ID   A0A160F2H3_9BACI        Unreviewed;       402 AA.
AC   A0A160F2H3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   Name=ilvA {ECO:0000313|EMBL:ANB59922.1};
GN   ORFNames=GFC30_1886 {ECO:0000313|EMBL:ANB59922.1};
OS   Anoxybacillus amylolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB59922.1, ECO:0000313|Proteomes:UP000076865};
RN   [1] {ECO:0000313|EMBL:ANB59922.1, ECO:0000313|Proteomes:UP000076865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB59922.1,
RC   ECO:0000313|Proteomes:UP000076865};
RX   PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA   Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA   Gambacorta A., Nicolaus B.;
RT   "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT   bacterium isolated from Mount Rittmann (Antarctica).";
RL   Syst. Appl. Microbiol. 29:300-307(2006).
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|ARBA:ARBA00025527}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP015438; ANB59922.1; -; Genomic_DNA.
DR   RefSeq; WP_066324650.1; NZ_CP015438.1.
DR   AlphaFoldDB; A0A160F2H3; -.
DR   KEGG; aamy:GFC30_1886; -.
DR   PATRIC; fig|294699.3.peg.1932; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000076865; Chromosome.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
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; 3.30.70.260; -; 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; 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   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   Lyase {ECO:0000313|EMBL:ANB59922.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076865}.
FT   DOMAIN          327..402
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   402 AA;  43928 MW;  F0321369BD2CED0D CRC64;
     MLTLNDVLQA REKMKGIVHQ TPLEHSQTFS QFSLNEVYMK LENLQKTGSF KVRGSFNKIM
     SLSEEERQRG VVAASAGNHA QGVAYSSTMI GIPCTIVMPK GAPLSKVQAT KGYGADVILH
     GDVFDESLEY ALELQRQRQA TFVHPFDDLA VMAGQGTISL EILEQLPDAE VVLCPVGGGG
     LLAGLAFTLK QLKPSIQVYG VESSACPGMT AALRHKKPVT ITSSDTIADG IAVKKPGNIT
     YEYIEKYVDG VVCVEEAEIS RTMLYLLERN KLLVEGSGAC SLAALLYHKL PFTGKKVVAV
     LSGGNVDVTL ISRIIERGLV ESGRFVTFTT VISDKPGQLN KLLRIIAELE ANVMSIHHQR
     IGAKVLPGQA EIHFSLETKN QDHIHHIHQV LMKEGYDVEF FQ
//