SCLY_RAT
ID SCLY_RAT Reviewed; 432 AA.
AC Q68FT9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Selenocysteine lyase {ECO:0000305};
DE EC=4.4.1.16 {ECO:0000269|PubMed:20164179};
GN Name=Scly;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL-PHOSPHATE,
RP COFACTOR, SUBUNIT, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-375.
RX PubMed=20164179; DOI=10.1074/jbc.m109.084475;
RA Omi R., Kurokawa S., Mihara H., Hayashi H., Goto M., Miyahara I.,
RA Kurihara T., Hirotsu K., Esaki N.;
RT "Reaction mechanism and molecular basis for selenium/sulfur discrimination
RT of selenocysteine lyase.";
RL J. Biol. Chem. 285:12133-12139(2010).
CC -!- FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine
CC and elemental selenium. {ECO:0000269|PubMed:20164179}.
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:0000269|PubMed:20164179};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11633;
CC Evidence={ECO:0000305|PubMed:20164179};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20164179};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 mM for L-selenocysteine {ECO:0000269|PubMed:20164179};
CC Vmax=26 umol/min/mg enzyme {ECO:0000269|PubMed:20164179};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20164179}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079358; AAH79358.1; -; mRNA.
DR RefSeq; NP_001007756.1; NM_001007755.1.
DR PDB; 3A9X; X-ray; 2.00 A; A/B=1-432.
DR PDB; 3A9Y; X-ray; 1.85 A; A/B=1-432.
DR PDB; 3A9Z; X-ray; 1.55 A; A/B=1-432.
DR PDBsum; 3A9X; -.
DR PDBsum; 3A9Y; -.
DR PDBsum; 3A9Z; -.
DR AlphaFoldDB; Q68FT9; -.
DR SMR; Q68FT9; -.
DR STRING; 10116.ENSRNOP00000027220; -.
DR PaxDb; Q68FT9; -.
DR PRIDE; Q68FT9; -.
DR Ensembl; ENSRNOT00000027220; ENSRNOP00000027220; ENSRNOG00000020083.
DR GeneID; 363285; -.
DR KEGG; rno:363285; -.
DR UCSC; RGD:1359514; rat.
DR CTD; 51540; -.
DR RGD; 1359514; Scly.
DR eggNOG; KOG1549; Eukaryota.
DR GeneTree; ENSGT00940000157773; -.
DR HOGENOM; CLU_003433_0_0_1; -.
DR InParanoid; Q68FT9; -.
DR OMA; IIYGQSE; -.
DR OrthoDB; 697150at2759; -.
DR PhylomeDB; Q68FT9; -.
DR TreeFam; TF313550; -.
DR BRENDA; 4.4.1.16; 5301.
DR Reactome; R-RNO-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR EvolutionaryTrace; Q68FT9; -.
DR PRO; PR:Q68FT9; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000020083; Expressed in adult mammalian kidney and 18 other tissues.
DR Genevisible; Q68FT9; RN.
DR GO; GO:1902494; C:catalytic complex; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016597; F:amino acid binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0009000; F:selenocysteine lyase activity; IMP:CAFA.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070279; F:vitamin B6 binding; IDA:CAFA.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:1900408; P:negative regulation of cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0001887; P:selenium compound metabolic process; ISO:RGD.
DR GO; GO:0016261; P:selenocysteine catabolic process; IMP:CAFA.
DR DisProt; DP00620; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Lyase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..432
FT /note="Selenocysteine lyase"
FT /id="PRO_0000317014"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="S-selanylcysteine intermediate"
FT /evidence="ECO:0000269|PubMed:20164179"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96I15"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I15"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:20164179,
FT ECO:0007744|PDB:3A9X, ECO:0007744|PDB:3A9Y,
FT ECO:0007744|PDB:3A9Z"
FT MUTAGEN 375
FT /note="C->A: Loss of selenocysteine lyase activity."
FT /evidence="ECO:0000269|PubMed:20164179"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 87..108
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3A9Z"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3A9Z"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 194..211
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:3A9Z"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3A9Z"
FT TURN 259..263
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 287..326
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:3A9Z"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:3A9Z"
FT HELIX 411..429
FT /evidence="ECO:0007829|PDB:3A9Z"
SQ SEQUENCE 432 AA; 47256 MW; FA5BB9DD941516A0 CRC64;
MDVARNGARG SVESPPNRKV YMDYNATTPL EPEVIQAVTE AMKEAWGNPS SSYVAGRKAK
DIINTARASL AKMIGGKPQD IIFTSGGTES NNLVIHSTVR CFHEQQTLQG RTVDQISPEE
GTRPHFITCT VEHDSIRLPL EHLVEDQVAE VTFVPVSKVN GQVEVEDILA AVRPTTCLVT
IMLANNETGV IMPISEISRR IKALNQIRAA SGLPRVLVHT DAAQALGKRR VDVEDLGVDF
LTIVGHKFYG PRIGALYVRG VGKLTPLYPM LFGGGQERNF RPGTENTPMI AGLGKAADLV
SENCETYEAH MRDIRDYLEE RLEAEFGKRI HLNSRFPGVE RLPNTCNFSI QGSQLRGYMV
LAQCQTLLAS VGASCHSDHE DRPSPVLLSC GIPVDVARNA VRLSVGRSTT RAEVDLIVQD
LKQAVNQLEG PV
