ID   SELA_SHIDS              Reviewed;         463 AA.
AC   Q328Y9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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}; OrderedLocusNames=SDY_4212;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB64116.1; -; Genomic_DNA.
DR   RefSeq; WP_000206268.1; NC_007606.1.
DR   RefSeq; YP_405607.1; NC_007606.1.
DR   AlphaFoldDB; Q328Y9; -.
DR   SMR; Q328Y9; -.
DR   STRING; 300267.SDY_4212; -.
DR   EnsemblBacteria; ABB64116; ABB64116; SDY_4212.
DR   KEGG; sdy:SDY_4212; -.
DR   PATRIC; fig|300267.13.peg.4952; -.
DR   HOGENOM; CLU_038142_1_0_6; -.
DR   OMA; GATNRTH; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000002716; 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_1000050382"
FT   MOD_RES         295
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   463 AA;  50739 MW;  DDBF8A781DC48E0E CRC64;
     MTTETRSLYS QLPAIDRLLR DSSFLSLRDT YGHTRVVELL RQMLDEAREV IRDSQTLPTW
     CENWAQEVDA RLTKEAQSAL RPVINLTGTV LHTNLGRALQ AEAAVEAVAQ AMRSPVTLEY
     DLDDAGRGHR DRALAQLLCR ITGVEDACIV NNNAAAVLLM LAATASGKEV VVSRGELVEI
     GGSFRIPDVM 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