ID   ILVA_MYCLE              Reviewed;         427 AA.
AC   Q9X7F1;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=ML1209;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC       ammonia from threonine in a two-step reaction. The first step involved
CC       a dehydration of threonine and a production of enamine intermediates
CC       (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC       Both intermediates are unstable and short-lived. The second step is the
CC       nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC       ketobutyrate and free ammonia. In the low water environment of the
CC       cell, the second step is accelerated by RidA (By similarity).
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; AL049478; CAB39589.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31590.1; -; Genomic_DNA.
DR   PIR; C87060; C87060.
DR   RefSeq; NP_301876.1; NC_002677.1.
DR   RefSeq; WP_010908197.1; NC_002677.1.
DR   AlphaFoldDB; Q9X7F1; -.
DR   SMR; Q9X7F1; -.
DR   STRING; 272631.ML1209; -.
DR   EnsemblBacteria; CAC31590; CAC31590; CAC31590.
DR   KEGG; mle:ML1209; -.
DR   PATRIC; fig|272631.5.peg.2219; -.
DR   Leproma; ML1209; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_2_11; -.
DR   OMA; VNFPQRA; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000000806; Chromosome.
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   GO; GO:0006566; P:threonine metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.1020.10; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR011820; IlvA.
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; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR02079; THD1; 1.
DR   PROSITE; PS51672; ACT_LIKE; 1.
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; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..427
FT                   /note="L-threonine dehydratase biosynthetic IlvA"
FT                   /id="PRO_0000185576"
FT   DOMAIN          343..417
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   BINDING         90
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..197
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  45172 MW;  86FB44221369682E CRC64;
     MSAEPSRNPR TPPVSAVDID GAAKRIAPVV TPTPLQLSDR LSAITGAAVY LKREDLQTVR
     SYKLRGAYNL LVQLTDEEIA AGVVCSSAGN HAQGVAYACR SLGVHGRVYV PAKTPKQKWD
     RIRYHGGAFI ELIVGRSTYD LAAAAAVDDI ERTGATLVPP YDDVRVIAGQ GTIAVELLEQ
     LNTEPDLVVV PVGGGGCIAG MTTYLAERTA NTAVLGVEPA GAAAMMAALA AGEPVTLDYV
     DQFVDGAAVN RVGTLPYAAL TAAGDMVSIT TVDEGAVCTA MLDLYQNEGI IAEPAGALSV
     AGLLETDIEP GSTVVCLISG GNNDVLRYGE VLERSLIHLG LKHYFLVDFP QKPGALRRFL
     DEVLGPNDDI TLFEYVKRNN RETGEALVGI QLGSAVDLDV LLARMQGTEM HVETLQPGSP
     AYRYLLL