(data stored in ACNUC7421 zone)

SWISSPROT: SELA_PARDP

ID   SELA_PARDP              Reviewed;         466 AA.
AC   A1AYS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=Pden_0301;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000489; ABL68415.1; -; Genomic_DNA.
DR   RefSeq; WP_011746648.1; NC_008686.1.
DR   SMR; A1AYS1; -.
DR   STRING; 318586.Pden_0301; -.
DR   PRIDE; A1AYS1; -.
DR   EnsemblBacteria; ABL68415; ABL68415; Pden_0301.
DR   KEGG; pde:Pden_0301; -.
DR   eggNOG; ENOG4105C1Y; Bacteria.
DR   eggNOG; COG1921; LUCA.
DR   HOGENOM; HOG000163726; -.
DR   KO; K01042; -.
DR   OMA; GATNRTH; -.
DR   BioCyc; PDEN318586:G1GW1-295-MONOMER; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
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;
DR   PRODOM; A1AYS1.
DR   SWISS-2DPAGE; A1AYS1.
KW   Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Selenium; Transferase.
FT   CHAIN           1..466
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_1000050373"
FT   MOD_RES         293
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   466 AA;  49843 MW;  DC5E07766E655033 CRC64;
     MDPRSTLPSI DRLLRQAEAR ELIAHHGRDN VVGMLRRLLQ DRRMAAGRGD RAAGERAAGE
     GVLDECAERL AAQARPSLRP VLNLTGTVNH TNLGRALLSR RAAEAAFRAM ISATNLEYDL
     ERGTRGDRDS HVEALICRLT GAEAATVVNN NAAAVMLMLN TLALGREVVV SRGELVEIGG
     AFRVPDVMAR AGCRLHEVGT TNRTHLRDFA NAVNEDTAAF MKVHASNYAI EGFTAEVPQA
     DLAALARRHG IPLLIDLGSG SLLDLDAFGL PPEPTARQAI RDGADAVTFS GDKLLGGPQC
     GIIAGSRALV DRMRANPLKR ALRVDKIILA ALAETLQSHG DPERARAEIP TLRLLTRPQD
     EIRALAERLC PPVHAALSGL AEVRVVDCLS QIGSGAQPVD LLPSAGLGFA ETGAVPVSRI
     AQAFRDLPLP VIGRVHKGEF LLDLRCLEDE TPFLAQLDRL ALAGPA
//

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