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Database: UniProt
Entry: K8WLD0_9GAMM
LinkDB: K8WLD0_9GAMM
Original site: K8WLD0_9GAMM 
ID   K8WLD0_9GAMM            Unreviewed;       463 AA.
AC   K8WLD0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000256|HAMAP-Rule:MF_00423};
DE            EC=2.9.1.1 {ECO:0000256|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteine synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE            Short=Sec synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|HAMAP-Rule:MF_00423};
GN   Name=selA {ECO:0000256|HAMAP-Rule:MF_00423};
GN   ORFNames=OO7_01601 {ECO:0000313|EMBL:EKT61359.1};
OS   Providencia sneebia DSM 19967.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT61359.1, ECO:0000313|Proteomes:UP000010290};
RN   [1] {ECO:0000313|EMBL:EKT61359.1, ECO:0000313|Proteomes:UP000010290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT61359.1,
RC   ECO:0000313|Proteomes:UP000010290};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(2012).
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00423};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000256|PIRSR:PIRSR618319-50};
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:0000256|HAMAP-Rule:MF_00423}.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers. Binds only one seryl-
CC       tRNA(Sec) per dimer. {ECO:0000256|HAMAP-Rule:MF_00423}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00423}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKT61359.1}.
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DR   EMBL; AKKN01000002; EKT61359.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8WLD0; -.
DR   PATRIC; fig|1141660.3.peg.317; -.
DR   HOGENOM; CLU_038142_1_0_6; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000010290; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1150.180; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR00474; selA; 1.
DR   PANTHER; PTHR32328; L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR   PANTHER; PTHR32328:SF0; L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR   Pfam; PF12390; Se-cys_synth_N; 1.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00423};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00423}; Reference proteome {ECO:0000313|Proteomes:UP000010290};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:EKT61359.1}.
FT   DOMAIN          9..48
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         295
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   463 AA;  50934 MW;  5581B4549D268B9F CRC64;
     MPDSNASLYR QLPSIDKLLQ LSDVQALVEK SGLHWVTENL RSMQEQAREC IQQQGSLPSW
     HDNWGAKLVQ NHDAMQESAL KSVFNLTGTV LHTNLGRAVM AQSAMTAVSR VMSSPVTLEY
     SLDGATRGHR DRPLADLLCQ LTGAEDACIV NNNAAAVLLL LATLAQGRQV IVSRGELVEI
     GGAFRVPDVM SQAGCQLVEV GTTNRTHLRD YEHAINENTA LLMKVHTSNY SIEGFTAEVD
     GAQLAQLGQQ YQLPTAIDLG SGSMVDMGKY GLPVEPMPHT YLAQGIDLVS ISGDKLLGGP
     QAGIILGKKK WIEAIQKHPL KRALRADKMT LAALEATLQL YLTPEKLVSE LPTLRWLTRD
     AEEIKTRAER ILVPLQAFYG DNFIVEIEQC QSQIGSGSLP VDRLPSYAIT FSPLEKHGYS
     LAQLAEHWRQ SPQPVIGRLK EGKLWLDLRC LDDEHSLLQV LLS
//
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