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Protein

L-seryl-tRNA(Sec) selenium transferase

Gene

selA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule.2 Publications

Catalytic activityi

L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: selenocysteinyl-tRNA(Sec) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route).
Proteins known to be involved in this subpathway in this organism are:
  1. L-seryl-tRNA(Sec) selenium transferase (selA)
This subpathway is part of the pathway selenocysteinyl-tRNA(Sec) biosynthesis, which is itself part of Aminoacyl-tRNA biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route), the pathway selenocysteinyl-tRNA(Sec) biosynthesis and in Aminoacyl-tRNA biosynthesis.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • L-seryl-tRNASec selenium transferase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  • selenocysteine biosynthetic process Source: EcoCyc
  • selenocysteine incorporation Source: UniProtKB-HAMAP
  • selenocysteinyl-tRNA(Sec) biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, Selenium

Enzyme and pathway databases

BioCyciEcoCyc:EG10941-MONOMER.
ECOL316407:JW3564-MONOMER.
MetaCyc:EG10941-MONOMER.
UniPathwayiUPA00906; UER00896.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:selA
Synonyms:fdhA
Ordered Locus Names:b3591, JW3564
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10941. selA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi224 – 2241K → N: Still binds PLP. 1 Publication
Mutagenesisi295 – 2951K → N: Loss of activity and PLP binding. 1 Publication
Mutagenesisi328 – 3281K → N: Loss of PLP binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463L-seryl-tRNA(Sec) selenium transferasePRO_0000189599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951N6-(pyridoxal phosphate)lysine1 Publication

Proteomic databases

PaxDbiP0A821.
PRIDEiP0A821.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers. Binds only one seryl-tRNA(Sec) per dimer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261876. 5 interactions.
DIPiDIP-10847N.
IntActiP0A821. 2 interactions.
STRINGi511145.b3591.

Structurei

3D structure databases

ProteinModelPortaliP0A821.
SMRiP0A821. Positions 31-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SelA family.Curated

Phylogenomic databases

eggNOGiENOG4105C1Y. Bacteria.
COG1921. LUCA.
HOGENOMiHOG000163726.
InParanoidiP0A821.
KOiK01042.
OMAiNRTHARD.
OrthoDBiEOG69WFGN.
PhylomeDBiP0A821.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_00423. SelA.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR018319. SelA-like.
IPR004534. SelA_trans.
IPR025862. SelA_trans_N_dom.
[Graphical view]
PfamiPF12390. Se-cys_synth_N. 1 hit.
PF03841. SelA. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00474. selA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTETRSLYS QLPAIDRLLR DSSFLSLRDT YGHTRVVELL RQMLDEAREV
60 70 80 90 100
IRGSQTLPAW CENWAQEVDA RLTKEAQSAL RPVINLTGTV LHTNLGRALQ
110 120 130 140 150
AEAAVEAVAQ AMRSPVTLEY DLDDAGRGHR DRALAQLLCR ITGAEDACIV
160 170 180 190 200
NNNAAAVLLM LAATASGKEV VVSRGELVEI GGAFRIPDVM RQAGCTLHEV
210 220 230 240 250
GTTNRTHAND YRQAVNENTA LLMKVHTSNY SIQGFTKAID EAELVALGKE
260 270 280 290 300
LDVPVVTDLG SGSLVDLSQY GLPKEPMPQE LIAAGVSLVS FSGDKLLGGP
310 320 330 340 350
QAGIIVGKKE MIARLQSHPL KRALRADKMT LAALEATLRL YLHPEALSEK
360 370 380 390 400
LPTLRLLTRS AEVIQIQAQR LQAPLAAHYG AEFAVQVMPC LSQIGSGSLP
410 420 430 440 450
VDRLPSAALT FTPHDGRGSH LESLAARWRE LPVPVIGRIY DGRLWLDLRC
460
LEDEQRFLEM LLK
Length:463
Mass (Da):50,607
Last modified:June 7, 2005 - v1
Checksum:iCD724FF681D882DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → F in AAA24624 (PubMed:2007584).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64177 Genomic DNA. Translation: AAA24624.1.
U00039 Genomic DNA. Translation: AAB18568.1.
U00096 Genomic DNA. Translation: AAC76615.1.
AP009048 Genomic DNA. Translation: BAE77702.1.
PIRiA65159.
RefSeqiNP_418048.1. NC_000913.3.
WP_000206223.1. NZ_CP014272.1.
WP_000206275.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76615; AAC76615; b3591.
BAE77702; BAE77702; BAE77702.
GeneIDi948124.
KEGGiecj:JW3564.
eco:b3591.
PATRICi32122660. VBIEscCol129921_3707.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64177 Genomic DNA. Translation: AAA24624.1.
U00039 Genomic DNA. Translation: AAB18568.1.
U00096 Genomic DNA. Translation: AAC76615.1.
AP009048 Genomic DNA. Translation: BAE77702.1.
PIRiA65159.
RefSeqiNP_418048.1. NC_000913.3.
WP_000206223.1. NZ_CP014272.1.
WP_000206275.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A821.
SMRiP0A821. Positions 31-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261876. 5 interactions.
DIPiDIP-10847N.
IntActiP0A821. 2 interactions.
STRINGi511145.b3591.

Proteomic databases

PaxDbiP0A821.
PRIDEiP0A821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76615; AAC76615; b3591.
BAE77702; BAE77702; BAE77702.
GeneIDi948124.
KEGGiecj:JW3564.
eco:b3591.
PATRICi32122660. VBIEscCol129921_3707.

Organism-specific databases

EchoBASEiEB0934.
EcoGeneiEG10941. selA.

Phylogenomic databases

eggNOGiENOG4105C1Y. Bacteria.
COG1921. LUCA.
HOGENOMiHOG000163726.
InParanoidiP0A821.
KOiK01042.
OMAiNRTHARD.
OrthoDBiEOG69WFGN.
PhylomeDBiP0A821.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00896.
BioCyciEcoCyc:EG10941-MONOMER.
ECOL316407:JW3564-MONOMER.
MetaCyc:EG10941-MONOMER.

Miscellaneous databases

PROiP0A821.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_00423. SelA.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR018319. SelA-like.
IPR004534. SelA_trans.
IPR025862. SelA_trans_N_dom.
[Graphical view]
PfamiPF12390. Se-cys_synth_N. 1 hit.
PF03841. SelA. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00474. selA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the gene (selA) and purification of the protein."
    Forchhammer K., Leinfelder W., Boesmiller K., Veprek B., Boeck A.
    J. Biol. Chem. 266:6318-6323(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence."
    Forchhammer K., Boeck A.
    J. Biol. Chem. 266:6324-6328(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
  6. "Structure of selenocysteine synthase from Escherichia coli and location of tRNA in the seryl-tRNA(sec)-enzyme complex."
    Engelhardt H., Forchhammer K., Mueller S., Goldie K.N., Boeck A.
    Mol. Microbiol. 6:3461-3467(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Bacterial selenocysteine synthase -- structural and functional properties."
    Tormay P., Wilting R., Lottspeich F., Mehta P.K., Christen P., Boeck A.
    Eur. J. Biochem. 254:655-661(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PLP BINDING SITE, SUBSTRATE SPECIFICITY, MUTAGENESIS OF LYS-224; LYS-295 AND LYS-328.

Entry informationi

Entry nameiSELA_ECOLI
AccessioniPrimary (citable) accession number: P0A821
Secondary accession number(s): P23328
, P58225, P78119, Q2M7Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 6, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.