ID D4JF88_9FIRM Unreviewed; 398 AA.
AC D4JF88;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=EC1_15080 {ECO:0000313|EMBL:CBK88860.1};
OS Faecalitalea cylindroides T2-87.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalitalea.
OX NCBI_TaxID=717960 {ECO:0000313|EMBL:CBK88860.1, ECO:0000313|Proteomes:UP000008801};
RN [1] {ECO:0000313|EMBL:CBK88860.1, ECO:0000313|Proteomes:UP000008801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2-87 {ECO:0000313|EMBL:CBK88860.1,
RC ECO:0000313|Proteomes:UP000008801};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium cylindroides T2-87.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK88860.1, ECO:0000313|Proteomes:UP000008801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2-87 {ECO:0000313|EMBL:CBK88860.1,
RC ECO:0000313|Proteomes:UP000008801};
RA Pajon A.;
RL Submitted (MAR-2010) 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|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 biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810}.
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; FP929041; CBK88860.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JF88; -.
DR STRING; 717960.EC1_15080; -.
DR KEGG; euc:EC1_15080; -.
DR PATRIC; fig|717960.3.peg.1000; -.
DR HOGENOM; CLU_021152_4_1_9; -.
DR UniPathway; UPA00047; UER00054.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000008801; 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR CDD; cd04886; ACT_ThrD-II-like; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR044561; ACT_ThrD-II-like.
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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Lyase {ECO:0000256|RuleBase:RU363083, ECO:0000313|EMBL:CBK88860.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363083};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU363083}.
FT DOMAIN 325..398
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 398 AA; 42813 MW; 417FB474080E4604 CRC64;
MLSLDKIYHA RFVLKDVARK TDLIYAPKID PESNVYLKTE NLQNTGSFKL RGAYYKISQL
SKEEKERGVI ACSAGNHAQG VALAATKNNI PSIICLPDGA PISKVEATKE YGAKVCLVPG
VYDDAYNKAI ELRDKEGYTF IHPFDDEDVI AGQGTIGLEI LDQLPDVEAV VVPVGGGGLI
SGIAYALKSL NPNIKVYGVQ AQGAASMVTS LKEDEIVKLE EVGTIADGIK VKEPGVNTFD
ICKKYVDDIV TVSDDEVASA ILALIEQHKL ITEGAGAVSV AAVMFNKVPV KGKNVVCLLS
GGNIDVTILS KVIERGLLKS GRSDTLMIQL EDKPGQLQGV SSTIAKYGAN VTGVFYEKAS
EGSNITDCVL RINVETRNFD HIHSLREGLK LEGFKIIE
//
