SELA_PSEA7
ID SELA_PSEA7 Reviewed; 468 AA.
AC A6VCR3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=PSPA7_5527;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR84515.1; -; Genomic_DNA.
DR RefSeq; WP_012077530.1; NC_009656.1.
DR AlphaFoldDB; A6VCR3; -.
DR SMR; A6VCR3; -.
DR EnsemblBacteria; ABR84515; ABR84515; PSPA7_5527.
DR KEGG; pap:PSPA7_5527; -.
DR HOGENOM; CLU_038142_1_0_6; -.
DR OMA; GATNRTH; -.
DR OrthoDB; 1124266at2; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000001582; 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..468
FT /note="L-seryl-tRNA(Sec) selenium transferase"
FT /id="PRO_1000050374"
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ SEQUENCE 468 AA; 50456 MW; 8C63ABCAE3718C8A CRC64;
MSSVRLPSVD RLLRSAAAAP LHQRYGREAL LATLRDLLDE LREPARQGAL AAIELSEAVL
AGRAGERLAA QHASRVRRVF NLTGTVLHTN LGRALLPEEA IEAITLAARY PLNLEFDLAS
GKRGDRDDLI TGLIRELTGA EAVTVVNNNA AAVLLALNSL GARKEGIISR GELIEIGGAF
RIPDIMTRAG VRLHEVGTTN RTHARDYEAA IGPRSGLLMR VHTSNYSVQG FTASVPTAQL
AAIAHGHGLP LLEDLGSGTL VDLTRWGLPK EPTVQEALAD GADIVTFSGD KLLGGPQAGL
ILGNRELVGR IKKNPLKRAL RVDKLTLAAL EAVLGLYRDP DRLAERLTTL RLLSRPAVEI
RAQAERLAPA LAEALGEDWE VAVVDALGMI GSGAQPVARL ASAALCLRPR QPRRLRGRTL
RNLEEALRGL PLPVIGRLDD DALWLDLRQL DDEPAFRAQL PRLRGELS