ILVA_LACLA
ID ILVA_LACLA Reviewed; 416 AA.
AC Q02145; O34132; Q9CG81;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
GN Name=ilvA; OrderedLocusNames=LL1227; ORFNames=L0081;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400210; DOI=10.1128/jb.174.20.6580-6589.1992;
RA Godon J.-J., Chopin M.-C., Ehrlich S.D.;
RT "Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp.
RT lactis.";
RL J. Bacteriol. 174:6580-6589(1992).
RN [2]
RP SEQUENCE REVISION.
RA Delorme C., Goupil-Feuillerat N., Godon J.-J., Ehrlich S.D., Renault P.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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; U92974; AAB81922.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05325.1; -; Genomic_DNA.
DR PIR; C86778; C86778.
DR PIR; S35141; S35141.
DR RefSeq; NP_267383.1; NC_002662.1.
DR RefSeq; WP_010905840.1; NC_002662.1.
DR AlphaFoldDB; Q02145; -.
DR SMR; Q02145; -.
DR STRING; 272623.L0081; -.
DR PaxDb; Q02145; -.
DR EnsemblBacteria; AAK05325; AAK05325; L0081.
DR KEGG; lla:L0081; -.
DR PATRIC; fig|272623.7.peg.1326; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_9; -.
DR OMA; VNFPQRA; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000002196; 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; 3.40.50.1100; -; 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; 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..416
FT /note="L-threonine dehydratase biosynthetic IlvA"
FT /id="PRO_0000185575"
FT DOMAIN 333..407
FT /note="ACT-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT BINDING 78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 184..188
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 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 345
FT /note="A -> S (in Ref. 1; AAB81922)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="D -> N (in Ref. 1; AAB81922)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="H -> R (in Ref. 1; AAB81922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 45577 MW; AFDAC61464D7E977 CRC64;
MISAKEVEDA YDLLKAVVTK TPLQLDPYLS NKYQANIYLK EENLQKVRSF KLRGAYYSIS
KLSDEQRSKG VVCASAGNHA QGVAFAANQL NISATIFMPV TTPNQKISQV KFFGESHVTI
RLIGDTFDES ARAAKAFSQD NDKPFIDPFD DENVIAGQGT VALEIFAQAK KQGISLDKIF
VQIGGGGLIA GITAYSKERY PQTEIIGVEA KGATSMKAAY SAGQPVTLEH IDKFADGIAV
ATVGQKTYQL INDKVKQLLA VDEGLISQTI LELYSKLGIV AEPAGATSVA ALELIKDEIK
GKNIVCIISG GNNDISRMQE IEERALVYEG LKHYFVINFP QRPGALRTFV SDILGPNDDI
TRFEYIKRAD KGKGPCLVGI LLSDASDYDS LIDRIERFDN RYVNLHGNDS LYELLV
