ID YI168_YEAST Reviewed; 127 AA. AC P0CF21; P17324; P40443; P40444; Q6Q579; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 57. DE RecName: Full=Putative truncated L-serine dehydratase YIL168W; DE EC=4.3.1.17; GN OrderedLocusNames=YIL168W; ORFNames=YI9402.08A; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). 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 -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. CC {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene unlikely to encode a CC functional protein. This is a truncated version of L-serine CC dehydratase. Strain S288c has a stop codon in position 128, which CC disrupts the gene coding for this protein and produces two ORFs YIL167W CC and YIL168W. Because of that it is not part of the S.cerevisiae S288c CC complete/reference proteome set. A contiguous sequence for L-serine CC dehydratase can be found in other strain backgrounds (AC P0CF23). CC {ECO:0000305|PubMed:24374639}. 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; Z46921; CAA87024.1; -; Genomic_DNA. DR EMBL; AY558344; AAS56670.1; -; Genomic_DNA. DR PIR; S12731; S12731. DR AlphaFoldDB; P0CF21; -. DR SMR; P0CF21; -. DR SGD; S000001430; YIL168W. DR UniPathway; UPA00138; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. 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:SF2; CATABOLIC L-SERINE_THREONINE DEHYDRATASE; 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 5: Uncertain; KW Cytoplasm; Gluconeogenesis; Lyase; Pyridoxal phosphate. FT CHAIN 1..127 FT /note="Putative truncated L-serine dehydratase YIL168W" FT /id="PRO_0000393393" FT MOD_RES 39 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" SQ SEQUENCE 127 AA; 13943 MW; 3943C545FFE8B54C CRC64; MEMTYYEKTP LIRQFLNNGK TNSWFYVKHE MLQPGGSFKS RGIGHLIRKS NEEALSEGSG KLAVFSSSGG NAGLAAATAC RSMALNCSVV VPKTTKPRMV KKIQSAGAKV IIHGDHWGEA DEYLRHE //