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Database: UniProt
Entry: A0A453JIQ7_AEGTS
LinkDB: A0A453JIQ7_AEGTS
Original site: A0A453JIQ7_AEGTS 
ID   A0A453JIQ7_AEGTS        Unreviewed;       567 AA.
AC   A0A453JIQ7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET5Gv20073000.5, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET5Gv20073000.5}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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|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|RuleBase:RU362012}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|RuleBase:RU362012}.
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DR   AlphaFoldDB; A0A453JIQ7; -.
DR   STRING; 200361.A0A453JIQ7; -.
DR   EnsemblPlants; AET5Gv20073000.5; AET5Gv20073000.5; AET5Gv20073000.
DR   Gramene; AET5Gv20073000.5; AET5Gv20073000.5; AET5Gv20073000.
DR   OMA; ICRKLMD; -.
DR   OrthoDB; 5476420at2759; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000015105; Chromosome 5D.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012}; Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        529..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..377
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   567 AA;  59959 MW;  263133077E93F658 CRC64;
     MEAAAAAASS PSMTPFRPAP RVACLARSRV AATPLRAVPL MRVAPESLQA ASGSLVGVPS
     RGTGDLDGPG AMEYLTAVLA SKVYDVAVQT PLERAGKLSE RLGVDLHIKR EDLQPEPAFS
     FKLRGAYNMM AKLSQEQLNN GVICSSAGNH AQGVALSAQR LGCHAVIVMP VTTPENKWRS
     VEKLGATVVL KGDSYDEAQS YAKLLCEEEG LTFIPPFDHP DIIAGQGTVG MEIVRQLQGP
     LHAIFVPVGG GGLIAGIAAY VKRVCPEVKI IGVEPSDANA MALSLFHGQR VMLEHIGGFA
     DGVAVKVVGK ETFPLCQDFV DGIVLVSQDA ICASIKDMFE ENRNILEPSG ALALAGAEAY
     CKYYGLKGET VVAISSGANM NFDTLRLVTE LPDVGRKPEA VLPTFSPKEQ GSFKEFAELV
     SRMNITEFKH IYDSHGKEAL VLHSGSDDVG DEPVEAKPVE AGDDGKECED SCRPCGEGEK
     PLAWLNARVV TTTGIINLMT AGLGLYVKAH HPSVLGLVVT CWEALPLTMV RVVLVSGLGA
     ALALGVLLMY AGIKMSLQGG PRPARPS
//
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