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UniProtKB - P07913 (TDH_ECOLI)

Entry version 186 (02 Jun 2021)
Sequence version 1 (01 Nov 1988)
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Protein

L-threonine 3-dehydrogenase

Gene

tdh

Organism
Escherichia coli (strain K12)
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. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP+ instead of NAD+.

1 Publication

<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

Zn2+UniRule annotation1 Publication1 Publication, Co2+1 Publication, Cd2+1 PublicationNote: Binds 2 Zn2+ ions per subunit. Co2+ and Cd2+ can exchange for Zn2+ (PubMed:2007567). Probably contains one structural ion and one catalytic ion that seems to be less tightly bound at the site (PubMed:9784233).UniRule annotation1 Publication1 Publication

<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

Is totally inhibited by EDTA in vitro.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=1.43 mM for L-threonine (at 37 degrees Celsius and pH 8.4)1 Publication
  2. KM=0.19 mM for NAD+ (at 37 degrees Celsius and pH 8.4)1 Publication
  1. Vmax=57 µmol/min/mg enzyme for the NAD+ oxidation of L-threonine1 Publication

pH dependencei

Optimum pH is 10.3. At pH 9.0 and 11.0, the activity is 35% and only 6%, respectively, of the optimal level.1 Publication

<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-threonine degradation via oxydo-reductase pathway

This protein is involved in step 1 of the subpathway that synthesizes glycine from L-threonine.UniRule annotation 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%5Fsection">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 bindingi38Zinc 1; catalyticUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei40Charge relay systemUniRule annotation1
Active sitei43Charge relay systemUniRule annotation1
Metal bindingi63Zinc 1; via tele nitrogen; catalyticUniRule annotation1
Metal bindingi64Zinc 1; catalyticUniRule annotation1
Metal bindingi93Zinc 2UniRule annotation1
Metal bindingi96Zinc 2UniRule annotation1
Metal bindingi99Zinc 2UniRule annotation1
Metal bindingi107Zinc 2UniRule annotation1
<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>Sitei148Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atomUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei175NAD; via amide nitrogenUniRule annotation1
Binding sitei195NADUniRule annotation1
Binding sitei200NADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi262 – 264NADUniRule annotation3
Nucleotide bindingi286 – 287NADUniRule annotation2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • L-serine biosynthetic process Source: EcoliWiki
  • L-threonine catabolic process to glycine Source: UniProtKB-UniPathway
  • threonine catabolic process Source: EcoCyc
Complete GO annotation on QuickGO ...

<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
LigandCobalt, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:THREODEHYD-MONOMER
MetaCyc:THREODEHYD-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.103, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P07913

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%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:
L-threonine 3-dehydrogenaseUniRule annotation (EC:1.1.1.103UniRule annotation1 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%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:tdh1 Publication
Ordered Locus Names:b3616, JW3591
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <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
  • UP000000625 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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi38C → D: Shows only 1% of wild-type catalytic activity. This mutant can be stimulated to the wild-type activity level after incubation with Zn(+). 1 Publication1
Mutagenesisi38C → S: Loss of catalytic activity. This mutant cannot be stimulated to the wild-type activity level after incubation with Zn(+). 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001608371 – 341L-threonine 3-dehydrogenaseAdd BLAST341

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P07913

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

More...PaxDbi		P07913

PRoteomics IDEntifications database

More...PRIDEi		P07913

<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.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263307, 26 interactors
852446, 1 interactor

Database of interacting proteins

More...DIPi		DIP-6855N

Protein interaction database and analysis system

More...IntActi		P07913, 6 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3616

<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		P07913

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 zinc-containing alcohol dehydrogenase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1063, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026673_11_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07913

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07913

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%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.

P07913-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW 
        60         70         80         90        100
SQKTIPVPMV VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR 
       110        120        130        140        150
GGRTHLCRNT IGVGVNRPGC FAEYLVIPAF NAFKIPDNIS DDLAAIFDPF 
       160        170        180        190        200
GNAVHTALSF DLVGEDVLVS GAGPIGIMAA AVAKHVGARN VVITDVNEYR 
       210        220        230        240        250
LELARKMGIT RAVNVAKENL NDVMAELGMT EGFDVGLEMS GAPPAFRTML 
       260        270        280        290        300
DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA 
       310        320        330        340 
LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D
Length:341
Mass (Da):37,239
Last modified:November 1, 1988 - 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:i039FBD6B1CE8C2B2
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
X06690 Genomic DNA Translation: CAA29884.1
U00039 Genomic DNA Translation: AAB18593.1
U00096 Genomic DNA Translation: AAC76640.1
AP009048 Genomic DNA Translation: BAE77676.1

Protein sequence database of the Protein Information Resource

More...PIRi		A33276, DEECTH

NCBI Reference Sequences

More...RefSeqi		NP_418073.1, NC_000913.3
WP_000646007.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76640; AAC76640; b3616
BAE77676; BAE77676; BAE77676

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948139

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3591
eco:b3616

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3090

<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
X06690 Genomic DNA Translation: CAA29884.1
U00039 Genomic DNA Translation: AAB18593.1
U00096 Genomic DNA Translation: AAC76640.1
AP009048 Genomic DNA Translation: BAE77676.1
PIRiA33276, DEECTH
RefSeqiNP_418073.1, NC_000913.3
WP_000646007.1, NZ_LN832404.1

3D structure databases

SMRiP07913
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4263307, 26 interactors
852446, 1 interactor
DIPiDIP-6855N
IntActiP07913, 6 interactors
STRINGi511145.b3616

Proteomic databases

jPOSTiP07913
PaxDbiP07913
PRIDEiP07913

Genome annotation databases

EnsemblBacteriaiAAC76640; AAC76640; b3616
BAE77676; BAE77676; BAE77676
GeneIDi948139
KEGGiecj:JW3591
eco:b3616
PATRICifig|1411691.4.peg.3090

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0986

Phylogenomic databases

eggNOGiCOG1063, Bacteria
HOGENOMiCLU_026673_11_0_6
InParanoidiP07913
PhylomeDBiP07913

Enzyme and pathway databases

UniPathwayiUPA00046;UER00505
BioCyciEcoCyc:THREODEHYD-MONOMER
MetaCyc:THREODEHYD-MONOMER
BRENDAi1.1.1.103, 2026
SABIO-RKiP07913

Miscellaneous databases

Protein Ontology

More...PROi		PR:P07913

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

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_ECOLI
<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: P07913
Secondary accession number(s): Q2M7T0
<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: August 1, 1988
Last sequence update: November 1, 1988
Last modified: June 2, 2021
This is version 186 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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