ID A0A0U4FY50_9BACI Unreviewed; 302 AA.
AC A0A0U4FY50;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000256|ARBA:ARBA00022248, ECO:0000256|RuleBase:RU363083};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096, ECO:0000256|RuleBase:RU363083};
DE AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU363083};
GN ORFNames=AOX59_17630 {ECO:0000313|EMBL:ALX50693.1};
OS Lentibacillus amyloliquefaciens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX50693.1, ECO:0000313|Proteomes:UP000050331};
RN [1] {ECO:0000313|EMBL:ALX50693.1, ECO:0000313|Proteomes:UP000050331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX50693.1,
RC ECO:0000313|Proteomes:UP000050331};
RA Wang J.-L., He M.-X.;
RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT LAM0015T isolated from saline sediment.";
RL Submitted (JAN-2016) 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:RU363083}.
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|RuleBase:RU363083};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU363083};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway; propanoate from L-threonine: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004958, ECO:0000256|RuleBase:RU363083}.
CC -!- SUBUNIT: In the native structure, TdcB is in a dimeric form, whereas in
CC the TdcB-AMP complex, it exists in a tetrameric form (dimer of dimers).
CC {ECO:0000256|ARBA:ARBA00011447, ECO:0000256|RuleBase:RU363083}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|RuleBase:RU363083}.
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DR EMBL; CP013862; ALX50693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4FY50; -.
DR STRING; 1472767.AOX59_17630; -.
DR KEGG; lao:AOX59_17630; -.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000050331; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01127; ilvA_1Cterm; 1.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Lyase {ECO:0000256|RuleBase:RU363083};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363083};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU363083};
KW Reference proteome {ECO:0000313|Proteomes:UP000050331}.
FT DOMAIN 7..280
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 302 AA; 32289 MW; 47B55F5CFF77094F CRC64;
MRSTTTDALV GKQVYFKMEN QQKTGSFKFR GATFKLMQLS DEQLQKGVIA ASAGNHAQGV
ANAARKLNAQ ATIFMPEKTP AAKVNATRAY GAEVVLTGQS FQEAYDASMK RQLQTGAEYI
HPFDDYDVMA GQGTAAAEML QQEDRIDTIL VPVGGGGLIS GTAAAAKHID KNIKVIGVQS
AGASALYQSF YHNRVKQLEQ VSTIAEGIAV KKPGDRTLPL INEYVDDIVT VSDEEIASAI
VYMLERNKTL LEGAGAAALA ALLSRGSQLK SDHCGIIVSG GNMDISTLPM IQRLSNKLHH
SA
//
