ID   ILVA_ALKHC              Reviewed;         415 AA.
AC   Q9KC63;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=BH1711;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05430.1; -; Genomic_DNA.
DR   PIR; G83863; G83863.
DR   RefSeq; WP_010897872.1; NC_002570.2.
DR   AlphaFoldDB; Q9KC63; -.
DR   SMR; Q9KC63; -.
DR   STRING; 272558.10174328; -.
DR   EnsemblBacteria; BAB05430; BAB05430; BAB05430.
DR   KEGG; bha:BH1711; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_2_9; -.
DR   OMA; VNFPQRA; -.
DR   OrthoDB; 1876944at2; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001258; 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; IPR045865; ACT-like_dom_sf.
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   SUPFAM; SSF55021; SSF55021; 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..415
FT                   /note="L-threonine dehydratase biosynthetic IlvA"
FT                   /id="PRO_0000185569"
FT   DOMAIN          332..406
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   BINDING         80
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         183..187
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   415 AA;  46470 MW;  BF49D28E65C7CFA2 CRC64;
     MGKIQIEDII IANQTLKDVV VHTPLQKNQV LSERYECNVY LKREDMQVVR SFKIRGAFHQ
     ISSIPKEELN NGVVCASAGN HAQGVAYSCH TLQIPGKIFM PTTTPRQKVD QVKFFGKEYV
     EVILTGDTFD DSFNEAKEYG IKHKMTFIHP FDQEKIVAGQ GTVGMEIMND IDDNIDYLFC
     SIGGGGLISG VGTYIKSISP RTKVIGCEPA GAPAMKESLK QGKVIELEKI DKFVDGAAVK
     KVGEIPFEIC QKILEDIVLV PEGKICTTIL NLYNQDAIVA EPAGAMPIAA LDFFKDEIKG
     KTVVCVLSGG NNDIGRMQEM RERSLIYEGL QHYFIIQFPQ RAGALKEFIL DVLGPDDDIT
     RFEYTKKNNK SNGPVLIGIE LKCDEDYHRL MDRLNKKGFE YREINKNESL FNLLI