Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 48 (11 Dec 2019)
Sequence version 1 (01 Nov 1998)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

D-threonine aldolase

Gene
N/A
Organism
Arthrobacter sp.
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 reversible cleavage of D-threonine or D-allothreonine into glycine and acetaldehyde. Can also cleave D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid, D-beta-3,4-dihydroxyphenylserine and D-beta-3,4-methylenedioxyphenylserine into glycine and the corresponding aldehyde compounds. Inactive towards D-serine, beta-hydroxyaspartate and O-phospho-DL-threonine.2 Publications

<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

Protein has several cofactor binding sites:

<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

Inhibited by the carbonyl reagents hydroxylamine, phenylhydrazine and semicarbazide. Inhibited by the chelating agent EDTA. Inhibited by the sulfhydryl reagent p-chloromercuribenzoic acid, and by sodium cyanide. Inhibited by iodoacetate, Ag2SO4, HgCl2 and CdCl2. Competitively inhibited by beta-hydroxyaspartate and O-phospho-DL-threonine.1 Publication

<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=3.81 mM for D-threonine (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  2. KM=14.0 mM for D-allothreonine (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  3. KM=1.75 mM for D-threo-beta-hydroxy-alpha-aminovaleric acid (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  4. KM=46.8 mM for D-threo-beta-phenylserine (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  5. KM=8.4 mM for D-threonine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  6. KM=8.8 mM for D-threonine (at pH 8.0, in the absence of MnCl2)2 Publications
  7. KM=4.4 mM for D-allothreonine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  8. KM=4.3 mM for D-allothreonine (at pH 8.0, in the absence of MnCl2)2 Publications
  9. KM=5.4 mM for DL-threo-phenylserine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  10. KM=5.9 mM for DL-threo-phenylserine (at pH 8.0, in the absence of MnCl2)2 Publications
  11. KM=5.3 mM for DL-erythro-phenylserine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  12. KM=4.9 mM for DL-erythro-phenylserine (at pH 8.0, in the absence of MnCl2)2 Publications
  13. KM=1.8 mM for DL-threo-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  14. KM=1.8 mM for DL-threo-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the absence of MnCl2)2 Publications
  15. KM=2.5 mM for DL-erythro-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  16. KM=2.0 mM for DL-erythro-beta-3,4-methylenedioxyphenylserine (at pH 8.0, in the absence of MnCl2)2 Publications
  17. KM=1.2 mM for DL-threo-beta-3,4-dihydroxyphenylserine (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  18. KM=1.4 mM for DL-threo-beta-3,4-dihydroxyphenylserine (at pH 8.0, in the absence of MnCl2)2 Publications
  1. Vmax=38.8 µmol/min/mg enzyme with D-threonine as substrate (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  2. Vmax=102 µmol/min/mg enzyme with D-allothreonine as substrate (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  3. Vmax=9.01 µmol/min/mg enzyme with D-threo-beta-hydroxy-alpha-aminovaleric acid as substrate (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  4. Vmax=59.9 µmol/min/mg enzyme with D-threo-beta-phenylserine as substrate (at pH 7.5, in the presence of 0.5 mM MnCl2)2 Publications
  5. Vmax=32.1 µmol/min/mg enzyme with D-threonine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  6. Vmax=3.0 µmol/min/mg enzyme with D-threonine as substrate (at pH 8.0, in absence of MnCl2)2 Publications
  7. Vmax=34.9 µmol/min/mg enzyme with D-allothreonine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  8. Vmax=2.8 µmol/min/mg enzyme with D-allothreonine as substrate (at pH 8.0, in absence of MnCl2)2 Publications
  9. Vmax=209.8 µmol/min/mg enzyme with DL-threo-phenylserine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  10. Vmax=4.9 µmol/min/mg enzyme with DL-threo-phenylserine as substrate (at pH 8.0, in absence of MnCl2)2 Publications
  11. Vmax=164.4 µmol/min/mg enzyme with DL-erythro-phenylserine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  12. Vmax=1.9 µmol/min/mg enzyme with DL-erythro-phenylserine as substrate (at pH 8.0, in absence of MnCl2)2 Publications
  13. Vmax=129.3 µmol/min/mg enzyme with DL-threo-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  14. Vmax=9.2 µmol/min/mg enzyme with DL-threo-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in absence of MnCl2)2 Publications
  15. Vmax=16.0 µmol/min/mg enzyme with DL-erythro-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  16. Vmax=1.9 µmol/min/mg enzyme with DL-erythro-beta-3,4-methylenedioxyphenylserine as substrate (at pH 8.0, in absence of MnCl2)2 Publications
  17. Vmax=84.6 µmol/min/mg enzyme with DL-threo-beta-3,4-dihydroxyphenylserine as substrate (at pH 8.0, in the presence of 0.1 µM MnCl2)2 Publications
  18. Vmax=8.4 µmol/min/mg enzyme with DL-threo-beta-3,4-dihydroxyphenylserine as substrate (at pH 8.0, in absence of MnCl2)2 Publications

pH dependencei

Optimum pH is 8.0-9.0. Stable between pH 7.0 and 8.5.2 Publications

Temperature dependencei

Stable below 55 degrees Celsius.2 Publications

<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

  • aldehyde-lyase activity Source: UniProtKB
  • D-threonine aldolase activity Source: UniProtKB-EC

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
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.2.42 457

<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:
D-threonine aldolase2 Publications (EC:4.1.2.42)
<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>OrganismiArthrobacter sp.
<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 identifieri1667 [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 lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00004039972 – 379D-threonine aldolase1 PublicationAdd BLAST378

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 residuei59N6-(pyridoxal phosphate)lysine1

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O82872

<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

3D structure databases

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

More...
SMRi
O82872

Database of comparative protein structure models

More...
ModBasei
Search...

<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 DSD1 family.Curated

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K19967

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.37.20, 1 hit
3.20.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001608 Ala_racemase_N
IPR026956 D-ser_dehydrat-like_dom
IPR042208 D-ser_dehydrat-like_sf
IPR029066 PLP-binding_barrel

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01168 Ala_racemase_N, 1 hit
PF14031 D-ser_dehydrat, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01119 D-ser_dehydrat, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51419 SSF51419, 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.

<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 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.

O82872-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQEVIRGIA LPPPAQPGDP LARVDTPSLV LDLAPFEANL RAMQAWADRH
60 70 80 90 100
DVALRPHAKA HKCPEIALRQ LALGARGICC QKVSEALPFV AAGIQDIHIS
110 120 130 140 150
NEVVGPAKLA LLGQLARVAK ISVCVDNAHN LSQVSQAMVQ AGAQIDVLVE
160 170 180 190 200
VDVGQGRCGV SDDALVLALA QQARDLPGVN FAGLQAYHGS VQHYRTREER
210 220 230 240 250
AEVCRQAARI AASYAQLLRE SGIACDTITG GGTGSAEFDA ASGVYTELQA
260 270 280 290 300
GSYAFMDGDY GANEWDGPLA FENSLFVLAT VMSKPAPDRV ILDAGLKSTT
310 320 330 340 350
AECGPPAIFG EPGLTYTAIN DEHGVVRVEP GAQAPDLGAV LRLVPSHVDP
360 370
TFNLHDGLVV VRDGVVEDIW EISARGFSR
Length:379
Mass (Da):40,031
Last modified:November 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:iA5B6A3C2877CD2EB
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
AB010956 Genomic DNA Translation: BAA31547.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:BAA31547

<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
AB010956 Genomic DNA Translation: BAA31547.1

3D structure databases

SMRiO82872
ModBaseiSearch...

Proteomic databases

PRIDEiO82872

Genome annotation databases

KEGGiag:BAA31547

Phylogenomic databases

KOiK19967

Enzyme and pathway databases

BRENDAi4.1.2.42 457

Family and domain databases

Gene3Di2.40.37.20, 1 hit
3.20.20.10, 1 hit
InterProiView protein in InterPro
IPR001608 Ala_racemase_N
IPR026956 D-ser_dehydrat-like_dom
IPR042208 D-ser_dehydrat-like_sf
IPR029066 PLP-binding_barrel
PfamiView protein in Pfam
PF01168 Ala_racemase_N, 1 hit
PF14031 D-ser_dehydrat, 1 hit
SMARTiView protein in SMART
SM01119 D-ser_dehydrat, 1 hit
SUPFAMiSSF51419 SSF51419, 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 nameiDTA_ARTSP
<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: O82872
<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: February 8, 2011
Last sequence update: November 1, 1998
Last modified: December 11, 2019
This is version 48 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again