ID   ILVA_HAEIN              Reviewed;         513 AA.
AC   P46493;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
GN   Name=ilvA; OrderedLocusNames=HI_0738.1;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION.
RA   Koonin E.V., Rudd K.E.;
RL   Submitted (SEP-1995) to UniProtKB.
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; L42023; AAC22398.1; -; Genomic_DNA.
DR   RefSeq; NP_438898.1; NC_000907.1.
DR   AlphaFoldDB; P46493; -.
DR   SMR; P46493; -.
DR   STRING; 71421.HI_0738.1; -.
DR   EnsemblBacteria; AAC22398; AAC22398; HI_0738.1.
DR   KEGG; hin:HI_0738.1; -.
DR   PATRIC; fig|71421.8.peg.775; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_6_1_6; -.
DR   OrthoDB; 9811476at2; -.
DR   PhylomeDB; P46493; -.
DR   BioCyc; HINF71421:G1GJ1-777-MONOMER; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR   GO; GO:0006566; P:threonine metabolic process; ISS:UniProtKB.
DR   CDD; cd04906; ACT_ThrD-I_1; 1.
DR   CDD; cd04907; ACT_ThrD-I_2; 1.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
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; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01124; ilvA_2Cterm; 1.
DR   PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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_0000185574"
FT   DOMAIN          340..411
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          433..504
FT                   /note="ACT-like 2"
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         189..193
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
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   513 AA;  56663 MW;  DF42CA8B6FDE4CD7 CRC64;
     MKNLLTNPQP SQSDYINAIV KLGSRVYEAA QVTPLQKMGK LSERLHNNIW IKREDRQPVN
     SFKLRGAYAM ISSLSAEQKA AGVIAASAGN HAQGVALSAK QLGLKALIVM PQNTPSIKVD
     AVRGFGGEVL LHGANFDEAK AKAIELSKEK NMTFIPPFDH PLVIAGQGTL AMEMLQQVAD
     LDYVFVQVGG GGLAAGVAIL LKQFMPEIKI IGVESKDSAC LKAALDKGEP TDLTHIGLFA
     DGVAVKRIGD ETFRLCQQYL DDMVLVDSDE VCAAMKDLFE NVRAVAEPSG ALGLAGLKKY
     VKQNHIEGKN MAAILSGANL NFHTLRYVSE RCEIGENREA LLAVTMPEQP GSFLKFAYVL
     GNRAVTEFSY RYADDKRACV FVGVRTTNEQ EKADIIADLT KNGFDVEDMS DDDIAKTHVR
     YLMGGRAAND NERLYTFEFP EQKGALLKFL ETLQNRWNIS LFHYRAHGAD YGNILAGFQI
     EQREQAEFEQ GLAQLNYVFE DVTKSKSYRY FLR
//