SELA_ECOLI
ID SELA_ECOLI Reviewed; 463 AA.
AC P0A821; P23328; P58225; P78119; Q2M7Q4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=L-seryl-tRNA(Sec) selenium transferase;
DE EC=2.9.1.1;
DE AltName: Full=Selenocysteine synthase;
DE Short=Sec synthase;
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase;
GN Name=selA; Synonyms=fdhA; OrderedLocusNames=b3591, JW3564;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND COFACTOR.
RX PubMed=2007584; DOI=10.1016/s0021-9258(18)38120-1;
RA Forchhammer K., Leinfelder W., Boesmiller K., Veprek B., Boeck A.;
RT "Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the
RT gene (selA) and purification of the protein.";
RL J. Biol. Chem. 266:6318-6323(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=2007585; DOI=10.1016/s0021-9258(18)38121-3;
RA Forchhammer K., Boeck A.;
RT "Selenocysteine synthase from Escherichia coli. Analysis of the reaction
RT sequence.";
RL J. Biol. Chem. 266:6324-6328(1991).
RN [6]
RP SUBUNIT.
RX PubMed=1474891; DOI=10.1111/j.1365-2958.1992.tb01781.x;
RA Engelhardt H., Forchhammer K., Mueller S., Goldie K.N., Boeck A.;
RT "Structure of selenocysteine synthase from Escherichia coli and location of
RT tRNA in the seryl-tRNA(sec)-enzyme complex.";
RL Mol. Microbiol. 6:3461-3467(1992).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP PLP BINDING SITE, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF LYS-224;
RP LYS-295 AND LYS-328.
RX PubMed=9688279; DOI=10.1046/j.1432-1327.1998.2540655.x;
RA Tormay P., Wilting R., Lottspeich F., Mehta P.K., Christen P., Boeck A.;
RT "Bacterial selenocysteine synthase -- structural and functional
RT properties.";
RL Eur. J. Biochem. 254:655-661(1998).
CC -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC required for selenoprotein biosynthesis. Requires selenophosphate as
CC the selenium-donor molecule. {ECO:0000269|PubMed:2007584,
CC ECO:0000269|PubMed:2007585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-
CC selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728,
CC Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533,
CC ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000269|PubMed:2007585};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:2007584};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (bacterial route): step 1/1.
CC -!- SUBUNIT: Homodecamer; pentamer of dimers. Binds only one seryl-
CC tRNA(Sec) per dimer. {ECO:0000269|PubMed:1474891}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000305}.
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DR EMBL; M64177; AAA24624.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18568.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76615.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77702.1; -; Genomic_DNA.
DR PIR; A65159; A65159.
DR RefSeq; NP_418048.1; NC_000913.3.
DR RefSeq; WP_000206223.1; NZ_CP014272.1.
DR RefSeq; WP_000206275.1; NZ_STEB01000018.1.
DR AlphaFoldDB; P0A821; -.
DR SMR; P0A821; -.
DR BioGRID; 4261876; 36.
DR DIP; DIP-10847N; -.
DR IntAct; P0A821; 2.
DR STRING; 511145.b3591; -.
DR jPOST; P0A821; -.
DR PaxDb; P0A821; -.
DR PRIDE; P0A821; -.
DR EnsemblBacteria; AAC76615; AAC76615; b3591.
DR EnsemblBacteria; BAE77702; BAE77702; BAE77702.
DR GeneID; 66672516; -.
DR GeneID; 948124; -.
DR KEGG; ecj:JW3564; -.
DR KEGG; eco:b3591; -.
DR PATRIC; fig|1411691.4.peg.3120; -.
DR EchoBASE; EB0934; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_6; -.
DR InParanoid; P0A821; -.
DR OMA; GATNRTH; -.
DR PhylomeDB; P0A821; -.
DR BioCyc; EcoCyc:EG10941-MON; -.
DR BioCyc; MetaCyc:EG10941-MON; -.
DR UniPathway; UPA00906; UER00896.
DR PRO; PR:P0A821; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IDA:EcoCyc.
DR Gene3D; 3.40.640.10; -; 1.
DR HAMAP; MF_00423; SelA; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR018319; SelA-like.
DR InterPro; IPR004534; SelA_trans.
DR InterPro; IPR025862; SelA_trans_N_dom.
DR Pfam; PF12390; Se-cys_synth_N; 1.
DR Pfam; PF03841; SelA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00474; selA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Selenium; Transferase.
FT CHAIN 1..463
FT /note="L-seryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000189599"
FT MOD_RES 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:9688279"
FT MUTAGEN 224
FT /note="K->N: Still binds PLP."
FT /evidence="ECO:0000269|PubMed:9688279"
FT MUTAGEN 295
FT /note="K->N: Loss of activity and PLP binding."
FT /evidence="ECO:0000269|PubMed:9688279"
FT MUTAGEN 328
FT /note="K->N: Loss of PLP binding."
FT /evidence="ECO:0000269|PubMed:9688279"
FT CONFLICT 7
FT /note="S -> F (in Ref. 1; AAA24624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50607 MW; CD724FF681D882DF CRC64;
MTTETRSLYS QLPAIDRLLR DSSFLSLRDT YGHTRVVELL RQMLDEAREV IRGSQTLPAW
CENWAQEVDA RLTKEAQSAL RPVINLTGTV LHTNLGRALQ AEAAVEAVAQ AMRSPVTLEY
DLDDAGRGHR DRALAQLLCR ITGAEDACIV NNNAAAVLLM LAATASGKEV VVSRGELVEI
GGAFRIPDVM RQAGCTLHEV GTTNRTHAND YRQAVNENTA LLMKVHTSNY SIQGFTKAID
EAELVALGKE LDVPVVTDLG SGSLVDLSQY GLPKEPMPQE LIAAGVSLVS FSGDKLLGGP
QAGIIVGKKE MIARLQSHPL KRALRADKMT LAALEATLRL YLHPEALSEK LPTLRLLTRS
AEVIQIQAQR LQAPLAAHYG AEFAVQVMPC LSQIGSGSLP VDRLPSAALT FTPHDGRGSH
LESLAARWRE LPVPVIGRIY DGRLWLDLRC LEDEQRFLEM LLK
