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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 conversion of lactate to pyruvate. It is stereospecific for L+-lactate.UniRule annotation1 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 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

Allosterically activated by fructose 1,6-bisphosphate (FBP). Inactivated by Mn2+, Co2+, Cd2+ and Zn2+.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=30 µM for NADH (at 55 degrees Celsius and in the absence of fructose 1,6-bisphosphate (FBP))1 Publication
  2. KM=60 µM for pyruvate (at 55 degrees Celsius and in the presence of fructose 1,6-bisphosphate (FBP))1 Publication
  3. KM=90 µM for NAD+ (at 55 degrees Celsius and in the absence of fructose 1,6-bisphosphate (FBP))1 Publication
  4. KM=3.7 mM for pyruvate (at 55 degrees Celsius and in the absence of fructose 1,6-bisphosphate (FBP))1 Publication
  5. KM=25 mM for L+-lactate (at 55 degrees Celsius and in the presence of fructose 1,6-bisphosphate (FBP))1 Publication
  6. KM=410 mM for L+-lactate (at 55 degrees Celsius and in the absence of fructose 1,6-bisphosphate (FBP))1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    Long-term stability up to 80 degrees Celsius. Fructose 1,6-bisphosphate (FBP) increases the thermal stability at 90 degrees Celsius (pH 6.0).1 Publication

    <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: pyruvate fermentation to lactate

    This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh)
    This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei32NADUniRule annotationCombined sources1 Publication1
    Binding sitei37NADUniRule annotation1
    Binding sitei62NADUniRule annotation1
    Binding sitei79SubstrateUniRule annotation1
    Binding sitei85SubstrateUniRule annotation1
    Binding sitei140NADUniRule annotation1
    Binding sitei150Allosteric activatorUniRule annotation1
    Binding sitei165Allosteric activatorUniRule annotationCombined sources1 Publication1
    <p>This subsection of the ‘Function’ 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 sitei172Proton acceptorUniRule annotation1 Publication1
    Binding sitei226SubstrateUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi10 – 11NADCombined sources1 Publication2
    Nucleotide bindingi76 – 77NADUniRule annotation2
    Nucleotide bindingi115 – 117NADUniRule annotation3

    <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 functionAllosteric enzyme, Oxidoreductase
    LigandNAD

    Enzyme and pathway databases

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

    More...
    UniPathwayi
    UPA00554;UER00611

    <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-lactate dehydrogenase1 PublicationUniRule annotation (EC:1.1.1.27UniRule annotation1 Publication)
    Short name:
    L-LDH1 PublicationUniRule annotation
    <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:ldh1 PublicationUniRule annotation
    Ordered Locus Names:TM_1867
    <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>OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    <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 identifieri243274 [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 lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    <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
    • UP000008183 <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

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03940 Oxamic Acid

    <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_00001684061 – 319L-lactate dehydrogenaseAdd BLAST319

    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 residuei217PhosphotyrosineUniRule annotation1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P16115

    <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

    Homotetramer.UniRule annotation2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243274.TM1867

    <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

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P16115

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

    More...
    SMRi
    P16115

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P16115

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni117 – 120Substrate bindingUniRule annotation4
    Regioni145 – 148Substrate bindingUniRule annotation4

    <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 LDH/MDH superfamily. LDH family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C80 Bacteria
    COG0039 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P16115

    KEGG Orthology (KO)

    More...
    KOi
    K00016

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RQPGQTR

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.90.110.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00488 Lactate_dehydrog, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001557 L-lactate/malate_DH
    IPR011304 L-lactate_DH
    IPR018177 L-lactate_DH_AS
    IPR022383 Lactate/malate_DH_C
    IPR001236 Lactate/malate_DH_N
    IPR015955 Lactate_DH/Glyco_Ohase_4_C
    IPR036291 NAD(P)-bd_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02866 Ldh_1_C, 1 hit
    PF00056 Ldh_1_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000102 Lac_mal_DH, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00086 LLDHDRGNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit
    SSF56327 SSF56327, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01771 L-LDH-NAD, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00064 L_LDH, 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>.<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.

    P16115-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKIGIVGLGR VGSSTAFALL MKGFAREMVL IDVDKKRAEG DALDLIHGTP
    60 70 80 90 100
    FTRRANIYAG DYADLKGSDV VIVAAGVPQK PGETRLQLLG RNARVMKEIA
    110 120 130 140 150
    RNVSKYAPDS IVIVVTNPVD VLTYFFLKES GMDPRKVFGS GTVLDTARLR
    160 170 180 190 200
    TLIAQHCGFS PRSVHVYVIG EHGDSEVPVW SGAMIGGIPL QNMCQICQKC
    210 220 230 240 250
    DSKILENFAE KTKRAAYEII ERKGATHYAI ALAVADIVES IFFDEKRVLT
    260 270 280 290 300
    LSVYLEDYLG VKDLCISVPV TLGKHGVERI LELNLNEEEL EAFRKSASIL
    310
    KNAINEITAE ENKHQNTSG
    Length:319
    Mass (Da):34,994
    Last modified:June 1, 1994 - v2
    <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:iA1FB9B97CDCF290B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti14Missing AA sequence (PubMed:2318202).Curated1

    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
    X74302 Genomic DNA Translation: CAA52355.1
    AE000512 Genomic DNA Translation: AAD36929.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S36863

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_229663.1, NC_000853.1
    WP_004082418.1, NZ_CP011107.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAD36929; AAD36929; TM_1867

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    29653701
    897800

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tma:TM1867

    <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
    X74302 Genomic DNA Translation: CAA52355.1
    AE000512 Genomic DNA Translation: AAD36929.1
    PIRiS36863
    RefSeqiNP_229663.1, NC_000853.1
    WP_004082418.1, NZ_CP011107.1

    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
    1A5ZX-ray2.10A1-319[»]
    ProteinModelPortaliP16115
    SMRiP16115
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM1867

    Chemistry databases

    DrugBankiDB03940 Oxamic Acid

    Proteomic databases

    PRIDEiP16115

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD36929; AAD36929; TM_1867
    GeneIDi29653701
    897800
    KEGGitma:TM1867

    Phylogenomic databases

    eggNOGiENOG4105C80 Bacteria
    COG0039 LUCA
    InParanoidiP16115
    KOiK00016
    OMAiRQPGQTR

    Enzyme and pathway databases

    UniPathwayi
    UPA00554;UER00611

    Miscellaneous databases

    EvolutionaryTraceiP16115

    Family and domain databases

    Gene3Di3.90.110.10, 1 hit
    HAMAPiMF_00488 Lactate_dehydrog, 1 hit
    InterProiView protein in InterPro
    IPR001557 L-lactate/malate_DH
    IPR011304 L-lactate_DH
    IPR018177 L-lactate_DH_AS
    IPR022383 Lactate/malate_DH_C
    IPR001236 Lactate/malate_DH_N
    IPR015955 Lactate_DH/Glyco_Ohase_4_C
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF02866 Ldh_1_C, 1 hit
    PF00056 Ldh_1_N, 1 hit
    PIRSFiPIRSF000102 Lac_mal_DH, 1 hit
    PRINTSiPR00086 LLDHDRGNASE
    SUPFAMiSSF51735 SSF51735, 1 hit
    SSF56327 SSF56327, 1 hit
    TIGRFAMsiTIGR01771 L-LDH-NAD, 1 hit
    PROSITEiView protein in PROSITE
    PS00064 L_LDH, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiLDH_THEMA
    <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: P16115
    <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: April 1, 1990
    Last sequence update: June 1, 1994
    Last modified: December 5, 2018
    This is version 154 of the entry and version 2 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, Direct protein sequencing, Reference 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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