ID   A0A2L2T2N2_9HYPO        Unreviewed;       577 AA.
AC   A0A2L2T2N2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Threonine dehydratase {ECO:0000256|RuleBase:RU362012};
DE            EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012};
DE   AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI63928.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001274,
CC         ECO:0000256|RuleBase:RU362012};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004810, ECO:0000256|RuleBase:RU362012}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
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DR   EMBL; LN649229; CEI63928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2T2N2; -.
DR   STRING; 56646.A0A2L2T2N2; -.
DR   OrthoDB; 5476420at2759; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000245910; Chromosome i.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04906; ACT_ThrD-I_1; 1.
DR   CDD; cd04907; ACT_ThrD-I_2; 1.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; TD_ACT-like.
DR   InterPro; IPR038110; TD_ACT-like_sf.
DR   InterPro; IPR005787; Thr_deHydtase_biosynth.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01124; ilvA_2Cterm; 1.
DR   PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU362012};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW   ECO:0000256|RuleBase:RU362012}; Lyase {ECO:0000256|RuleBase:RU362012};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245910};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          398..474
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51672"
FT   DOMAIN          496..567
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51672"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  63093 MW;  49C87EE251458184 CRC64;
     MPSADPIVAV PANGAVNGTN GESRPQTPMT GMALTEYSAN PSTPSAEKQA RLREIVPEEY
     LLPTGYPDYL RLIASATSRV YEACKITPLT HAINLSNRLE CNVLLKREDE QPVFSFKLRG
     AYNKMAHLDP KKSWKGVVCC SAGNHAQGVA YSARKLKIPA TIVMPEATPS IKHLNVARLG
     GHVVLHGADF DAAKEECARR EVQDGLINIP PFDDPYVIAG QGTIGNELFG QVNMAKVEAI
     FCCVGGGGLI AGIGLYVKRM APHVKIIGVE AHDANAMAQS LKKGERVLLK EVGLFADGAA
     VKIPGEETFR ICKEVIDDVI EVSTDEICAA IKDMYDDTRS GLEPAGALSI AGLKKYVSQN
     PSDDSKRNLI AITSGANMNF DRLRFVAERA TMGEGKEALL SVQIPERPGA FSELINNIMP
     HGVTEFSYRY STDEVANILI GVSLTAPAHQ RSEELRSLID RIQSNNMTVT DLSNDELAKS
     HIRYLVGGRS GVPNERLYMF TFPERPGALE KFLVTLRPKF NISLFQYRNY GGDVGKIVTG
     ILCPDEEVTE LHNFLRKIGY PYEDCTESPV FKTFLRS
//