ID   SCLY_BOVIN              Reviewed;         437 AA.
AC   A2VDS1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Selenocysteine lyase;
DE            EC=4.4.1.16;
GN   Name=SCLY;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) 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; BC133375; AAI33376.1; -; mRNA.
DR   RefSeq; NP_001077273.1; NM_001083804.1.
DR   AlphaFoldDB; A2VDS1; -.
DR   SMR; A2VDS1; -.
DR   STRING; 9913.ENSBTAP00000013719; -.
DR   PaxDb; A2VDS1; -.
DR   PeptideAtlas; A2VDS1; -.
DR   PRIDE; A2VDS1; -.
DR   Ensembl; ENSBTAT00000013719; ENSBTAP00000013719; ENSBTAG00000017826.
DR   GeneID; 790815; -.
DR   KEGG; bta:790815; -.
DR   CTD; 51540; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017826; -.
DR   VGNC; VGNC:55677; SCLY.
DR   eggNOG; KOG1549; Eukaryota.
DR   GeneTree; ENSGT00940000157773; -.
DR   HOGENOM; CLU_003433_0_0_1; -.
DR   InParanoid; A2VDS1; -.
DR   OMA; IIYGQSE; -.
DR   OrthoDB; 697150at2759; -.
DR   TreeFam; TF313550; -.
DR   Reactome; R-BTA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000017826; Expressed in cortex of kidney and 104 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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   Acetylation; Cytoplasm; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..437
FT                   /note="Selenocysteine lyase"
FT                   /id="PRO_0000317011"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        380
FT                   /note="S-selanylcysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FT9"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96I15"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FT9"
SQ   SEQUENCE   437 AA;  47204 MW;  66B92AA026AEC039 CRC64;
     MEAAGARNRD ARSRAEKSPP ESRKVYMDYN ATTPLEPEVI EAMTEAMREA WGNPSSSYPA
     GRKAKEIINT ARENLAKMIG GQPQDVIFTS GGTESNNLVI QSVVKHFHKV HAANGDTGGH
     PNPVDGALPH IITCTVEHDS IRLPLEHLRE ERVAEVTFVP VSKVNGQVEA EDILAAVRPA
     TCLVTIMLAN NETGVIMPVP EISRRVRALN QQRVAGGLPG VLVHTDAAQA LGKQRVDVRD
     LGVDFLTIVG HKFYGPRIGA LYVRGLGEHT PLYPMLFGGG QERNFRPGTE NTPMIAGLGK
     AAELVAENGE AYEAHMRGVR DYLEERLAAE FGERIHLNSQ FPGAERLPNT CNFSIRGPQL
     QGRAVLAQCR TLLASVGAAC HSDLGDRPSP VLLSCGVPVD VARNAIRLSV GRSSTRAEVD
     LVVQDLKQAV ARLEGQA