SPCS_METJA
ID SPCS_METJA Reviewed; 434 AA.
AC Q58027;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase;
DE EC=2.9.1.2 {ECO:0000250|UniProtKB:Q6LZM9};
DE AltName: Full=Selenocysteine synthase;
DE Short=Sec synthase;
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase;
DE AltName: Full=Sep-tRNA:Sec-tRNA synthase;
DE Short=SepSecS;
GN Name=spcS; OrderedLocusNames=MJ0610;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, PYRIDOXAL PHOSPHATE AT LYS-277, AND MUTAGENESIS OF LYS-277.
RX PubMed=17142313; DOI=10.1073/pnas.0609703104;
RA Yuan J., Palioura S., Salazar J.C., Su D., O'Donoghue P., Hohn M.J.,
RA Cardoso A.M., Whitman W.B., Soell D.;
RT "RNA-dependent conversion of phosphoserine forms selenocysteine in
RT eukaryotes and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18923-18927(2006).
CC -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC tRNA(Sec) required for selenoprotein biosynthesis.
CC {ECO:0000269|PubMed:17142313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-
CC selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041,
CC Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:78573; EC=2.9.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q6LZM9};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q6LZM9};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (archaeal/eukaryal route): step 2/2. {ECO:0000250|UniProtKB:Q6LZM9}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q6LZM9}.
CC -!- SIMILARITY: Belongs to the SepSecS family. {ECO:0000305}.
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DR EMBL; L77117; AAB98603.1; -; Genomic_DNA.
DR PIR; B64376; B64376.
DR RefSeq; WP_010870114.1; NC_000909.1.
DR AlphaFoldDB; Q58027; -.
DR SMR; Q58027; -.
DR STRING; 243232.MJ_0610; -.
DR EnsemblBacteria; AAB98603; AAB98603; MJ_0610.
DR GeneID; 1451475; -.
DR KEGG; mja:MJ_0610; -.
DR eggNOG; arCOG00119; Archaea.
DR HOGENOM; CLU_022508_0_0_2; -.
DR InParanoid; Q58027; -.
DR OMA; HIINGAY; -.
DR OrthoDB; 16805at2157; -.
DR BRENDA; 2.9.1.2; 3260.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0098621; F:phosphoseryl-selenocysteinyl-tRNA selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR019872; Sec-tRNA_Se_transferase.
DR InterPro; IPR008829; SepSecS/SepCysS.
DR PANTHER; PTHR12944; PTHR12944; 1.
DR Pfam; PF05889; SepSecS; 1.
DR PIRSF; PIRSF017689; SepSecS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03531; selenium_SpcS; 1.
PE 1: Evidence at protein level;
KW Protein biosynthesis; Pyridoxal phosphate; Reference proteome; RNA-binding;
KW Selenium; Transferase; tRNA-binding.
FT CHAIN 1..434
FT /note="O-phosphoseryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000219881"
FT REGION 1..40
FT /note="Tetramerization"
FT /evidence="ECO:0000250|UniProtKB:Q6P6M7"
FT REGION 92..102
FT /note="Phosphate loop (P-loop)"
FT /evidence="ECO:0000250|UniProtKB:Q6P6M7"
FT BINDING 71
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT SITE 70
FT /note="May act as a substrate filter by repelling compounds
FT with a negatively charged alpha-carboxylate"
FT /evidence="ECO:0000250"
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q6LZM9,
FT ECO:0000269|PubMed:17142313"
FT MUTAGEN 277
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17142313"
SQ SEQUENCE 434 AA; 48684 MW; 09AFBC5819613EF5 CRC64;
MGLNITGLIP KHMENRGKLT LKENLKIIEN ILEQRKAPEN GIDEEHIKLL LRLLSFMDTD
KDPNVVQIGE REARVYTKLQ RDGVFDFCHG VGRSGNLIDP QPKAPGASVM YKLTNKLLES
FLKALGLKVN AIATPVATGM SLALCLSAAR KKYNSNVVIY PYAAHKSPIK ATSFIGMRMR
LVETVLDGDI VKVEVSDIED AIRKEINENN NPVVLSTLTF FPPRKSDDIK EIAKICQDYD
IPHIINGAYA IQNFYYIEKL KKALKYRIDA VVSSSDKNLF TPIGGGIIYT KDESFLKEIS
LTYPGRASAN PIVNILISLL AIGTKDYLNL MKEQKECKKL LNELLEDLAK KKGEKVLNVE
NPISSCITTK KDPLDVAGKL YNLRVTGPRG VRRNDKFGTC YLKEYPYDYI VVNSAIGVKK
EDIYKVIEKL DEVL
