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Entry version 130 (12 Aug 2020)
Sequence version 1 (01 May 1992)
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Protein

Threonine dehydratase 2 biosynthetic, chloroplastic

Gene

TD2

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Not required for normal growth and development of the plant (PubMed:21436043).1 Publication
Involved in defense against lepidopteran, but not coleopteran herbivore insects (PubMed:21436043, PubMed:17416643). Acts in the insect gut to degrade threonine, which is an essential and limiting nutrient for the growth of lepidopteran larvae (Probable). Active against both L-threonine and L-serine (PubMed:17416643).Curated2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphateBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Threonine dehydratase 2 biosynthetic, chloroplastic: Strongly inhibited by 1 mM isoleucine (PubMed:21436043). Processed threonine dehydratase 2: Not inhibited by isoleucine (PubMed:21436043, PubMed:17416643).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Threonine dehydratase 2 biosynthetic, chloroplastic: Active at alkaline pH (PubMed:21436043, PubMed:17416643). Processed threonine dehydratase 2: Optimum pH is 9. Has little or no activity at pH values below 6.0 (PubMed:17416643).2 Publications

Temperature dependencei

Threonine dehydratase 2 biosynthetic, chloroplastic: Optimum temperature is 60 degrees Celsius. Abnormally stable at elevated temperatures (PubMed:21436043). Processed threonine dehydratase 2: Active over a wide range of temperatures. Optimal enzyme activity against L-threonine is at 58 degrees Celsius (PubMed:17416643).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 2-oxobutanoate from L-threonine.
Proteins known to be involved in this subpathway in this organism are:
  1. Threonine dehydratase, Threonine dehydratase 2 biosynthetic, chloroplastic (TD2), Threonine dehydratase, Threonine dehydratase 1 biosynthetic, chloroplastic (TD1)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-oxobutanoate from L-threonine, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis, Plant defense
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.3.1.19, 3101

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00047;UER00054

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Threonine dehydratase 2 biosynthetic, chloroplasticCurated (EC:4.3.1.171 Publication, EC:4.3.1.193 Publications)
Alternative name(s):
SlTD21 Publication
Threonine deaminase 21 Publication
Cleaved into the following chain:
Alternative name(s):
Processed TD21 Publication
Short name:
pTD22 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TD21 Publication
Synonyms:TD1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4081 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumSolanum subgen. Lycopersicon
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000004994 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 51Chloroplast2 PublicationsAdd BLAST51
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003361452 – 595Threonine dehydratase 2 biosynthetic, chloroplastic2 PublicationsAdd BLAST544
ChainiPRO_000044551652 – 415Processed threonine dehydratase 21 PublicationAdd BLAST364

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei143N6-(pyridoxal phosphate)lysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytically cleaved by a chymotrypsin-like digestive protease in the midgut of the lepidopteran insects to remove the C-terminal regulatory domain, which allows efficient metabolizing of threonine in the presence of high isoleucine levels in the gut.2 Publications

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P25306

PRoteomics IDEntifications database

More...
PRIDEi
P25306

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in floral buds, 8-9 mm long flowers 1 to 2 days before anthesis, open flowers and floral organs including sepals, petals, stamens and carpels of 8-9 mm flowers (at protein level) (PubMed:7550377). Expressed in very early floral meristems of the anantha. Over 500-fold expression in mature flowers compared to leaves (PubMed:2011578). Expressed in sepals, petals, stamens and carpels of the mature flower. In sepals, mostly expressed in the abaxial mesophyll cells and in petals in parenchymal cells. Not expressed in epidermal or vascular tissues of sepals and petals. In stamens, expressed in parenchymal cells of the connective and lobes, but not expressed in differentiated tissues such as tapetum (TP), stomium (SM), or pollen grains (PG) (PubMed:2011578, PubMed:7550377). Not expressed in roots or seeds (PubMed:2011578). High level of expression in immature flower buds, unopened flowers and opened flowers (PubMed:17416643, PubMed:7550377). Not expressed in unstressed leaves, root, stem or petiole (PubMed:17416643).3 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

During the pre-organogenesis stage of the floral primordium, expressed in scattered islands of cells in the central parenchymatous pith region and in the peripheral ground parenchyma. Upon sepal buttresses emergence, expressed in all parenchyma mesophyll cells accumulating in a continous pattern in the central pith cells of the floral primordia, but not expressed in the future epidermal cells. As the mesophyll and vascular tissues elongate and differentiate, highly expressed in the abaxial mesophyll cells of sepals, but down-regulated in the adaxial cell layers. At anthesis, down-regulated expression in all mesophyll cells of the sepal. In petals, expressed in all mesophyll cells throughout development.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is induced in response to methyl jasmonate (MeJA) and locally and systemically in response to mechanical wounding (PubMed:17416643). Parenchyma-specific induction of expression in flowers and leaves by MeJA. No induction of expression by MeJA in epidermal, vascular or sporogenous tissues (PubMed:7550377). Caterpillar (Helicoverpa zea) labial saliva induces expression in leaves damaged by herbivory (PubMed:23065106).3 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P25306, baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P25306
With#Exp.IntAct
itself2EBI-15916506,EBI-15916506

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59625N

STRING: functional protein association networks

More...
STRINGi
4081.Solyc09g008670.2.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1595
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P25306

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P25306

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini420 – 492ACT-like 1PROSITE-ProRule annotationAdd BLAST73
Domaini514 – 585ACT-like 2PROSITE-ProRule annotationAdd BLAST72

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1250, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_021152_6_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25306

KEGG Orthology (KO)

More...
KOi
K01754

Identification of Orthologs from Complete Genome Data

More...
OMAi
YDEGRNI

Database of Orthologous Groups

More...
OrthoDBi
906802at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1020.10, 1 hit
3.40.50.1100, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001926, PLP-dep
IPR000634, Ser/Thr_deHydtase_PyrdxlP-BS
IPR001721, TD_ACT-like
IPR038110, TD_ACT-like_sf
IPR005787, Thr_deHydtase_biosynth
IPR036052, Trypto_synt_PLP_dependent

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00291, PALP, 1 hit
PF00585, Thr_dehydrat_C, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53686, SSF53686, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01124, ilvA_2Cterm, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51672, ACT_LIKE, 2 hits
PS00165, DEHYDRATASE_SER_THR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P25306-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEFLCLAPTR SFSTNPKLTK SIPSDHTSTT SRIFTYQNMR GSTMRPLALP
60 70 80 90 100
LKMSPIVSVP DITAPVENVP AILPKVVPGE LIVNKPTGGD SDELFQYLVD
110 120 130 140 150
ILASPVYDVA IESPLELAEK LSDRLGVNFY IKREDKQRVF SFKLRGAYNM
160 170 180 190 200
MSNLSREELD KGVITASAGN HAQGVALAGQ RLNCVAKIVM PTTTPQIKID
210 220 230 240 250
AVRALGGDVV LYGKTFDEAQ THALELSEKD GLKYIPPFDD PGVIKGQGTI
260 270 280 290 300
GTEINRQLKD IHAVFIPVGG GGLIAGVATF FKQIAPNTKI IGVEPYGAAS
310 320 330 340 350
MTLSLHEGHR VKLSNVDTFA DGVAVALVGE YTFAKCQELI DGMVLVANDG
360 370 380 390 400
ISAAIKDVYD EGRNILETSG AVAIAGAAAY CEFYKIKNEN IVAIASGANM
410 420 430 440 450
DFSKLHKVTE LAGLGSGKEA LLATFMVEQQ GSFKTFVGLV GSLNFTELTY
460 470 480 490 500
RFTSERKNAL ILYRVNVDKE SDLEKMIEDM KSSNMTTLNL SHNELVVDHL
510 520 530 540 550
KHLVGGSANI SDEIFGEFIV PEKAETLKTF LDAFSPRWNI TLCRYRNQGD
560 570 580 590
INASLLMGFQ VPQAEMDEFK NQADKLGYPY ELDNYNEAFN LVVSE
Length:595
Mass (Da):64,937
Last modified:May 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAC430BB5DD9F0348
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M61914 mRNA Translation: AAA34171.1
M61915 Genomic DNA Translation: AAA68097.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A38628

NCBI Reference Sequences

More...
RefSeqi
NP_001296095.1, NM_001309166.1

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
Solyc09g008670.3.1; Solyc09g008670.3.1; Solyc09g008670.3

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
543983

Gramene; a comparative resource for plants

More...
Gramenei
Solyc09g008670.3.1; Solyc09g008670.3.1; Solyc09g008670.3

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sly:543983

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61914 mRNA Translation: AAA34171.1
M61915 Genomic DNA Translation: AAA68097.1
PIRiA38628
RefSeqiNP_001296095.1, NM_001309166.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IAUX-ray2.35A/B53-418[»]
SMRiP25306
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59625N
STRINGi4081.Solyc09g008670.2.1

Proteomic databases

PaxDbiP25306
PRIDEiP25306

Genome annotation databases

EnsemblPlantsiSolyc09g008670.3.1; Solyc09g008670.3.1; Solyc09g008670.3
GeneIDi543983
GrameneiSolyc09g008670.3.1; Solyc09g008670.3.1; Solyc09g008670.3
KEGGisly:543983

Phylogenomic databases

eggNOGiKOG1250, Eukaryota
HOGENOMiCLU_021152_6_3_1
InParanoidiP25306
KOiK01754
OMAiYDEGRNI
OrthoDBi906802at2759

Enzyme and pathway databases

UniPathwayiUPA00047;UER00054
BRENDAi4.3.1.19, 3101

Miscellaneous databases

EvolutionaryTraceiP25306

Gene expression databases

ExpressionAtlasiP25306, baseline and differential

Family and domain databases

Gene3Di3.40.1020.10, 1 hit
3.40.50.1100, 2 hits
InterProiView protein in InterPro
IPR001926, PLP-dep
IPR000634, Ser/Thr_deHydtase_PyrdxlP-BS
IPR001721, TD_ACT-like
IPR038110, TD_ACT-like_sf
IPR005787, Thr_deHydtase_biosynth
IPR036052, Trypto_synt_PLP_dependent
PfamiView protein in Pfam
PF00291, PALP, 1 hit
PF00585, Thr_dehydrat_C, 2 hits
SUPFAMiSSF53686, SSF53686, 1 hit
TIGRFAMsiTIGR01124, ilvA_2Cterm, 1 hit
PROSITEiView protein in PROSITE
PS51672, ACT_LIKE, 2 hits
PS00165, DEHYDRATASE_SER_THR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTD2_SOLLC
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P25306
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: August 12, 2020
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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