ID   THDH_BLAAD              Reviewed;         550 AA.
AC   O42615;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Threonine dehydratase, mitochondrial;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
DE   Flags: Precursor;
GN   Name=ILV1;
OS   Blastobotrys adeninivorans (Yeast) (Arxula adeninivorans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Blastobotrys.
OX   NCBI_TaxID=409370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LS3;
RX   PubMed=9730281;
RX   DOI=10.1002/(sici)1097-0061(199808)14:11<1017::aid-yea314>3.0.co;2-0;
RA   Wartmann T., Roesel H., Kunze I., Bode R., Kunze G.;
RT   "AILV1 gene from the yeast Arxula adeninivorans LS3 -- a new selective
RT   transformation marker.";
RL   Yeast 14:1017-1025(1998).
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   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ222772; CAA10977.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42615; -.
DR   SMR; O42615; -.
DR   UniPathway; UPA00047; UER00054.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Lyase; Mitochondrion; Pyridoxal phosphate; Repeat;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..550
FT                   /note="Threonine dehydratase, mitochondrial"
FT                   /id="PRO_0000033615"
FT   DOMAIN          368..446
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          468..539
FT                   /note="ACT-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  60417 MW;  D08CE5BD55CC8A6F CRC64;
     MSNISTPRIS GLTEYTSQPD KSHYDSIESH FLLPDGTPDY LKLILTSKVY DVCNETPVTP
     AVNLSSKLGA NIFLKREDLQ PVFSFKLRGA YNMMAHLPQE TRWKGVIACS AGNHAQGVAY
     SAKHLNIPAT IVMPVVTPAI KYKNVDRLGA KVVLHGNDFD AAKAECNRLS EKHGLTNIPL
     FDNPYVIAGQ GTIGVELLRQ IDVESLKAIF VCIGGGGLIA GVGAYIKRIA PQVKIIGVET
     YDANAMRQSL QKGERITLSE VGLFADGAAV KILGEETFRL CQQVVDEIVL VSTDEICAAI
     KDVFTETRSI VEPAGALSVA GLVKYVESHP EIDHSASGYT AILSGANMDF DRLRFVSERA
     KLGEGSEVFI VATIPEKPGS FGKLIDLVHP RAVTEFSYRY SNGELEKSDG KAHVYISFSV
     DNAKAEVPRI LDDFKGAGFD AIDISHNEFP KSHPRYLVGA NQPVTNERVF RFEFPERPGA
     LVKFLHGVKS KWNITLFHYR NQGSDIAKVL AGISVPSHES DQFQQFLDNL EYPYAEETDN
     VVYKLFSQGD