SELA_PASMU
ID SELA_PASMU Reviewed; 460 AA.
AC Q9CK66;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=PM1768;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03852.1; -; Genomic_DNA.
DR RefSeq; WP_010907322.1; NC_002663.1.
DR AlphaFoldDB; Q9CK66; -.
DR SMR; Q9CK66; -.
DR STRING; 747.DR93_172; -.
DR EnsemblBacteria; AAK03852; AAK03852; PM1768.
DR KEGG; pmu:PM1768; -.
DR PATRIC; fig|272843.6.peg.1790; -.
DR HOGENOM; CLU_038142_1_0_6; -.
DR OMA; GATNRTH; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000000809; 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..460
FT /note="L-seryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000189610"
FT MOD_RES 293
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ SEQUENCE 460 AA; 50668 MW; FF96AB86AA0BCDD7 CRC64;
MSLYSSLPSI DKLLKTPEGA RLSHEFGHTA VVNICRQLIE QGREYIKNEN KLLPVFQDIS
DTLREIELQL HAQSQVKIQS VHNLTGTILH TNLGRALWSD AAQHAALTSM SHNVALEYDL
EEGKRSHRDH YISDLLCQLT GAEAACIVNN NAAAVLLMLA TFAQGKEVII SRGELIEIGG
AFRIPDIMQQ AGCKLVEVGT TNRTHLSDYR HAINENTAFL MKVHSSNYQI CGFTKSVTEA
ELVTLAREFN LPVMTDLGSG ALVDLAQYGL PKEPTVQEKW AQGVELISFS GDKLLGGPQA
GIIVGKKAWI DRLQTHPLKR ALRCDKVILA GLEATLRLYL QPEKLSQHLT TLRLLTQPVE
ALHEQAEQLQ SVLLTKLTTD YSVAITNSVA QIGSGSQPMA TIPSVAVTIS TEKAGKLTAL
LQRFKALPQP IICRVEKEKI WLDLRGLADI DSLLKTIMQL