TD1_SOLLC
ID TD1_SOLLC Reviewed; 606 AA.
AC A0FKE6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Threonine dehydratase 1 biosynthetic, chloroplastic {ECO:0000305};
DE EC=4.3.1.19 {ECO:0000255|RuleBase:RU362012, ECO:0000269|PubMed:21436043};
DE AltName: Full=SlTD1 {ECO:0000303|PubMed:17416643};
DE AltName: Full=Threonine deaminase 1 {ECO:0000303|PubMed:21436043};
DE Flags: Precursor;
GN Name=TD1 {ECO:0000303|PubMed:17416643};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|EMBL:ABK20067.1};
RN [1] {ECO:0000312|EMBL:ABK20067.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17416643; DOI=10.1104/pp.107.095588;
RA Chen H., Gonzales-Vigil E., Wilkerson C.G., Howe G.A.;
RT "Stability of plant defense proteins in the gut of insect herbivores.";
RL Plant Physiol. 143:1954-1967(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21436043; DOI=10.1073/pnas.1016157108;
RA Gonzales-Vigil E., Bianchetti C.M., Phillips G.N. Jr., Howe G.A.;
RT "Adaptive evolution of threonine deaminase in plant defense against insect
RT herbivores.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5897-5902(2011).
CC -!- FUNCTION: Has a housekeeping role in isoleucine biosynthesis
CC (Probable). {ECO:0000305|PubMed:17416643}.
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:0000255|RuleBase:RU362012,
CC ECO:0000269|PubMed:21436043};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|RuleBase:RU362012};
CC -!- ACTIVITY REGULATION: Strongly inhibited by 1 mM isoleucine.
CC {ECO:0000269|PubMed:21436043}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at alkaline pH. {ECO:0000269|PubMed:21436043};
CC Temperature dependence:
CC Optimum temperature is 16 degrees Celsius. Not active at temperatures
CC above 55 degrees Celsius. Complete loss of activity by incubation at
CC 55 degrees Celsius for 1 min. {ECO:0000269|PubMed:21436043};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000255|RuleBase:RU362012}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in all tissues examined
CC including root, stem, petiole, leaf, immature flower bud, unopened
CC flower and opened flower with the highest expression in opened flower
CC and lowest in leaf. {ECO:0000269|PubMed:17416643}.
CC -!- INDUCTION: Constitutively expressed. Not induced in response to methyl
CC jasmonate (MeJA) or mechanical wounding. {ECO:0000269|PubMed:17416643}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000255|RuleBase:RU362012, ECO:0000305}.
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DR EMBL; EF026088; ABK20067.1; -; mRNA.
DR RefSeq; NP_001234234.1; NM_001247305.2.
DR AlphaFoldDB; A0FKE6; -.
DR SMR; A0FKE6; -.
DR STRING; 4081.Solyc10g083760.1.1; -.
DR PaxDb; A0FKE6; -.
DR PRIDE; A0FKE6; -.
DR GeneID; 100037737; -.
DR KEGG; sly:100037737; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_6_2_1; -.
DR InParanoid; A0FKE6; -.
DR OrthoDB; 906802at2759; -.
DR PhylomeDB; A0FKE6; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000004994; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.1020.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001926; PLP-dep.
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; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Isoleucine biosynthesis; Lyase; Plastid; Pyridoxal phosphate;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN ?..606
FT /note="Threonine dehydratase 1 biosynthetic, chloroplastic"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445517"
FT DOMAIN 432..504
FT /note="ACT-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT DOMAIN 526..597
FT /note="ACT-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT MOD_RES 154
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04968"
SQ SEQUENCE 606 AA; 66182 MW; C64E3ACE0EACB7C5 CRC64;
MEVLRFTAVK SLNSCVRPEF TAMSSVIVPI STVKVSGTRK SKKKALICAK ATEILSSPAT
VTEPLKAEPA EAPVPLLRVS PSSLQCEPGY LLPNSPVLGT GGVTGYEYLT NILSSKVYDV
AYETPLQKAP KLSERLGVNV WLKREDLQPV FSFKIRGAYN MMAKLPKEQL EKGVICSSAG
NHAQGVALSA QRLGCDAVIV MPVTTPDIKW KSVKRLGATV VLVGDSYDEA QAYAKKRAES
EGRTFIPPFD HPDVIVGQGT VGMEINRQLK DNIHAIFVPV GGGGLIAGIA AYLKRVAPDI
KIIGVEPLDA NALALSLHHG QRVMLDQVGG FADGVAVKVV GEETYRLCEE LIDGVVLVGR
DAICASIKDM FEEKRSILEP AGALALAGAE AYCKYYGLKG ENVVAITSGA NMNFDRLRLV
TELADVGRQR EAVLATFMPE DPGSFKKFAE MVGPMNITEF KYRYNSDKER ALVLYSVGLH
TILELEGMVE RMESADLQTI NLTDNDLVKD HLRHLMGGRT NVHNELLCRF TFPEKPGALM
KFLDAFSPRW NISLFHYRAQ GDTGANVLVG IQVPPDEVVE FEGRADSLGY EYAMESLNEA
YQLIMH
