ID W9RGL2_9ROSA Unreviewed; 610 AA.
AC W9RGL2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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};
GN ORFNames=L484_022629 {ECO:0000313|EMBL:EXB75950.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB75950.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) 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; KE344693; EXB75950.1; -; Genomic_DNA.
DR RefSeq; XP_010098862.1; XM_010100560.1.
DR AlphaFoldDB; W9RGL2; -.
DR STRING; 981085.W9RGL2; -.
DR GeneID; 21405440; -.
DR KEGG; mnt:21405440; -.
DR eggNOG; KOG1250; Eukaryota.
DR OrthoDB; 5476420at2759; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000030645; Unassembled WGS sequence.
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:UP000030645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 437..508
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
FT DOMAIN 530..601
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
FT REGION 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 66310 MW; DFAE1869CF32BFF5 CRC64;
MEALRLTRAH SPLLPSKWPE LAQRRPNEAH RAANGRQIRP FIAATLSKPA AEISPNPSAP
SAGNGAAAAT LRNPPTAPAR LRVSADSLQY PAGYVGAAPD RSAIGDGDDA LSYLTNILSS
KVYDVAIESP LHFAPRLSER LGVKVWLKRE DLQPVFSFKL RGAYNMMAKL TKEDLERGVI
CSSAGNHAQG VALAAKKLGC DAVIAMPVTT PEIKWQSVER LGATVVLVGD SYDEAQAYAK
KRSEEEGRAF IPPFDHPDVI MGQGTVGMEI VRQMKGPLHA IFVPVGGGGL IAGIAAYVKR
VTPEVKIIGV EPSDANAMAL SLHHGQRVIL DQVGGFADGV AVKEVGEETF RLCRELVDGV
VLVSRDAICA SIKDMFEEKR SILEPAGALA LAGAEAYCRY YGIKGENVVA ISSGANMNFD
KLRVVTELAN VGRQQEAVLA TVLPEVAGSF KHFCQLVGPM DITEFKYRYS SDKEAVVLYS
VGVHTVSELK EMVERMASSQ LQTYNLTEND LVKDHLRYLM GGRLNVQNEV LCRFVFPERP
GALLKFLDAF SPRWNITLFH YRGQGATGAN VLVGIQVPSS EMDEFRDRAD SLGYEYTVVT
NDGDFKLLMH
//
