TDCB_STAAW
ID TDCB_STAAW Reviewed; 346 AA.
AC Q8NWQ4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=L-threonine dehydratase catabolic TdcB;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
GN Name=tdcB; OrderedLocusNames=MW1327;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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 -!- ACTIVITY REGULATION: Each protein molecule can bind up to four
CC molecules of AMP, which act as an allosteric activator to the enzyme.
CC {ECO:0000250}.
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway; propanoate from L-threonine: step 1/4.
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:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; BA000033; BAB95192.1; -; Genomic_DNA.
DR RefSeq; WP_000210828.1; NC_003923.1.
DR AlphaFoldDB; Q8NWQ4; -.
DR SMR; Q8NWQ4; -.
DR EnsemblBacteria; BAB95192; BAB95192; BAB95192.
DR KEGG; sam:MW1327; -.
DR HOGENOM; CLU_021152_4_2_9; -.
DR OMA; LIHPFDH; -.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000000418; 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 Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01127; ilvA_1Cterm; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Lyase; Nucleotide-binding; Pyridoxal phosphate.
FT CHAIN 1..346
FT /note="L-threonine dehydratase catabolic TdcB"
FT /id="PRO_0000287331"
FT BINDING 59..60
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 125..126
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37306 MW; A69CB839024C9C5F CRC64;
MTTNTVTLQT AHIVSLGDIE EAKASIKPFI RRTPLIKSMY LSQSITKGNV FLKLENMQFT
GSFKFRGASN KINHLTDEQK EKGIIAASAG NHAQGVALTA KLLGIDATIV MPETAPQAKQ
QATKGYGAKV ILKGKNFNET RLYMEELAKE NGMTIVHPYD DKFVMAGQGT IGLEILDDIW
NVNTVIVPVG GGGLIAGIAT ALKSFNPSIH IIGVQSENVH GMAESFYKRD LTEHRVDSTI
ADGCDVKVPG EQTYEVVKHL VDEFILVTEE EIEHAMKDLM QRAKIITEGA GALPTAAILS
GKINNKWLED KNVVALVSGG NVDLTRVSGV IEHGLNIADT SKGVVG