ID Q8G466_BIFLO Unreviewed; 415 AA.
AC Q8G466;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN Name=tdcB {ECO:0000313|EMBL:AAN25319.1};
GN OrderedLocusNames=BL1527 {ECO:0000313|EMBL:AAN25319.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN25319.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN25319.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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}.
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DR EMBL; AE014295; AAN25319.1; -; Genomic_DNA.
DR RefSeq; NP_696683.1; NC_004307.2.
DR AlphaFoldDB; Q8G466; -.
DR STRING; 206672.BL1527; -.
DR EnsemblBacteria; AAN25319; AAN25319; BL1527.
DR KEGG; blo:BL1527; -.
DR PATRIC; fig|206672.9.peg.1428; -.
DR HOGENOM; CLU_021152_4_1_11; -.
DR OrthoDB; 9811476at2; -.
DR PhylomeDB; Q8G466; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000000439; Chromosome.
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:0006567; P:threonine catabolic process; IEA:InterPro.
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 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:UP000000439}.
FT DOMAIN 339..415
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 415 AA; 44115 MW; 5BDC90684ED93A89 CRC64;
MKALQRDHAA ELKLAAERLK GTARHTEIIP SPVLSEMTGH EILLKPENLQ VTGSFKIRGA
YNKIASLTEE QIAHGIVTAS AGNHAQGVAY AARERGAKAT ICMPQITPPL KVDATKAYGA
DVVLYGDVFD ESAAHAAELA DKEGMIYVPP FDDYEVICGQ GTIGLEILED VPNVTDVVVP
LGGGGLGAGV ALAIKTFKPE VRVIGAIPEG SPAWKDSLAA GRVSPADHVV TSAEGVAVKH
PGDLPFALIN EFLDDLVTVT ERDINEMILL MLEKHKLVVE AAGAVSLAAL EHLNLRSRKF
AAATGPHVVV PIMSGGNIDT VTMGAVIQKG MIARGRIMNF EVELPDTPGQ LVKVATLLAE
QRANVIQLDH DQFKASGHYT NAVSLGVTVE TNGPEHIDRI LAALREAGFQ PKRIY
//
