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O67140 (SELA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:
L-seryl-tRNA(Sec) selenium transferase
EC=2.9.1.1
Alternative name(s):
Selenocysteine synthase
Short name=Sec synthase
Selenocysteinyl-tRNA(Sec) synthase
Gene names
Name:selA
Ordered Locus Names:aq_1031
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis By similarity. HAMAP MF_00423

Catalytic activity

L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate. HAMAP MF_00423

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_00423

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1. HAMAP MF_00423

Subcellular location

Cytoplasm By similarity HAMAP MF_00423.

Sequence similarities

Belongs to the selA family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
Selenium
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processselenocysteine incorporation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-seryl-tRNASec selenium transferase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452L-seryl-tRNA(Sec) selenium transferase HAMAP MF_00423
PRO_0000189594

Amino acid modifications

Modified residue2851N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O67140 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E511326E17E9F015

FASTA45250,848
        10         20         30         40         50         60 
MKSLLRQIPQ ISKVVEIFKK KYPEIYVVKA AREVAEKYRK EIIEGKRKDL NGFLEDVERK 

        70         80         90        100        110        120 
IKSLMKPNIK RVINATGVVI NTNLGRAPLS KDVINFISEI ANGYSNLEYN LEEGKRGSRI 

       130        140        150        160        170        180 
AHIEKYLNEL TGAESSFVVN NNAGAVFLVL NTLAEGKEVI ISRGELVEIG GSFRIPDIMK 

       190        200        210        220        230        240 
KSGAILREVG TTNKTKVSDY EGAINQNTAL LMKVHKSNFY MEGFVEEVKL EDLVKLGHKY 

       250        260        270        280        290        300 
GIPTYYDAGS GLLINLKEFG ISVDEPNFRD CISLGIDLVS GSGDKLLGGP QAGIIVGKKN 

       310        320        330        340        350        360 
LIEKIKKNPI ARALRIDKLT LSGLEMTLKL YFEKRYEDIP VIRMLTQDEK ALRQKAKRLE 

       370        380        390        400        410        420 
KLLKDIPGLK ISVIKDKAKP GGGSLPELEL PTYCVAIRHD RLSSQELSRR LRLAEPPIVC 

       430        440        450 
RIREDQLLFD MRTVFHEDLK TIKKTLQELL SI

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC07094.1.
PIRA70389.
RefSeqNP_213703.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67140.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193774.
GenomeReviewsGene locus aq_1031 in contig AE000657_GR.
KEGGaae:aq_1031.
NMPDRfig|224324.1.peg.718.
PATRIC20959366. VBIAquAeo85532_0805.

Phylogenomic databases

HOGENOMHBG564950.
OMAENTAFLM.
PhylomeDBO67140.
ProtClustDBPRK04311.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1031-MONOMER.

Family and domain databases

HAMAPMF_00423. SelA.
[Tree]
InterProIPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR018319. Pyridoxal-P-dep_Trfase.
IPR004534. SelA_trans.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KOK01042.
PfamPF03841. SelA. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00474. SelA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSELA_AQUAE
AccessionPrimary (citable) accession number: O67140
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 69 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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