ID R5DW74_9FIRM Unreviewed; 397 AA.
AC R5DW74;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BN462_00927 {ECO:0000313|EMBL:CCX83164.1};
OS Ruminococcus sp. CAG:108.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262950 {ECO:0000313|EMBL:CCX83164.1, ECO:0000313|Proteomes:UP000018037};
RN [1] {ECO:0000313|EMBL:CCX83164.1, ECO:0000313|Proteomes:UP000018037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:108 {ECO:0000313|Proteomes:UP000018037};
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:CCX83164.1}.
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DR EMBL; CAXD010000069; CCX83164.1; -; Genomic_DNA.
DR AlphaFoldDB; R5DW74; -.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000018037; 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; 3.40.50.1100; -; 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; PF01842; ACT; 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, ECO:0000313|EMBL:CCX83164.1};
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:UP000018037}.
FT DOMAIN 325..397
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 397 AA; 42587 MW; E1894DEE49F03D8C CRC64;
MLTLDKIYHA SYVLKDVIRQ TNIVQARGIC DDCDVYLKPE NLQITGSFKV RGSGYKISQL
TEEEKARGVI ACSAGNHAQG VALAATKYGI KSLICLPDGA PISKVEATKN YGAEVCMVPG
VYDDAYNEAL RLRDEKNYTF IHPFDDENVI AGQGTIGIEI MNEMPDVDAV VCAIGGGGLI
SGVACAIKSL NPNIKVYGVQ AEGAPSMVES IKNGEPVHLD SVSTIADGIQ VKEPGEHTFE
YVKKYVDDIV TVSDDEISSA ILKLIESQKM IAEGAGAAPL AAVMFNKLPV KGKKVVCVVS
GGNIDVTILS RVIKRGLLMT GRQQTFCVEL QDKPGQLVAV SNIIAEKGAN VISIHHERGG
EGTDVNGCYL RVVLETRDFA QIKEIRDALV DAGFKLV
//
