位置:首页 > 蛋白库 > YI168_YEAST
YI168_YEAST
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   03-AUG-2022, entry version 52.
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   PRIDE; P0CF21; -.
DR   SGD; S000001430; YIL168W.
DR   VEuPathDB; FungiDB:YIL167W; -.
DR   InParanoid; P0CF21; -.
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:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024