ID R5KNH6_9CLOT Unreviewed; 399 AA.
AC R5KNH6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000256|RuleBase:RU363083};
DE EC=4.3.1.19 {ECO:0000256|RuleBase:RU363083};
DE AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU363083};
GN ORFNames=BN753_00323 {ECO:0000313|EMBL:CCY66614.1};
OS Clostridium sp. CAG:678.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262831 {ECO:0000313|EMBL:CCY66614.1, ECO:0000313|Proteomes:UP000017959};
RN [1] {ECO:0000313|EMBL:CCY66614.1, ECO:0000313|Proteomes:UP000017959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:678 {ECO:0000313|Proteomes:UP000017959};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 degradation; L-threonine degradation via propanoate
CC pathway; propanoate from L-threonine: step 1/4.
CC {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|RuleBase:RU363083}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|RuleBase:RU363083}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCY66614.1}.
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DR EMBL; CAYP010000015; CCY66614.1; -; Genomic_DNA.
DR AlphaFoldDB; R5KNH6; -.
DR STRING; 1262831.BN753_00323; -.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000017959; Unassembled WGS sequence.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
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; 3.30.70.260; -; 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; 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; PF13291; ACT_4; 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.
PE 3: Inferred from homology;
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};
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:UP000017959}.
FT DOMAIN 326..399
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 399 AA; 42570 MW; F22734A3C6E5FF32 CRC64;
MLTLDRVYTA ARVLKEIIRE TDMIYAPNIS KNAQIYLKTE NLQVTGSFKI RGSYFKISQL
SDEEKKHGVI ACSAGNHAQG VALAATRSGI KSIICLPDGA PISKVEATKR FGAQVCMVKG
VYDDAYNKAI ELRDEKGYTF IHPFDDEDVI AGQGTIGLEI MEQLPNADAV IVPIGGGGLI
SGVAYTIKQI NPKCKVYGVQ AQGAPSMQKS VSDGKIETLP KVQTIADGIA VKTPGDITYD
MVSQYVDGIY TVSDDEIALA ILTLLEQQKL ISEGAGAVPV AAVLAGKIPD IEGKNVCCLV
SGGNIDVTIL SRVIERGLKM SGRTANITIA LSDKPGQLAD VSKIISQTGA NVTSVNYDST
DLDMNITDCY LRIGVETRDY AHVVAIKAAL KDAGFEVCD
//
