ILVA_BURM1
ID ILVA_BURM1 Reviewed; 507 AA.
AC P53607; A9AFB5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, 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=Bmul_0562, BMULJ_02699;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bartell J.B., Lessie T.G.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; U40630; AAA83215.1; -; Genomic_DNA.
DR EMBL; CP000868; ABX14257.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG44589.1; -; Genomic_DNA.
DR RefSeq; WP_006398295.1; NC_010804.1.
DR AlphaFoldDB; P53607; -.
DR SMR; P53607; -.
DR STRING; 395019.Bmul_0562; -.
DR EnsemblBacteria; BAG44589; BAG44589; BMULJ_02699.
DR GeneID; 66527640; -.
DR KEGG; bmj:BMULJ_02699; -.
DR KEGG; bmu:Bmul_0562; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_6_2_4; -.
DR OMA; KHICDSH; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000008815; Chromosome 1.
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; 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; Pyridoxal phosphate; Reference proteome;
KW Repeat.
FT CHAIN 1..507
FT /note="L-threonine dehydratase biosynthetic IlvA"
FT /id="PRO_0000185571"
FT DOMAIN 333..404
FT /note="ACT-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT DOMAIN 427..498
FT /note="ACT-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT BINDING 79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 182..186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 55327 MW; E9A5D110B0597664 CRC64;
MASHDYLKKI LTARVYDVAF ETELEPARNL SARLRNPVYL KREDNQPVFS FKLRGAYNKM
AHIPADALAR GVITASAGNH AQGVAFSAAR MGVKAVIVVP VTTPQVKVDA VRAHGGPGVE
VIQAGESYSD AYAHALKVQE ERGLTFVHPF DDPYVIAGQG TIAMEILRQH QGPIHAIFVP
IGGGGLAAGV AAYVKAVRPE IKVIGVQAED SCAMAQSLQA GKRVELAEVG LFADGTAVKL
VGEETFRLCK EYLDGVVTVD TDALCAAIKD VFQDTRSVLE PSGALAVAGA KLYAEREGIE
NQTLVAVTSG ANMNFDRMRF VAERAEVGEA REAVFAVTIP EERGSFKRFC SLVGDRNVTE
FNYRIADAQS AHIFVGVQIR RRGESADIAA NFESHGFKTA DLTHDELSKE HIRYMVGGRS
PLALDERLFR FEFPERPGAL MKFLSSMAPD WNISLFHYRN QGADYSSILV GLQVPQADHA
EFERFLAALG YPYVEESANP AYRLFLS
