SELA_PSEPK
ID SELA_PSEPK Reviewed; 475 AA.
AC Q88QJ8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PP_0493;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(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}.
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; AE015451; AAN66122.1; -; Genomic_DNA.
DR RefSeq; NP_742658.1; NC_002947.4.
DR RefSeq; WP_010951785.1; NC_002947.4.
DR AlphaFoldDB; Q88QJ8; -.
DR SMR; Q88QJ8; -.
DR STRING; 160488.PP_0493; -.
DR EnsemblBacteria; AAN66122; AAN66122; PP_0493.
DR KEGG; ppu:PP_0493; -.
DR PATRIC; fig|160488.4.peg.525; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_6; -.
DR OMA; GATNRTH; -.
DR PhylomeDB; Q88QJ8; -.
DR BioCyc; PPUT160488:G1G01-541-MON; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000000556; 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..475
FT /note="L-seryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000189613"
FT MOD_RES 297
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ SEQUENCE 475 AA; 51724 MW; 1CB067F80E0B6658 CRC64;
MSNSLASDTP RLPSIDTLLR HPACLPLIDR HGRDAVLNTL RQLLDDLREP ARNGELGSAE
LAPEILLGRS GERLALQQRS QVRRVFNLTG TVLHTNLGRA LLPDEAIEAM QTAARYPLNL
EFDLATGKRG DRDDLIEGLI RELTGAEAVT VVNNNAAAVL LALNSLGARK EGIISRGELI
EIGGAFRIPD IMARAGVKLH EVGTTNRTHA RDYEAAIGPR TGLLMRVHCS NYSIQGFTTQ
VPTAELARIA HQHELPLLED LGSGSLLDLT RWGLPAEPTV RQALADGADI VTFSGDKLLG
GPQAGIIVGH KDLITRIKKN PLKRALRVDK ITLAALEAVL ALYRNPDRLA ERLPSLRLLT
RSQAEIQAQA ERLAPELQAR LGEQWAISVE PALGMIGSGS QPVARLPSAA LCLRPQVSKK
LRGRSLHVLE RALRDLPVPV LGRIDDDALW LDLRQLDDEA QWLAQLPALQ LGPVQ