ID SDHL_YEAS6 Reviewed; 338 AA. AC B5VKE8; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 15-FEB-2017, entry version 23. DE RecName: Full=L-serine dehydratase; DE EC=4.3.1.17; DE AltName: Full=L-serine deaminase; GN Name=SDL1; Synonyms=SDH1; ORFNames=AWRI1631_90030; OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=545124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI1631; RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x; RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.; RT "Comparative genome analysis of a Saccharomyces cerevisiae wine RT strain."; RL FEMS Yeast Res. 8:1185-1195(2008). CC -!- CATALYTIC ACTIVITY: L-serine = pyruvate + NH(3). 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 --------------------------------------------------------------------------- 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; ABSV01001169; EDZ71597.1; -; Genomic_DNA. DR SMR; B5VKE8; -. DR TopDownProteomics; B5VKE8; -. DR OrthoDB; EOG092D2PSJ; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000008988; Unassembled WGS sequence. 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:cellular amino acid metabolic process; IEA:InterPro. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Lyase; KW Pyridoxal phosphate. FT CHAIN 1 338 L-serine dehydratase. FT /FTId=PRO_0000393396. FT MOD_RES 39 39 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 338 AA; 36862 MW; 199DA2F645421F7D CRC64; MEMTHYEKTP LIRQVFNNGK TNSWFYVKHE ILQPGGSFKS RGIGHLIRKN NEEALSEGSG KLAVFSSSGG NAGLAAATAC RSMALNCSVV VPKTTKPRMV KKIQSAGAKV IIHGDHWGEA DEYLRHELMA QESQHGSKTL YVHPFDNETI WEGHSTIVDE IIEQLKENDI SLPRVKALVC SVGGGGLFSG IIKGLERNHL AEKIPVVAVE TAGCDVLNKS LKKGSPVTLE KLTSVATSLG SPYIASFAFE SFNKYGCKSV VLSDQDVLAT CLRYADDYNF IVEPACGASL HLCYHPEILE DILEQKIYED DIVIIIACGG SCMTYEDFVK ASSTLNVS //