Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P9WQD1 (ACSA_MYCTU)

Entry version 31 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. M.tuberculosis may use AcsA for both acetate and propionate assimilation.UniRule annotation2 Publications

Miscellaneous

Could be also autoacetylated on Lys-617 in the presence of acetate as an acetyl donor and ATP. Autoacetylation is effectively inhibited by CoA. If CoA is not available or the concentration of CoA is low in vivo, the enzyme can transfer acetyl group from AcAMP to itself, resulting in autoacetylation and inactivation. When CoA is available, the acetyl group is donated to CoA forming AcCoA (PubMed:21896569).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

Mg2+UniRule annotation1 Publication, Ca2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication, Ni2+UniRule annotation1 Publication, Zn2+UniRule annotation1 PublicationNote: Magnesium, but can also use calcium, manganese, nickel or zinc ions.UniRule annotation1 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=0.35 mM for CoA (at pH 8 and at 37 degrees Celsius)1 Publication
  2. KM=1.2 mM for acetate (at pH 8 and at 37 degrees Celsius)1 Publication
  3. KM=2.1 mM for propionate (at pH 8 and at 37 degrees Celsius)1 Publication
  4. KM=5.6 mM for ATP (at pH 8 and at 37 degrees Celsius)1 Publication
  5. KM=509 mM for butyrate (at pH 8 and at 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is around 8. The enzyme is stable under neutral and alkaline conditions, while its activity decreases rapidly below pH 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. It lost its activity rapidly below 25 degrees Celsius or above 45 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei311Coenzyme AUniRule annotation1
    Binding sitei508ATPUniRule annotation1
    Binding sitei523ATPUniRule annotation1
    Binding sitei531Coenzyme A; via carbonyl oxygenUniRule annotation1
    Binding sitei534ATPUniRule annotation1
    <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 bindingi545Magnesium; via carbonyl oxygenUniRule annotation1
    Metal bindingi547Magnesium; via carbonyl oxygenUniRule annotation1
    Metal bindingi550Magnesium; via carbonyl oxygenUniRule annotation1

    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 bindingi387 – 389ATPUniRule annotation3
    Nucleotide bindingi411 – 416ATPUniRule annotation6

    <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

    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 functionLigase
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MTBH37RV:G185E-7950-MONOMER

    <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:
    Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
    Short name:
    AcCoA synthetaseUniRule annotation
    Short name:
    AcsUniRule annotation
    Alternative name(s):
    Acetate--CoA ligaseUniRule annotation
    Acyl-activating enzymeUniRule 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:acsAUniRule annotation
    Synonyms:acs
    Ordered Locus Names:Rv3667
    ORF Names:MTV025.015
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...    TubercuListi    		Rv3667

    <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

    Complete GO annotation on QuickGO ...

    <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>Mutagenesisi617K → R: Complete loss of acetyl-coenzyme A synthetase activity. 2 Publications1

    <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 methionineiRemovedCombined sources
    <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_00002083692 – 651Acetyl-coenzyme A synthetaseAdd BLAST650

    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 residuei2N-acetylserineCombined sources1
    Modified residuei617N6-acetyllysineUniRule annotation1 Publication1

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

    Acetylated on Lys-617 by Pat in the presence of acetyl-CoA as an acetyl donor and ATP. Acetylation results in the inactivation of the enzyme. Deacetylation by the SIR2-homolog deacetylase CobB is required to activate the enzyme.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

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

    More...    PaxDbi    		P9WQD1

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P9WQD1

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		83332.Rv3667

    <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    		P9WQD1

    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

    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>Regioni190 – 193Coenzyme A 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 ATP-dependent AMP-binding enzyme family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4108IQF Bacteria
    COG0365 LUCA

    KEGG Orthology (KO)

    More...    KOi    		K01895

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		DHWWHDL

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P9WQD1

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.12780, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01123 Ac_CoA_synth, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR011904 Ac_CoA_lig
    IPR032387 ACAS_N
    IPR025110 AMP-bd_C
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR042099 AMP-dep_Synthh-like_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF16177 ACAS_N, 1 hit
    PF00501 AMP-binding, 1 hit
    PF13193 AMP-binding_C, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR02188 Ac_CoA_lig_AcsA, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00455 AMP_BINDING, 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.

    P9WQD1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSESTPEVSS SYPPPAHFAE HANARAELYR EAEEDRLAFW AKQANRLSWT 
            60         70         80         90        100
    TPFTEVLDWS GAPFAKWFVG GELNVAYNCV DRHVEAGHGD RVAIHWEGEP 
           110        120        130        140        150
    VGDRRTLTYS DLLAEVSKAA NALTDLGLVA GDRVAIYLPL IPEAVIAMLA 
           160        170        180        190        200
    CARLGIMHSV VFGGFTAAAL QARIVDAQAK LLITADGQFR RGKPSPLKAA 
           210        220        230        240        250
    ADEALAAIPD CSVEHVLVVR RTGIEMAWSE GRDLWWHHVV GSASPAHTPE 
           260        270        280        290        300
    PFDSEHPLFL LYTSGTTGKP KGIMHTSGGY LTQCCYTMRT IFDVKPDSDV 
           310        320        330        340        350
    FWCTADIGWV TGHTYGVYGP LCNGVTEVLY EGTPDTPDRH RHFQIIEKYG 
           360        370        380        390        400
    VTIYYTAPTL IRMFMKWGRE IPDSHDLSSL RLLGSVGEPI NPEAWRWYRD 
           410        420        430        440        450
    VIGGGRTPLV DTWWQTETGS AMISPLPGIA AAKPGSAMTP LPGISAKIVD 
           460        470        480        490        500
    DHGDPLPPHT EGAQHVTGYL VLDQPWPSML RGIWGDPARY WHSYWSKFSD 
           510        520        530        540        550
    KGYYFAGDGA RIDPDGAIWV LGRIDDVMNV SGHRISTAEV ESALVAHSGV 
           560        570        580        590        600
    AEAAVVGVTD ETTTQAICAF VVLRANYAPH DRTAEELRTE VARVISPIAR 
           610        620        630        640        650
    PRDVHVVPEL PKTRSGKIMR RLLRDVAENR ELGDTSTLLD PTVFDAIRAA 

    K
    Length:651
    Mass (Da):71,476
    Last modified:April 16, 2014 - 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:i94290C0517A0445B
    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
    		AL123456 Genomic DNA Translation: CCP46490.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		D70789

    NCBI Reference Sequences

    More...    RefSeqi    		NP_218184.1, NC_000962.3
    WP_003899631.1, NZ_NVQJ01000028.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		CCP46490; CCP46490; Rv3667

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		885479

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mtu:Rv3667
    mtv:RVBD_3667

    <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
    		AL123456 Genomic DNA Translation: CCP46490.1
    PIRiD70789
    RefSeqiNP_218184.1, NC_000962.3
    WP_003899631.1, NZ_NVQJ01000028.1

    3D structure databases

    SMRiP9WQD1
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3667

    PTM databases

    iPTMnetiP9WQD1

    Proteomic databases

    PaxDbiP9WQD1

    Genome annotation databases

    EnsemblBacteriaiCCP46490; CCP46490; Rv3667
    GeneIDi885479
    KEGGimtu:Rv3667
    mtv:RVBD_3667

    Organism-specific databases

    TubercuListiRv3667

    Phylogenomic databases

    eggNOGiENOG4108IQF Bacteria
    COG0365 LUCA
    KOiK01895
    OMAiDHWWHDL
    PhylomeDBiP9WQD1

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-7950-MONOMER

    Family and domain databases

    Gene3Di3.40.50.12780, 1 hit
    HAMAPiMF_01123 Ac_CoA_synth, 1 hit
    InterProiView protein in InterPro
    IPR011904 Ac_CoA_lig
    IPR032387 ACAS_N
    IPR025110 AMP-bd_C
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR042099 AMP-dep_Synthh-like_sf
    PfamiView protein in Pfam
    PF16177 ACAS_N, 1 hit
    PF00501 AMP-binding, 1 hit
    PF13193 AMP-binding_C, 1 hit
    TIGRFAMsiTIGR02188 Ac_CoA_lig_AcsA, 1 hit
    PROSITEiView protein in PROSITE
    PS00455 AMP_BINDING, 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 nameiACSA_MYCTU
    <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: P9WQD1
    Secondary accession number(s): L0TGD8, O69635
    <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 16, 2014
    Last sequence update: April 16, 2014
    Last modified: September 18, 2019
    This is version 31 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    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