ID B8C339_THAPS Unreviewed; 476 AA.
AC B8C339;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase {ECO:0000256|ARBA:ARBA00021963};
DE EC=2.9.1.2 {ECO:0000256|ARBA:ARBA00012464};
DE AltName: Full=Selenocysteine synthase {ECO:0000256|ARBA:ARBA00030669};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|ARBA:ARBA00032048};
DE AltName: Full=Sep-tRNA:Sec-tRNA synthase {ECO:0000256|ARBA:ARBA00032693};
DE Flags: Fragment;
GN ORFNames=THAPSDRAFT_262555 {ECO:0000313|EMBL:EED92493.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:EED92493.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED92493.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED92493.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:EED92493.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED92493.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
CC -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC tRNA(Sec) required for selenoprotein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00002552}.
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:0000256|ARBA:ARBA00001746};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR017689-50};
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:0000256|ARBA:ARBA00004822}.
CC -!- SIMILARITY: Belongs to the SepSecS family.
CC {ECO:0000256|ARBA:ARBA00007037}.
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DR EMBL; CM000642; EED92493.1; -; Genomic_DNA.
DR RefSeq; XP_002290741.1; XM_002290705.1.
DR AlphaFoldDB; B8C339; -.
DR STRING; 35128.B8C339; -.
DR PaxDb; 35128-Thaps262555; -.
DR EnsemblProtists; EED92493; EED92493; THAPSDRAFT_262555.
DR GeneID; 7450104; -.
DR KEGG; tps:THAPSDRAFT_262555; -.
DR eggNOG; KOG3843; Eukaryota.
DR HOGENOM; CLU_022508_0_0_1; -.
DR InParanoid; B8C339; -.
DR OMA; MSHANDY; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000001449; Chromosome 5.
DR GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:InterPro.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR03531; selenium_SpcS; 1.
DR PANTHER; PTHR12944:SF2; O-PHOSPHOSERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR PANTHER; PTHR12944; SOLUBLE LIVER ANTIGEN/LIVER PANCREAS ANTIGEN; 1.
DR Pfam; PF05889; SepSecS; 1.
DR PIRSF; PIRSF017689; SepSecS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR017689-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRSR:PIRSR017689-
KW 50};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PIRSR:PIRSR017689-
KW 50}.
FT BINDING 51
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 407
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 472
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT SITE 50
FT /note="May act as a substrate filter by repelling compounds
FT with a negatively charged alpha-carboxylate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
FT MOD_RES 287
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED92493.1"
FT NON_TER 476
FT /evidence="ECO:0000313|EMBL:EED92493.1"
SQ SEQUENCE 476 AA; 51829 MW; D85B9F02D906E6FD CRC64;
ASNSQTKALF HHKRLPDHGW TDVQIQRLLL ELSVLDTNCE ESVKWTGAGE REGRIYAPLV
SQRHFGFGHG IGRSGDVMEA QPKAVGSSAL LRLTLRLTLD AVRRGAGLNG TLGKGDSRNG
PASFGTLLPV CTGMSMALVL SGLRDRARTL DSASIGTEHV NTERNIVLWS RIDQKSCYKS
ILSAGLKCVV LPTKKHPDTD EVSTDLEALK EALDSFGNSI LAVLTTTSCF CPRVPDEVDQ
VAKMIMSAGV SHVVNHAYGL QCQTTNKLLN RACIIGRVDA IICSTDKNFL VPVGGALILS
PDSNVIETIS KNYPGRASSS PMVDLFITLL SMGLNGYKGI LEERKRLTEL FGQSLQRVAT
VFGETVLNCP RNTISFGMTL DNLATINGSD DELNSLITKF GSMLFTRCIS GTRVVPRGST
KTISGHTFEG FGSSNDDYPY AYMTSACAVG MGEEEMNEFF VRLEKSWIDY RKKLEQ
//