ID   SCLY_XENLA              Reviewed;         426 AA.
AC   Q66IQ6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Selenocysteine lyase;
DE            EC=4.4.1.16;
GN   Name=scly;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine
CC       and elemental selenium. {ECO:0000250|UniProtKB:Q68FT9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC         alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC         ChEBI:CHEBI:57972; EC=4.4.1.16;
CC         Evidence={ECO:0000250|UniProtKB:Q68FT9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11633;
CC         Evidence={ECO:0000250|UniProtKB:Q68FT9};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q68FT9};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q68FT9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9JLI6}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; BC081243; AAH81243.1; -; mRNA.
DR   RefSeq; NP_001087800.1; NM_001094331.1.
DR   AlphaFoldDB; Q66IQ6; -.
DR   SMR; Q66IQ6; -.
DR   MaxQB; Q66IQ6; -.
DR   DNASU; 447624; -.
DR   GeneID; 447624; -.
DR   KEGG; xla:447624; -.
DR   CTD; 447624; -.
DR   Xenbase; XB-GENE-6077566; scly.L.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 447624; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0009000; F:selenocysteine lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..426
FT                   /note="Selenocysteine lyase"
FT                   /id="PRO_0000317015"
FT   ACT_SITE        367
FT                   /note="S-selanylcysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FT9"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FT9"
SQ   SEQUENCE   426 AA;  46263 MW;  BD53EF03FC70C6B4 CRC64;
     MVDTESQKEK NHLNHKIYLD YNATTPPARE VVGTVAEALQ EAWGNPSSSY TAGCKAKELI
     DTARARIAKM VGGKPEDIIF TSGGTEANNM VLFSAVENFN RTSKERQNNN VDWALPHIIT
     SNVEHDSVAL PLLQLQKTHK AEITFVPVST VTGRVEVEDV ISAVRPNTCL VSIMLANNET
     GVIMPVGELS QCLASLSRKR SAQGLPEILL HTDAAQALGK VEVDVQELGV NYLTIVGHKF
     YGPRIGALYV GGLGHQSPLL PMLYGGGREG NFRPGTENTP MIAGLGQAAE LVSLHCAAYE
     VHMRRIRDYL EQKLEAVFGD RIRLNSRFPG AERLPNTCNV SLLKPAVLGR EWLSHCQYLQ
     ASVGAACHSD RGDSPSPVLL KSGVPQDAAR SAVRLSVGRE TSQDDVDLIV RDLEQAAQLL
     GMNKQS