SCLY_XENTR
ID SCLY_XENTR Reviewed; 431 AA.
AC Q5U4Q9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Selenocysteine lyase;
DE EC=4.4.1.16;
GN Name=scly;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH84987.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC084987; AAH84987.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001011164.1; NM_001011164.1.
DR RefSeq; XP_012825815.1; XM_012970361.2.
DR RefSeq; XP_017949356.1; XM_018093867.1.
DR AlphaFoldDB; Q5U4Q9; -.
DR SMR; Q5U4Q9; -.
DR STRING; 8364.ENSXETP00000010463; -.
DR PaxDb; Q5U4Q9; -.
DR DNASU; 496582; -.
DR Ensembl; ENSXETT00000026454; ENSXETP00000026454; ENSXETG00000026777.
DR GeneID; 496582; -.
DR KEGG; xtr:496582; -.
DR CTD; 51540; -.
DR Xenbase; XB-GENE-485701; scly.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_0_0_1; -.
DR InParanoid; Q5U4Q9; -.
DR OrthoDB; 697150at2759; -.
DR Reactome; R-XTR-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000026777; Expressed in early embryo and 16 other tissues.
DR ExpressionAtlas; Q5U4Q9; differential.
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..431
FT /note="Selenocysteine lyase"
FT /id="PRO_0000317016"
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 431 AA; 46993 MW; E70B89260137E797 CRC64;
MADAESQNGE NHLPHKIYLD YNATTPPATE VVKAVEEALR EAWGNPSSSY TAGCKAKELI
DTARAHVAKM VGGKPEDIIF TSGGTEANNM VLFSTVENFN STSKERQNNR VALALPHIIT
SNVEHDSVAL PLLHLQKTHR AEITFVPVST VTGRIEVEDI ISAVRPNTCL VSIMLANNET
GVIMPVGELS QCLASMSKER SAQGLPKILL HTDAAQALGK VEVDVQELGV NYLTIVGHKF
YGPRIGALYV RGLGQHSSLL PMLYGGGQER NFRPGTENTP MIAGLGKAAE LVFLHCAVYE
AHMRRIRDYL EERLEAVFED RIRLNSRFPG AERLPNTCNV SLLKPAMLGH EWLSHCQYLQ
ASIGAACHSD RGDRPSPVLL NSGVPQEAAT SAVRLSVGRE TSQDDVDLIV RDLEQAAQLL
GVNKKSLKKL P