SELA_ECO57
ID SELA_ECO57 Reviewed; 463 AA.
AC P0A822; P23328; P58225; P78119;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000255|HAMAP-Rule:MF_00423};
DE EC=2.9.1.1 {ECO:0000255|HAMAP-Rule:MF_00423};
DE AltName: Full=Selenocysteine synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE Short=Sec synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000255|HAMAP-Rule:MF_00423};
GN Name=selA {ECO:0000255|HAMAP-Rule:MF_00423};
GN OrderedLocusNames=Z5012, ECs4468;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00423}.
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:0000255|HAMAP-
CC Rule:MF_00423};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00423};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (bacterial route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00423}.
CC -!- SUBUNIT: Homodecamer; pentamer of dimers. Binds only one seryl-
CC tRNA(Sec) per dimer. {ECO:0000255|HAMAP-Rule:MF_00423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP-
CC Rule:MF_00423}.
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DR EMBL; AE005174; AAG58735.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37891.1; -; Genomic_DNA.
DR PIR; C86034; C86034.
DR PIR; D91187; D91187.
DR RefSeq; NP_312495.1; NC_002695.1.
DR RefSeq; WP_000206275.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A822; -.
DR SMR; P0A822; -.
DR STRING; 155864.EDL933_4851; -.
DR EnsemblBacteria; AAG58735; AAG58735; Z5012.
DR EnsemblBacteria; BAB37891; BAB37891; ECs_4468.
DR GeneID; 66672516; -.
DR GeneID; 915592; -.
DR KEGG; ece:Z5012; -.
DR KEGG; ecs:ECs_4468; -.
DR PATRIC; fig|386585.9.peg.4679; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_6; -.
DR OMA; GATNRTH; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
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_0000189600"
FT MOD_RES 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
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
