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Entry version 133 (08 May 2019)
Sequence version 1 (01 Aug 1998)
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Protein

L-threonine 3-dehydrogenase

Gene

tdh

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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

Catalyzes the NAD+-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate (PubMed:16233775, PubMed:15902509). Is much less efficient when using NADP+ instead of NAD+ (PubMed:16233775). To a lesser extent, also catalyzes the oxidation of L-serine and DL-threo-3-phenylserine, but not that of L-allo-threonine, D-threonine and D-allo-threonine and many other L-amino acids (PubMed:15902509).2 Publications

Miscellaneous

The enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of NADH.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Zn2+UniRule annotation2 PublicationsNote: Binds 2 Zn2+ ions per subunit. Contains one structural ion and one catalytic ion that seems to be less tightly bound at the site (PubMed:16233775). Zn2+ can be replaced by Mn2+ or Co2+ to some extent (PubMed:15902509).UniRule annotation1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Is totally inhibited by EDTA in vitro.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>Kineticsi

  1. KM=0.20 mM for L-threonine (at 50 degrees Celsius)1 Publication
  2. KM=0.024 mM for NAD+ (at 50 degrees Celsius)1 Publication
  3. KM=0.013 mM for L-threonine (in the presence of NAD+ as cosubstrate, at 65 degrees Celsius)1 Publication
  4. KM=0.010 mM for NAD+ (at 65 degrees Celsius)1 Publication
  5. KM=0.447 mM for L-threonine (in the presence of NAD+ as cosubstrate, at 65 degrees Celsius)1 Publication
  6. KM=0.689 mM for NADP+ (at 65 degrees Celsius)1 Publication
  1. Vmax=1.75 mmol/min/mg enzyme for the NAD+ oxidation of L-threonine (at 65 degrees Celsius)1 Publication
  2. Vmax=1.32 mmol/min/mg enzyme for the NADP+ oxidation of L-threonine (at 65 degrees Celsius)1 Publication

pH dependencei

Optimum pH is around 10. Below and above pH 10, the marked decrease of activity is observed: the relative activities are 50, 22 and 55% at pH 9.5, 9.2 and 12, respectively. Is stable over a wide pH range: upon heating at 50 degrees Celsius for 20 minutes, the enzyme does not lose activity at pH 4.5-10.0.1 Publication

Temperature dependencei

Optimum tempreature is 70 degrees Celsius. Extremely thermostable, the activity is not lost after incubation at 100 degrees Celsius for 20 minutes.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-threonine degradation via oxydo-reductase pathway

This protein is involved in step 1 of the subpathway that synthesizes glycine from L-threonine.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. L-threonine 3-dehydrogenase (tdh)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-threonine degradation via oxydo-reductase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from L-threonine, the pathway L-threonine degradation via oxydo-reductase pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi42Zinc 1; catalyticUniRule annotationCombined sources2 Publications1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei44Charge relay system1 Publication1
Active sitei47Charge relay system1 Publication1
Metal bindingi67Zinc 1; via tele nitrogen; catalyticUniRule annotationCombined sources2 Publications1 Publication1
Metal bindingi68Zinc 1; catalyticUniRule annotationCombined sources2 Publications1 Publication1
Metal bindingi97Zinc 2UniRule annotationCombined sources1 Publication1
Metal bindingi100Zinc 2UniRule annotationCombined sources1 Publication1
Metal bindingi103Zinc 2UniRule annotationCombined sources1 Publication1
Metal bindingi111Zinc 2UniRule annotationCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei152Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei179NAD; via amide nitrogen2 Publications1
Binding sitei199NADCombined sources2 Publications1
Binding sitei204NADCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi266 – 268NADCombined sources1 Publication3
Nucleotide bindingi291 – 292NADCombined sources1 Publication2

<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 functionOxidoreductase
LigandMetal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PHOR70601:G1G39-639-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.103 5244

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O58389

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

More...
UniPathwayi
UPA00046;UER00505

<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_and_taxonomy_section">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:
L-threonine 3-dehydrogenaseUniRule annotation (EC:1.1.1.103UniRule annotation2 Publications)
Short name:
L-ThrDH1 Publication
Short name:
TDH1 PublicationUniRule annotation
Alternative name(s):
L-threonine dehydrogenase2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:tdhUniRule annotation
Ordered Locus Names:PH0655
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri70601 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000752 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44T → A: Total loss of enzymatic activity. 1 Publication1
Mutagenesisi152E → A or Q: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi152E → C: 120-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi152E → D: Shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD(+), compared to wild-type. 1 Publication1
Mutagenesisi152E → K: Total loss of enzymatic activity. 1 Publication1
Mutagenesisi199E → A: Large decrease in affinity for NAD(+). 1 Publication1
Mutagenesisi204R → A: Large decrease in affinity for NAD(+). 1 Publication1
Mutagenesisi294R → A: 4000-fold decrease in catalytic efficiency. 1 Publication1

<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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001608771 – 348L-threonine 3-dehydrogenaseAdd BLAST348

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:16233775). Homotetramer; dimer of dimers (PubMed:17188300) (PubMed:15902509).

3 Publications

Protein-protein interaction databases

Molecular INTeraction database

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MINTi
O58389

STRING: functional protein association networks

More...
STRINGi
70601.3257063

<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

1348
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
O58389

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O58389

<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

<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

Belongs to the zinc-containing alcohol dehydrogenase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG01459 Archaea
COG1063 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000294686

KEGG Orthology (KO)

More...
KOi
K00060

Identification of Orthologs from Complete Genome Data

More...
OMAi
QIMGHEV

Database of Orthologous Groups

More...
OrthoDBi
67758at2157

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00627 Thr_dehydrog, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR004627 L-Threonine_3-DHase
IPR036291 NAD(P)-bd_dom_sf
IPR020843 PKS_ER

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00829 PKS_ER, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00692 tdh, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00059 ADH_ZINC, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

O58389-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEKMVAIMK TKPGYGAELV EVDVPKPGPG EVLIKVLATS ICGTDLHIYE
60 70 80 90 100
WNEWAQSRIK PPQIMGHEVA GEVVEIGPGV EGIEVGDYVS VETHIVCGKC
110 120 130 140 150
YACRRGQYHV CQNTKIFGVD TDGVFAEYAV VPAQNIWKNP KSIPPEYATL
160 170 180 190 200
QEPLGNAVDT VLAGPISGKS VLITGAGPLG LLGIAVAKAS GAYPVIVSEP
210 220 230 240 250
SDFRRELAKK VGADYVINPF EEDVVKEVMD ITDGNGVDVF LEFSGAPKAL
260 270 280 290 300
EQGLQAVTPA GRVSLLGLYP GKVTIDFNNL IIFKALTIYG ITGRHLWETW
310 320 330 340
YTVSRLLQSG KLNLDPIITH KYKGFDKYEE AFELMRAGKT GKVVFMLK
Length:348
Mass (Da):37,786
Last modified:August 1, 1998 - 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:i313F368AE83F793E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BA000001 Genomic DNA Translation: BAA29746.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H71110

NCBI Reference Sequences

More...
RefSeqi
WP_010884751.1, NC_000961.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAA29746; BAA29746; BAA29746

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1442986

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pho:PH0655

<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
BA000001 Genomic DNA Translation: BAA29746.1
PIRiH71110
RefSeqiWP_010884751.1, NC_000961.1

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
2D8AX-ray2.05A1-348[»]
2DFVX-ray2.05A/B/C2-348[»]
SMRiO58389
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

MINTiO58389
STRINGi70601.3257063

Genome annotation databases

EnsemblBacteriaiBAA29746; BAA29746; BAA29746
GeneIDi1442986
KEGGipho:PH0655

Phylogenomic databases

eggNOGiarCOG01459 Archaea
COG1063 LUCA
HOGENOMiHOG000294686
KOiK00060
OMAiQIMGHEV
OrthoDBi67758at2157

Enzyme and pathway databases

UniPathwayiUPA00046;UER00505
BioCyciPHOR70601:G1G39-639-MONOMER
BRENDAi1.1.1.103 5244
SABIO-RKiO58389

Miscellaneous databases

EvolutionaryTraceiO58389

Family and domain databases

HAMAPiMF_00627 Thr_dehydrog, 1 hit
InterProiView protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR004627 L-Threonine_3-DHase
IPR036291 NAD(P)-bd_dom_sf
IPR020843 PKS_ER
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SMARTiView protein in SMART
SM00829 PKS_ER, 1 hit
SUPFAMiSSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00692 tdh, 1 hit
PROSITEiView protein in PROSITE
PS00059 ADH_ZINC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiTDH_PYRHO
<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: O58389
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: August 1, 1998
Last modified: May 8, 2019
This is version 133 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 programProkaryotic 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, Complete proteome

Documents

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