ID A0A1H3QFU7_9FIRM Unreviewed; 404 AA.
AC A0A1H3QFU7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000256|ARBA:ARBA00022248};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=SAMN05660462_01919 {ECO:0000313|EMBL:SDZ12143.1};
OS Proteiniborus ethanoligenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=415015 {ECO:0000313|EMBL:SDZ12143.1, ECO:0000313|Proteomes:UP000198625};
RN [1] {ECO:0000313|EMBL:SDZ12143.1, ECO:0000313|Proteomes:UP000198625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21650 {ECO:0000313|EMBL:SDZ12143.1,
RC ECO:0000313|Proteomes:UP000198625};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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}.
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}.
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DR EMBL; FNQE01000020; SDZ12143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3QFU7; -.
DR STRING; 415015.SAMN05660462_01919; -.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000198625; Unassembled WGS sequence.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
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; 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.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000198625}.
FT DOMAIN 329..404
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 404 AA; 44349 MW; FAF74AC68D161263 CRC64;
MNLKALTLND ILEAKERIRD ICVNTKLIYS SDFSKECGNE VYIKPENLQI TGAFKLRGAL
NKISKLTEEQ RKRGLIASSA GNHAQGVAYS ANRLGIKATI VMPKTTPLIK VQATREYGSN
VILKGEYYDE AYLEAKRLEK EKGYIFIHPF DDIEIMAGQG TIALEILEEL KDADAILVPI
GGGGLISGIA VAAKSVNPNI KVIGVEPEGA KAMKISIGED KLVNLPAVDT IADGGAVKKP
GHIAFDIIRE YVDEIITVDD FELMEAVFIL LEKHKLVVEA TGALTIAALK NLKFKGKKVV
SLVSGGNIDV VTMASMLNRG LLLRGRIFCF SVKLKDTPGQ LLKISEILAR LGANVIRLEH
DQFKAIDRLK HAVLEITVET NGREHIDEIT QELNREGYNV DKVY
//
