SELA_HAEIN
ID SELA_HAEIN Reviewed; 461 AA.
AC P43910;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=HI_0708;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22365.1; -; Genomic_DNA.
DR PIR; H64087; H64087.
DR RefSeq; NP_438866.1; NC_000907.1.
DR RefSeq; WP_005694593.1; NC_000907.1.
DR AlphaFoldDB; P43910; -.
DR SMR; P43910; -.
DR STRING; 71421.HI_0708; -.
DR PRIDE; P43910; -.
DR DNASU; 950262; -.
DR EnsemblBacteria; AAC22365; AAC22365; HI_0708.
DR KEGG; hin:HI_0708; -.
DR PATRIC; fig|71421.8.peg.738; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_6; -.
DR OMA; GATNRTH; -.
DR PhylomeDB; P43910; -.
DR BioCyc; HINF71421:G1GJ1-742-MON; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000000579; 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..461
FT /note="L-seryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000189605"
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ SEQUENCE 461 AA; 51127 MW; FDC5F721498670F3 CRC64;
MTALFQQLPS VDKILKTPQG LQLITEFGHT AVVATCRELL TQARQFIKKN NQLPEYFSNF
DRTFLEIHSH LQKQNQVQIK AVHNLTGTVL HTNLGRALWS EAAQQAALSA MQKNVSLEYD
LDEGKRSHRD NYISELLCKL TGAEAACIVN NNAAAVLLML ATFAQGKEVI ISRGELIEIG
GAFRIPDIME QAGCHLVEVG TTNRTHLKDY RNAITENTAF LMKVHSSNYQ ICGFTSSVSE
EELTELGQEM NVPVVTDLGS GALVDLSQYG LPKEPTVQEK IAQGVDLVSF SGDKLLGGVQ
AGIIVGKKEW IEQLQAHPLK RVLRCDKVIL AGLEATLRLY LNPEKLTEKL PTLRLLTQPL
KQLKINAMRL KERLESRLNS QFELQIEASQ AQIGSGSQPM ERIPSVAVTI AEKTNAKLSA
LSARFKQLSQ PIIGRMENGK IWLDLRSLAD IETLLNTLDE L
