ID   SELA_KLEP3              Reviewed;         462 AA.
AC   B5XMW1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=KPK_0157;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI10056.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XMW1; -.
DR   SMR; B5XMW1; -.
DR   EnsemblBacteria; ACI10056; ACI10056; KPK_0157.
DR   KEGG; kpe:KPK_0157; -.
DR   HOGENOM; CLU_038142_1_0_6; -.
DR   OMA; GATNRTH; -.
DR   OrthoDB; 1124266at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000001734; 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; Selenium;
KW   Transferase.
FT   CHAIN           1..462
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_1000124146"
FT   MOD_RES         295
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   462 AA;  50495 MW;  5F72D8DA97727875 CRC64;
     MTTDIRALYT RLPAIDRLLR DPAFSPLLAQ HGHSQVVAQL RQMLDEAREQ ISQRQTLPDW
     SHDWLHACEQ RLTAGQRSAL RPVFNLTGTV LHTNLGRAIQ AESAVEAVAS AMRAPVTLEY
     DLDDAGRGHR DRAIADLLCQ ITGAEDACIV NNNAAAVLLM LAATASGREV VVSRGELVEI
     GGAFRIPDVM RQAGCQLHEV GTTNRTHAKD YRQAVNDNTA LLMKVHTSNY SIEGFTKAVD
     EAELAAIGRE LDIPVVADLG SGSLVDLSQY GLPKEPMPQE MIAAGVSLVS FSGDKLLGGP
     QAGIIVGKRA LIARLQSHPL KRALRADKMT LAALEATLRL YQHPEVLTER LPTLRLLTRP
     AEEIRRLAER LLPDLAAHYA DFAVSVAACQ SQIGSGSLPV DRLPSAALTF TPHDGRGSRL
     EALAARWRAL PCPVIGRIDD GRLWLDLRCL EDETRFMEML LR