ID D6XUF2_BACIE Unreviewed; 422 AA.
AC D6XUF2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=L-threonine dehydratase {ECO:0000256|RuleBase:RU362012};
DE EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012};
DE AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012};
GN Name=ilvA {ECO:0000256|RuleBase:RU362012};
GN OrderedLocusNames=Bsel_1934 {ECO:0000313|EMBL:ADH99438.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99438.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH99438.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) 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.
CC {ECO:0000256|ARBA:ARBA00025527, ECO:0000256|RuleBase:RU362012}.
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 Evidence={ECO:0000256|ARBA:ARBA00001274,
CC ECO:0000256|RuleBase:RU362012};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362012};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810, ECO:0000256|RuleBase:RU362012}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|RuleBase:RU362012}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
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DR EMBL; CP001791; ADH99438.1; -; Genomic_DNA.
DR AlphaFoldDB; D6XUF2; -.
DR STRING; 439292.Bsel_1934; -.
DR KEGG; bse:Bsel_1934; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_9; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR011820; IlvA.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR02079; THD1; 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; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51672; ACT_LIKE; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU362012};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW ECO:0000256|RuleBase:RU362012}; Lyase {ECO:0000256|RuleBase:RU362012};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362012}.
FT DOMAIN 339..413
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 422 AA; 46982 MW; 7AE22EDDE3D18D2F CRC64;
MTMSKTLTDA LPVRDILIAH QNLKDVVVNT PLQRDPILSE KYEANIYLKR EDLQVVRSFK
LRGAYHFMMS LSDQELQQGV VCASAGNHAQ GVAYACKALG VRGKIFMPTT TPRQKVSRVE
FFGEPYVEVI LHGDTFDDAF EAAMKVCNEH EMTFIHPFDD LRTIAGQGTV GMEILEGMDE
PVSHVFMSVG GGGLISGVGS YIKNISPDTK VVGVEPSGAP SMKTSFEAGS VQKLEEINKF
VDGASVKSVG EITFQIAQRV VDDIVLVDEG EVCSTILSLY NEQAIVAEPA GALAVSALEH
RRHEIKGKTV VCIVSGGNND IDRMQEIKER SLIYDGYKHY FIVDFPQRAG ALRQFLTNVL
GENDDITRFE YTKKNDRDKG PVLVGIELKY KEDYHPLVHR MEKHGFSYIE INKDQKLFNL
LI
//
