss-Prot entry Q8F930

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

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Entry information
Entry name SERC_LEPIN
Primary accession number Q8F930
Secondary accession numbers None
Integrated into Swiss-Prot on February 15, 2005
Sequence was last modified on July 10, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 41)
Name and origin of the protein
Protein name Phosphoserine aminotransferase
Synonyms EC 2.6.1.52
Phosphohydroxythreonine aminotransferase
PSAT
Gene name
Name: serC
OrderedLocusNames: LA_0366
From
Leptospira interrogans [TaxID: 173] [HAMAP proteome]
Taxonomy Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
DOI=10.1038/nature01597; PubMed=12712204 [NCBI, ExPASy, EBI, Israel, Japan]
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing.";
Nature 422:888-893(2003).
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
AE010300; AAN47566.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_710548.2; -.
3D structure databases
HSSP P23721; 1BJN. [HSSP ENTRY / PDB]
ModBase Q8F930.
Enzyme and pathway databases
BioCyc LINT189518:LA0367-MON; -.
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.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 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; 1.
BLOCKS Q8F930.
ProtoNet Q8F930.
Genome annotation databases
GeneID 1149710; -.
GenomeReviews AE010300_GR; LA_0366.
KEGG lil:LA0366; -.
Phylogenomic databases
HOGENOM Q8F930; -.
Genome annotation databases
CMR Q8F930; LA_0366.
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   363  363     Phosphoserine aminotransferase. PRO_0000150182
REGION   80    81  2     Pyridoxal phosphate binding (By similarity). 
REGION   241   242  2     Pyridoxal phosphate binding (By similarity). 
BINDING   46    46        L-glutamate (By similarity). 
BINDING   106   106        Pyridoxal phosphate (By similarity). 
BINDING   156   156        Pyridoxal phosphate (By similarity). 
BINDING   176   176        Pyridoxal phosphate (By similarity). 
BINDING   199   199        Pyridoxal phosphate (By similarity). 
BINDING   200   200        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 40587 Da [This is the MW of the unprocessed precursor] CRC64: 07747CC7A2F7A554 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MYLFQERIYN FGAGPAMLPN EVMEIAAAEF LNYKGSGMSV MEVSHREPLF EDVITEAEIL 

        70         80         90        100        110        120 
LRKLLNLGED YSIAFFSGGA TLHFSALPLN LLKEGESFDV AHTGIWTKKA WEEGLKFNEV 

       130        140        150        160        170        180 
NVIYDSTNNH FTDVPVLTDS NLSGKGKYLH ITSNNTIYGT QYPEIPKIKQ IPLVADMTSE 

       190        200        210        220        230        240 
LLSRKIDVKD FGVIFAGAQK NIGPSGLSLA IIRNDLLGIS GRKIPILLDY SVMVKNRSLY 

       250        260        270        280        290        300 
NTPSTYSIYI AKLVFEWLLK LGGIEAIEKV NEQKAKLIYD FIDSSSLYVC PVQKRARSKM 

       310        320        330        340        350        360 
NVVFLLKDKN LDSKFLDEAE KNGLHGLGGH RLVGGFRASI YNSMPLTGVQ KLVSFMKDFE 


SKI
Q8F930 in FASTA format

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