ID   SPCS_METKA              Reviewed;         431 AA.
AC   Q8TXK0;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=MK0672;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC   -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC       tRNA(Sec) required for selenoprotein biosynthesis.
CC       {ECO:0000250|UniProtKB:Q6LZM9}.
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; AE009439; AAM01887.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TXK0; -.
DR   SMR; Q8TXK0; -.
DR   STRING; 190192.MK0672; -.
DR   EnsemblBacteria; AAM01887; AAM01887; MK0672.
DR   KEGG; mka:MK0672; -.
DR   PATRIC; fig|190192.8.peg.710; -.
DR   HOGENOM; CLU_022508_0_0_2; -.
DR   OMA; HIINGAY; -.
DR   UniPathway; UPA00906; UER00898.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0098621; F:phosphoseryl-selenocysteinyl-tRNA selenium transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Protein biosynthesis; Pyridoxal phosphate; Reference proteome; RNA-binding;
KW   Selenium; Transferase; tRNA-binding.
FT   CHAIN           1..431
FT                   /note="O-phosphoseryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000219882"
FT   REGION          1..36
FT                   /note="Tetramerization"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P6M7"
FT   REGION          88..98
FT                   /note="Phosphate loop (P-loop)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P6M7"
FT   BINDING         67
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZM9"
FT   SITE            66
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         269
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZM9"
SQ   SEQUENCE   431 AA;  47589 MW;  4557FD9AF640CA03 CRC64;
     MRGLIPDHML ERGRTVLDSY REPVERLLSE RRMPEEGWPD DVIATFLWEL SRMDTDKDPK
     AARIGEREAR VASRLAEESV FGFCHGVGRS GTLVDPQPKA PGASIMYALT NRLVTDFLRR
     LGFRIEGAFV VPGATGLSIA LCLSALGEGE EVIYPYAAHK SPIKAVRLAG FGMRVVDTEI
     EGDRIVVDPG DVEEALERSE SPAAVLSTLT FFPPRSSDPL PEIAELCEEY GVPHVVNAAY
     GIQHEQYRDL LNRAIKRGRV DVVVSSTDKN LLTPVGGGIV YAPDEETLRE VSRAYPGRAS
     AAPVAHALIS LLSLGMKGYR RLMRRQKECK ALLDELLEDL EARRDDVRVL DVDNPIASAV
     AVEGHDPVDL AARLYVRRVT GPRGVRADDP FGTSRLRGYH SNYITINAAI GVREEDVKTA
     VERLERELEG E