THDH_YEAST
ID THDH_YEAST Reviewed; 576 AA.
AC P00927; D3DLZ2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Threonine dehydratase, mitochondrial;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
DE Flags: Precursor;
GN Name=ILV1; OrderedLocusNames=YER086W;
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].
RA Kielland-Brandt M.C., Holmberg S., Petersen J.G.L., Nilsson-Tillgren T.;
RT "Nucleotide sequence of the gene for threonine deaminase (ILV1) of
RT Saccharomyces cerevisiae.";
RL Carlsberg Res. Commun. 49:567-575(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
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 [4]
RP ACTIVITY REGULATION.
RX PubMed=782558; DOI=10.1016/s0300-9084(76)80374-4;
RA Ahmed S.I., Bollon A.P., Rogers S.J., Magee P.T.;
RT "Purification and properties of threonine deaminase from Saccharomyces
RT cerevisiae.";
RL Biochimie 58:225-232(1976).
RN [5]
RP ENZYME ACTIVITY, AND INDUCTION.
RX PubMed=3289762; DOI=10.1007/bf00387766;
RA Holmberg S., Petersen J.G.;
RT "Regulation of isoleucine-valine biosynthesis in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 13:207-217(1988).
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
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 Evidence={ECO:0000269|PubMed:3289762};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Isoleucine allosterically inhibits while valine
CC allosterically activates this enzyme. {ECO:0000269|PubMed:782558}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- INDUCTION: In response to starvation for tryptophan and branched-chain
CC amino acid imbalance. {ECO:0000269|PubMed:3289762}.
CC -!- MISCELLANEOUS: Present with 11900 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; M36383; AAA34705.1; -; Genomic_DNA.
DR EMBL; X01466; CAA25696.1; -; Genomic_DNA.
DR EMBL; U18839; AAB64641.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07746.1; -; Genomic_DNA.
DR PIR; S50589; DWBYT.
DR RefSeq; NP_011009.1; NM_001178977.1.
DR AlphaFoldDB; P00927; -.
DR SMR; P00927; -.
DR BioGRID; 36830; 773.
DR DIP; DIP-4029N; -.
DR IntAct; P00927; 38.
DR MINT; P00927; -.
DR STRING; 4932.YER086W; -.
DR MaxQB; P00927; -.
DR PaxDb; P00927; -.
DR PRIDE; P00927; -.
DR EnsemblFungi; YER086W_mRNA; YER086W; YER086W.
DR GeneID; 856819; -.
DR KEGG; sce:YER086W; -.
DR SGD; S000000888; ILV1.
DR VEuPathDB; FungiDB:YER086W; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_6_0_1; -.
DR InParanoid; P00927; -.
DR OMA; VNFPQRA; -.
DR BioCyc; YEAST:YER086W-MON; -.
DR UniPathway; UPA00047; UER00054.
DR PRO; PR:P00927; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P00927; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IMP:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IMP:SGD.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IGI:SGD.
DR Gene3D; 3.40.1020.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR038110; TD_ACT-like_sf.
DR InterPro; IPR005787; Thr_deHydtase_biosynth.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Isoleucine biosynthesis; Lyase;
KW Mitochondrion; Pyridoxal phosphate; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..576
FT /note="Threonine dehydratase, mitochondrial"
FT /id="PRO_0000033616"
FT DOMAIN 393..473
FT /note="ACT-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT DOMAIN 495..566
FT /note="ACT-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 259
FT /note="I -> T (in Ref. 1; AAA34705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 63831 MW; 0801BCBD7EEDDC1F CRC64;
MSATLLKQPL CTVVRQGKQS KVSGLNLLRL KAHLHRQHLS PSLIKLHSEL KLDELQTDNT
PDYVRLVLRS SVYDVINESP ISQGVGLSSR LNTNVILKRE DLLPVFSFKL RGAYNMIAKL
DDSQRNQGVI ACSAGNHAQG VAFAAKHLKI PATIVMPVCT PSIKYQNVSR LGSQVVLYGN
DFDEAKAECA KLAEERGLTN IPPFDHPYVI AGQGTVAMEI LRQVRTANKI GAVFVPVGGG
GLIAGIGAYL KRVAPHIKII GVETYDAATL HNSLQRNQRT PLPVVGTFAD GTSVRMIGEE
TFRVAQQVVD EVVLVNTDEI CAAVKDIFED TRSIVEPSGA LSVAGMKKYI STVHPEIDHT
KNTYVPILSG ANMNFDRLRF VSERAVLGEG KEVFMLVTLP DVPGAFKKMQ KIIHPRSVTE
FSYRYNEHRH ESSSEVPKAY IYTSFSVVDR EKEIKQVMQQ LNALGFEAVD ISDNELAKSH
GRYLVGGASK VPNERIISFE FPERPGALTR FLGGLSDSWN LTLFHYRNHG ADIGKVLAGI
SVPPRENLTF QKFLEDLGYT YHDETDNTVY QKFLKY
