ID B7FV74_PHATC Unreviewed; 512 AA.
AC B7FV74;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 08-NOV-2023, entry version 69.
DE RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase {ECO:0000256|ARBA:ARBA00021963, ECO:0000256|PIRNR:PIRNR017689};
DE EC=2.9.1.2 {ECO:0000256|ARBA:ARBA00012464, ECO:0000256|PIRNR:PIRNR017689};
DE AltName: Full=Selenocysteine synthase {ECO:0000256|ARBA:ARBA00030669, ECO:0000256|PIRNR:PIRNR017689};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|ARBA:ARBA00032048, ECO:0000256|PIRNR:PIRNR017689};
DE AltName: Full=Sep-tRNA:Sec-tRNA synthase {ECO:0000256|ARBA:ARBA00032693, ECO:0000256|PIRNR:PIRNR017689};
GN ORFNames=PHATRDRAFT_26649 {ECO:0000313|EMBL:EEC49787.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC49787.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:EEC49787.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC49787.1,
RC ECO:0000313|Proteomes:UP000000759};
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).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC tRNA(Sec) required for selenoprotein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00002552, ECO:0000256|PIRNR:PIRNR017689}.
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 ECO:0000256|PIRNR:PIRNR017689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR017689, 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 ECO:0000256|PIRNR:PIRNR017689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR017689}.
CC -!- SIMILARITY: Belongs to the SepSecS family.
CC {ECO:0000256|ARBA:ARBA00007037, ECO:0000256|PIRNR:PIRNR017689}.
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DR EMBL; CM000608; EEC49787.1; -; Genomic_DNA.
DR RefSeq; XP_002179089.1; XM_002179053.1.
DR AlphaFoldDB; B7FV74; -.
DR STRING; 556484.B7FV74; -.
DR PaxDb; 2850-Phatr26649; -.
DR EnsemblProtists; Phatr3_J26649.t1; Phatr3_J26649.p1; Phatr3_J26649.
DR GeneID; 7199666; -.
DR KEGG; pti:PHATRDRAFT_26649; -.
DR eggNOG; KOG3843; Eukaryota.
DR HOGENOM; CLU_022508_0_0_1; -.
DR InParanoid; B7FV74; -.
DR OMA; MSHANDY; -.
DR OrthoDB; 121300at2759; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000000759; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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 Cytoplasm {ECO:0000256|PIRNR:PIRNR017689};
KW Protein biosynthesis {ECO:0000256|PIRNR:PIRNR017689};
KW Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR017689,
KW ECO:0000256|PIRSR:PIRSR017689-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017689};
KW Selenium {ECO:0000256|PIRNR:PIRNR017689};
KW Transferase {ECO:0000256|PIRNR:PIRNR017689};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555,
KW ECO:0000256|PIRNR:PIRNR017689}.
FT BINDING 90
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 441
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 506
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT SITE 89
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 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
SQ SEQUENCE 512 AA; 55385 MW; 10A80494129961F8 CRC64;
MNSVDELTTA LTALHIPSTH VTVGVANLIA SHKDLRTLLV NRRLPEHGWS DVQIQHVLYT
MATLDTNNKR SGSSSSDDSG SSRWCGVGER EGRVYSALVS SRHFGLSHGV GRSGDIAEPQ
PKALGSTVLA KLTLCLVLDA VRRGSGLHPQ TAAKSGILLP LCTGMSMALV LGTLRQLQDN
HQTSANAAIK PYRNIVLWSR IDQKSCFKAI QSAGLECVVV PTRLAGDAVV TDLDAFQASL
LTYGDRVLAV VTTTSCFAPR VPDQVDAVAR LCAEQCVPHV INNAYGLQSS DTSKLLNRAC
AVGRVDAIVC STDKNFMVPI GGAIVLSPDE SLIQNVGKVY AGRASASPML DLFITLCSMG
LRGYQQLLTS RRILLPTFTE RLKEVANKYG ERVLECRTNC ISFGVTLDGL VRPPRQDEDD
VAYRTSVSRD VSSLGAMLFQ RCVSGTRVVP RGTVQRMGGM EFCGFGSSHD AYPHAYLTAA
CAIGLTASEG DDFFTRLDQT LHEFQKRQRR RA
//
