ID   SELA_SHEON              Reviewed;         473 AA.
AC   Q8EKI8;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=SO_0105;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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}.
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DR   EMBL; AE014299; AAN53192.1; -; Genomic_DNA.
DR   RefSeq; NP_715747.1; NC_004347.2.
DR   RefSeq; WP_011070513.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EKI8; -.
DR   SMR; Q8EKI8; -.
DR   STRING; 211586.SO_0105; -.
DR   PaxDb; Q8EKI8; -.
DR   PRIDE; Q8EKI8; -.
DR   DNASU; 1168002; -.
DR   KEGG; son:SO_0105; -.
DR   PATRIC; fig|211586.12.peg.104; -.
DR   eggNOG; COG1921; Bacteria.
DR   HOGENOM; CLU_038142_1_0_6; -.
DR   OMA; GATNRTH; -.
DR   OrthoDB; 1124266at2; -.
DR   PhylomeDB; Q8EKI8; -.
DR   BioCyc; SONE211586:G1GMP-101-MON; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IBA:GO_Central.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IBA:GO_Central.
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..473
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000189617"
FT   MOD_RES         302
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   473 AA;  51341 MW;  C333A2F7A42DBCC2 CRC64;
     MMTQVPDTPQ ALYRALPSMD SLLADAVLAP LLQRYGKAAV KAALDSQLRT ARELIAQERR
     LPAWCANPSL LNGYLVDQLS KDYSHSLKPV WNLTGTILHT NLGRAQQSEA AIRAVTSVMR
     YPTPLEFELA AGERGHRDNA ISGLIQRLTG AEACCVVNNN AAAVLLMLSA VAAGKEVIVS
     RGELVEIGGA FRIPDIMRQA GCTLVEVGST NRTHLKDYEQ AITENTAAIM KVHTSNYHIS
     GFTAAVEEAR LGQLCRERGI LLISDLGSGS LTDLRRFGLK QEPTPQAMLA DGVDLVSFSG
     DKLLGGPQSG LIVGKQALIN KLQSHPLKRA LRCDKLILAA LEATLIHYLN PETLDKELPI
     MAKFARSQAE LRQIGERLQQ ALAPLFTPSY GLELVECQTQ VGSGSQPDTF LPSIGLCFNA
     QEGGSLTLLE QHFKQAQRPV IGRMTQDQLR LDLRGIDDEA ELLAELSTLG VQL