ID A0A060WGC6_ONCMY Unreviewed; 327 AA.
AC A0A060WGC6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=L-serine ammonia-lyase {ECO:0000256|ARBA:ARBA00012093};
DE EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
DE AltName: Full=L-serine deaminase {ECO:0000256|ARBA:ARBA00041766};
DE AltName: Full=L-threonine dehydratase {ECO:0000256|ARBA:ARBA00042605};
GN ORFNames=GSONMT00074893001 {ECO:0000313|EMBL:CDQ66197.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ66197.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ66197.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ66197.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSOMYP00000002436.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00001161};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; FR904534; CDQ66197.1; -; Genomic_DNA.
DR STRING; 8022.A0A060WGC6; -.
DR PaxDb; 8022-A0A060WGC6; -.
DR Ensembl; ENSOMYT00000002724.2; ENSOMYP00000002436.1; ENSOMYG00000001289.2.
DR GeneTree; ENSGT00940000160172; -.
DR OrthoDB; 8406at2759; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR Proteomes; UP000694395; Chromosome 6.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06448; L-Ser-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR48078:SF8; L-SERINE DEHYDRATASE_L-THREONINE DEAMINASE; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000193380}.
FT DOMAIN 12..306
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 327 AA; 34912 MW; 28DAC5F0F50D8181 CRC64;
MKNPQERALH VATPLRESLA LTKVAGTSVY LKLDSSQPTG SFKIRGIGHL CKTWAKRGCE
RFVCCSGGNA GMAAAYSARK LGVPATIIVP SVTPKPTVER LRDEGANVVI HGKALNESIE
YGQQLVANNP GWIFISPFDD PLIWEGHMSL VKELESELQE KPGAMVLSVG GGGLMNGVVE
GLRRAGWNDV PVIAMETVGA HSLNAAMKAG KLITLTEITS IATTLGLTRV SAQTLKLAGE
HTVYSELVTD QEAVKAVERF VDDEKVLVEP ACGAALAAVY CDIIPRLQKE GKLARDLGPV
VIVVCGGNNI SMKQLQKLKK QLGMSFS
//