ID G3TA83_LOXAF Unreviewed; 431 AA.
AC G3TA83;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Selenocysteine lyase {ECO:0000256|ARBA:ARBA00040554};
DE EC=4.4.1.16 {ECO:0000256|ARBA:ARBA00039054};
GN Name=SCLY {ECO:0000313|Ensembl:ENSLAFP00000010749.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000010749.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000010749.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010749.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000010749.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010749.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine
CC and elemental selenium. {ECO:0000256|ARBA:ARBA00037407}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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DR AlphaFoldDB; G3TA83; -.
DR STRING; 9785.ENSLAFP00000010749; -.
DR Ensembl; ENSLAFT00000012854.3; ENSLAFP00000010749.3; ENSLAFG00000012853.3.
DR eggNOG; KOG1549; Eukaryota.
DR GeneTree; ENSGT00940000157773; -.
DR HOGENOM; CLU_003433_0_0_1; -.
DR InParanoid; G3TA83; -.
DR OMA; IIYGQSE; -.
DR TreeFam; TF313550; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR Gene3D; 1.10.260.50; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11601:SF62; SELENOCYSTEINE LYASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 20..415
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 431 AA; 46735 MW; 823882F3561DDEAB CRC64;
FSNSTSFSLT HLCFLSLRKV YMDYNATTPL EPEVIQAVTE AMWEAWGNPS SSYPAGRKAK
EIINAARESL AKMIGGKPSD IIFTSGGTES NNLVIHSVVQ HFHKNQAAKE DGVQPLGDEA
QPHFITCTVE HDSIRLPLEH LQAKGTAAVT FVPVSKVSGQ AEVDDVLAAV RPTTCLVTIM
LANNETGVIM RVPEISQRVK ALNSRRAASG LPRILVHTDA AQALGKRRVD VEDLDVDFLT
IVGHKFYGPR IGALYVRGLG EQTALHPMLF GGGQERNFRP GTENTPMIAG LGKAAELVSE
NCEAYEAHMR EVRDYLEERL QAEFGKKRIH LNSQFPGSER LANTCNVSIR GPQLQGRLVL
AQCRTLLASV GAACHSDLGD RPSPVLLSCG IPFEVARNAL RLSVGRGTTK AEVDLVVEDL
KQAVALLEGS A
//
