ID   SELA_PEPAC              Reviewed;         467 AA.
AC   Q9S3K3;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 84.
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};
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=11041351; DOI=10.1007/s002030000196;
RA   Gursinsky T., Jaeger J., Andreesen J.R., Soehling B.;
RT   "A selDABC cluster for selenocysteine incorporation in Eubacterium
RT   acidaminophilum.";
RL   Arch. Microbiol. 174:200-212(2000).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ245960; CAB53234.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S3K3; -.
DR   SMR; Q9S3K3; -.
DR   UniPathway; UPA00906; UER00896.
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; Selenium;
KW   Transferase.
FT   CHAIN           1..467
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000189602"
FT   MOD_RES         298
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   467 AA;  52470 MW;  2539B06FC0EEE771 CRC64;
     MDKRTLFSKL PSVDKILGND GVIELEKEYP RSLIVEVIRE QIELARKRIL ELNESDMEGF
     DIDEDILIND IGHQLKLKYA LKLKRLINAT GVVVHTNLGR SPMAEEIKED LWLIASRYSN
     LEYDIESGKR GSRYSHLEEI VRKITGAEDV LVVNNNAAAV MLVLGTMAQG KEVITSRGEL
     VEIGGSFRIP SVMEQSGAKL VEVGTTNKTY ASDYEAAITE NTGALLKVHT SNFRVVGFTN
     TPELEELREI GDKYDIPVIE DLGSGVFIDL SKYGLSYEPT VMDSLRKGAD IVTFSGDKIL
     GGPQAGIIVG KKKYIDKMKK NQLTRALRVD KFIICALEAT MRYYIEEEIA IKKIPTLRML
     TYKLDEIKEK AQRLNEMIGR LGIPAEVKIE VGHSQVGGGL LPLERIESRV ISIVPENMSV
     SRLEESLRLC DDHIIGRVYD EKYVIDVRTL FDEEYEIICN QLKSILG