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Entry version 115 (02 Jun 2021)
Sequence version 1 (01 Jun 1998)
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Protein

Long-chain-fatty-acid--AMP ligase FadD32

Gene

fadD32

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

Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:19477415).

Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (PubMed:15042094, PubMed:19436070, PubMed:19477415, PubMed:27547819, PubMed:27590338).

Can use dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16) (PubMed:19182784, PubMed:19436070, PubMed:19477415, PubMed:23364516, PubMed:26900152, PubMed:27590338).

In vitro, displays a preference for long-chain over medium and short-chain fatty acid substrates (PubMed:19477415).

8 Publications

Miscellaneous

Was identified as a drug target (PubMed:23364516, PubMed:23798446, PubMed:30316633). Inhibited by a series of 4,6-diaryl-5,7-dimethyl coumarins that directly inhibit the acyl-acyl carrier protein synthetase activity of FadD32 and kill M.tuberculosis. They effectively block bacterial replication both in vitro and in animal models of tuberculosis (PubMed:23798446). Quinoline-2-carboxamides have also potent anti-tubercular activity (PubMed:30316633).3 Publications

<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 <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

Fatty acyl-AMP ligase activity and transferase activity onto Pks13 are both inhibited by phosphorylation (PubMed:27590338). The acyl-AMP ligase activity is inhibited by the alkylphosphate ester of AMP, adenosine 50-dodecylphosphate (AMPC12) (PubMed:19477415, PubMed:26900152). Also inhibited by eicosyl-AMP (AMPC20) (PubMed:26900152). Loading of the acyl-AMP onto Pks13 is inhibited by 5'-O-[N-(11-phenoxyundecanoyl)sulfamoyl]adenosine (PhU-AMS) (PubMed:27547819).4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.150 min(-1) with dodecanoate as substrate (PubMed:19477415). kcat is 2.04 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.123 min(-1) with tetradecanoate as substrate (PubMed:19477415). kcat is 0.98 min(-1) with tetradecanoate as substrate (PubMed:26900152). kcat is 0.015 min(-1) with hexadecanoate as sustrate (PubMed:19477415).2 Publications
  1. KM=2640 µM for dodecanoate1 Publication
  2. KM=72.09 µM for dodecanoate1 Publication
  3. KM=20.5 µM for tetradecanoate1 Publication
  4. KM=4.77 µM for tetradecanoate1 Publication
  5. KM=3.2 µM for hexadecanoate1 Publication
  6. KM=2020 µM for ATP1 Publication
  7. KM=248 µM for ATP1 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: mycolic acid biosynthesis

    This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.2 Publications
    View all proteins of this organism that are known to be involved in the pathway mycolic acid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei349ATP; via carbonyl oxygenBy similarity1
    Binding sitei353ATP; via amide nitrogenBy similarity1
    Binding sitei476ATPBy similarity1
    Binding sitei490ATPBy similarity1

    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 bindingi194 – 199ATPBy similarity6

    <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 functionLigase
    Biological processFatty acid metabolism, Lipid metabolism
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:G185E-8097-MONOMER

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

    More...
    UniPathwayi
    UPA00915

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000972

    <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:
    Long-chain-fatty-acid--AMP ligase FadD32Curated (EC:6.2.1.201 Publication)
    Short name:
    FAAL1 Publication
    Alternative name(s):
    Acyl-AMP synthetase
    FAAL321 Publication
    <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:fadD32
    Ordered Locus Names:Rv3801c
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv3801c

    <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

    <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>Mutagenesisi120E → A: Confers resistance to the coumarin inhibitors. 1 Publication1
    Mutagenesisi291F → L: Confers resistance to the coumarin inhibitors. 1 Publication1
    Mutagenesisi383F → A: Catalyzes the formation of acyl-CoA; when associated with A-481. 1 Publication1
    Mutagenesisi481F → A: Catalyzes the formation of acyl-CoA; when associated with A-383. 1 Publication1
    Mutagenesisi552T → D: Phosphomimetic mutant. 55% decrease in activity. 1 Publication1
    Mutagenesisi552T → V: Cannot be phosphorylated. No change in activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4295665

    <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_00004066341 – 637Long-chain-fatty-acid--AMP ligase FadD32Add BLAST637

    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 residuei552Phosphothreonine1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    Phosphorylated on Thr-552 by PknA, PknB, PknD and PknF. Dephosphorylated by PstP. Phosphorylation regulates activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

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

    More...
    PaxDbi
    O53580

    <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

    Monomer in solution.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv3801c

    <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

    1637
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    O53580

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0318, Bacteria

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O53580

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NGRNIWP

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O53580

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd05931, FAAL, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.12780, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000873, AMP-dep_Synth/Lig
    IPR042099, AMP-dep_Synthh-like_sf
    IPR040097, FAAL/FAAC

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00501, 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%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.

    O53580-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MFVTGESGMA YHNPFIVNGK IRFPANTNLV RHVEKWAKVR GDKLAYRFLD
    60 70 80 90 100
    FSTERDGVAR DILWSDFSAR NRAVGARLQQ VTQPGDRVAI LCPQNLDYLI
    110 120 130 140 150
    SFFGALYSGR IAVPLFDPAE PGHVGRLHAV LDDCAPSTIL TTTDSAEGVR
    160 170 180 190 200
    KFIRARSAKE RPRVIAVDAV PTEVAATWQQ PEANEETVAY LQYTSGSTRI
    210 220 230 240 250
    PSGVQITHLN LPTNVVQVLN ALEGQEGDRG VSWLPFFHDM GLITVLLASV
    260 270 280 290 300
    LGHSFTFMTP AAFVRRPGRW IRELARKPGE TGGTFSAAPN FAFEHAAVRG
    310 320 330 340 350
    VPRDDEPPLD LSNVKGILNG SEPVSPASMR KFFEAFAPYG LKQTAVKPSY
    360 370 380 390 400
    GLAEATLFVS TTPMDEVPTV IHVDRDELNN QRFVEVAADA PNAVAQVSAG
    410 420 430 440 450
    KVGVSEWAVI VDADTASELP DGQIGEIWLH GNNLGTGYWG KEEESAQTFK
    460 470 480 490 500
    NILKSRISES RAEGAPDDAL WVRTGDYGTY FKDHLYIAGR IKDLVIIDGR
    510 520 530 540 550
    NHYPQDLECT AQESTKALRV GYAAAFSVPA NQLPQTVFDD SHAGLKFDPE
    560 570 580 590 600
    DTSEQLVIVG ERAAGTHKLD HQPIVDDIRA AIAVGHGVTV RDVLLVSAGT
    610 620 630
    IPRTSSGKIG RRACRAAYLD GSLRSGVGSP TVFATSD
    Length:637
    Mass (Da):69,232
    Last modified:June 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:i0A3A86CED9AE0EDC
    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: CCP46630.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E70887

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_218318.1, NC_000962.3
    WP_003899700.1, NZ_NVQJ01000022.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    886130

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv3801c

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|83332.111.peg.4226

    <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: CCP46630.1
    PIRiE70887
    RefSeqiNP_218318.1, NC_000962.3
    WP_003899700.1, NZ_NVQJ01000022.1

    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
    5HM3X-ray2.25A2-637[»]
    SMRiO53580
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3801c

    Chemistry databases

    ChEMBLiCHEMBL4295665
    SwissLipidsiSLP:000000972

    Proteomic databases

    PaxDbiO53580

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    886130

    Genome annotation databases

    GeneIDi886130
    KEGGimtu:Rv3801c
    PATRICifig|83332.111.peg.4226

    Organism-specific databases

    TubercuListiRv3801c

    Phylogenomic databases

    eggNOGiCOG0318, Bacteria
    InParanoidiO53580
    OMAiNGRNIWP
    PhylomeDBiO53580

    Enzyme and pathway databases

    UniPathwayiUPA00915
    BioCyciMetaCyc:G185E-8097-MONOMER

    Family and domain databases

    CDDicd05931, FAAL, 1 hit
    Gene3Di3.40.50.12780, 1 hit
    InterProiView protein in InterPro
    IPR000873, AMP-dep_Synth/Lig
    IPR042099, AMP-dep_Synthh-like_sf
    IPR040097, FAAL/FAAC
    PfamiView protein in Pfam
    PF00501, AMP-binding, 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 nameiFAA32_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: O53580
    Secondary accession number(s): L0TGT1
    <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: April 5, 2011
    Last sequence update: June 1, 1998
    Last modified: June 2, 2021
    This is version 115 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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