ID   ILVA_PASMU              Reviewed;         513 AA.
AC   Q9CKJ2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=PM1624;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; AE004439; AAK03708.1; -; Genomic_DNA.
DR   RefSeq; WP_005718461.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKJ2; -.
DR   SMR; Q9CKJ2; -.
DR   STRING; 747.DR93_475; -.
DR   EnsemblBacteria; AAK03708; AAK03708; PM1624.
DR   KEGG; pmu:PM1624; -.
DR   HOGENOM; CLU_021152_6_2_6; -.
DR   OMA; VNFPQRA; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000000809; 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; 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; 2.
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; Pyridoxal phosphate; Reference proteome;
KW   Repeat.
FT   CHAIN           1..513
FT                   /note="L-threonine dehydratase biosynthetic IlvA"
FT                   /id="PRO_0000185579"
FT   DOMAIN          338..409
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          432..504
FT                   /note="ACT-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   BINDING         88
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..191
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  56288 MW;  3E427ADC54E5FC7C CRC64;
     MVNNLHSAHP TGAEYLKAVL SSKVYDVAQV TPLQDMAKLS ERLGNKVFIK REDRQPVHSF
     KLRGAYAMIA GLSAEQKASG VIAASAGNHA QGVALSAKHL GLRALIVMPQ NTPSIKVDAV
     RGFGGEVLLH GANFDEAKAK AIELAESKNM TFIPPFDHPA VIAGQGSIAM ELLQQNSQID
     RIFVPVGGGG LAAGIAVLIK QLMPEIKVIG VESKDSACLY RALKAGKPID LDRVGLFADG
     VAVKRIGDET FRVCQQYIDD VVLVDGDEIC AAVKDIFENV RAIAEPSGAL SLAGLKKYVK
     EHNIQGETLV NVLSGANLNF HTLRYVSERC EIGEQHEALL AVTIPEQPGS FLKFCHILGH
     VPVTEFKYRY ADDKQACIFV GVRITGQEEK QTIINQLQQN GYDLIDLSND DIAKTHVRYM
     IGGRSNSPLK ERLYSFEFPE QKGALLKFLE TLGQTHWNIS VFHYRAHGAD YGNVLAGFQL
     NDEDLDAFNQ HLEKLGYVYQ DVTESPAYRY FLV