STDH_YEAST
ID STDH_YEAST Reviewed; 360 AA.
AC P25379; D6VQV4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Catabolic L-serine/threonine dehydratase;
DE Includes:
DE RecName: Full=L-serine dehydratase;
DE EC=4.3.1.17;
DE AltName: Full=L-serine deaminase;
DE Includes:
DE RecName: Full=L-threonine dehydratase;
DE EC=4.3.1.19;
DE AltName: Full=L-threonine deaminase;
GN Name=CHA1; OrderedLocusNames=YCL064C; ORFNames=YCL64C;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1628804; DOI=10.1093/genetics/131.3.531;
RA Bornaes C., Petersen J.G., Holmberg S.;
RT "Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1
RT polypeptide is homologous with other serine and threonine dehydratases.";
RL Genetics 131:531-539(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 268; 317 AND 318.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- INTERACTION:
CC P25379; P38622: RCK1; NbExp=2; IntAct=EBI-3804607, EBI-14880;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 36600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; M85194; AAA35040.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42403.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07423.1; -; Genomic_DNA.
DR PIR; S19395; DWBYLH.
DR RefSeq; NP_001018030.1; NM_001178706.1.
DR AlphaFoldDB; P25379; -.
DR SMR; P25379; -.
DR BioGRID; 30924; 70.
DR DIP; DIP-7970N; -.
DR IntAct; P25379; 31.
DR MINT; P25379; -.
DR STRING; 4932.YCL064C; -.
DR iPTMnet; P25379; -.
DR MaxQB; P25379; -.
DR PaxDb; P25379; -.
DR PRIDE; P25379; -.
DR EnsemblFungi; YCL064C_mRNA; YCL064C; YCL064C.
DR GeneID; 850295; -.
DR KEGG; sce:YCL064C; -.
DR SGD; S000000569; CHA1.
DR VEuPathDB; FungiDB:YCL064C; -.
DR eggNOG; KOG1250; Eukaryota.
DR GeneTree; ENSGT00940000174246; -.
DR HOGENOM; CLU_021152_3_1_1; -.
DR InParanoid; P25379; -.
DR OMA; PKPWVET; -.
DR BioCyc; YEAST:YCL064C-MON; -.
DR Reactome; R-SCE-8849175; Threonine catabolism.
DR PRO; PR:P25379; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25379; protein.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:SGD.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IGI:SGD.
DR GO; GO:0006567; P:threonine catabolic process; IGI:SGD.
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 1: Evidence at protein level;
KW Acetylation; Lyase; Mitochondrion; Pyridoxal phosphate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..360
FT /note="Catabolic L-serine/threonine dehydratase"
FT /id="PRO_0000185598"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 37
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="G -> A (in Ref. 1; AAA35040)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="T -> P (in Ref. 1; AAA35040)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="GG -> AS (in Ref. 1; AAA35040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39301 MW; FC905FF3D111187D CRC64;
MSIVYNKTPL LRQFFPGKAS AQFFLKYECL QPSGSFKSRG IGNLIMKSAI RIQKDGKRSP
QVFASSGGNA GFAAATACQR LSLPCTVVVP TATKKRMVDK IRNTGAQVIV SGAYWKEADT
FLKTNVMNKI DSQVIEPIYV HPFDNPDIWE GHSSMIDEIV QDLKSQHISV NKVKGIVCSV
GGGGLYNGII QGLERYGLAD RIPIVGVETN GCHVFNTSLK IGQPVQFKKI TSIATSLGTA
VISNQTFEYA RKYNTRSVVI EDKDVIETCL KYTHQFNMVI EPACGAALHL GYNTKILENA
LGSKLAADDI VIIIACGGSS NTIKDLEEAL DSMRKKDTPV IEVADNFIFP EKNIVNLKSA
