ID A0A1M6PJC9_9FIRM Unreviewed; 403 AA.
AC A0A1M6PJC9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000256|ARBA:ARBA00022248};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=SAMN02745123_00619 {ECO:0000313|EMBL:SHK08062.1};
OS Desulforamulus aeronauticus DSM 10349.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121421 {ECO:0000313|EMBL:SHK08062.1, ECO:0000313|Proteomes:UP000183997};
RN [1] {ECO:0000313|EMBL:SHK08062.1, ECO:0000313|Proteomes:UP000183997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10349 {ECO:0000313|EMBL:SHK08062.1,
RC ECO:0000313|Proteomes:UP000183997};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRAR01000006; SHK08062.1; -; Genomic_DNA.
DR RefSeq; WP_072910827.1; NZ_FRAR01000006.1.
DR AlphaFoldDB; A0A1M6PJC9; -.
DR STRING; 1121421.SAMN02745123_00619; -.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR UniPathway; UPA00052; UER00507.
DR Proteomes; UP000183997; 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; 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}.
FT DOMAIN 329..403
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 403 AA; 42419 MW; 314EC6C0E7077174 CRC64;
MQNITLADIY TARECLKGVI HHTDLVPNTT LSEMTGSDVY LKLENLQKTG SFKIRGAFNK
ICNLSSAEKQ AGVIASSAGN HAQGVALAAS TYGIRSTIVM PTCAPLAKIT ATKSYGANVV
LHGNVYDDAY AKAMEIQKET GATFIHPFDD PYVIAGQGTI ALEILDELPA VDAILIPIGG
GGIVAGIAIA AKAIKPSVKI IGVEPANAAS MRESSQAGKI ITLSSANTIA DGIAVKTPGT
LTYDIVKEYV DEFVTVEEDE IANAILILME RCKLIAEGAG AASVAALLNS KVNLPGKKIA
AVISGGNIDV NMLSRIVDKG LAKAGRKTEL TTIIPDKPGQ LQGLLKSIGD LSANVVEVHH
NRIRSEVELG SARVDLVLET QDSEHLASII QELIKKGYCV QRI
//
