Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 99 (02 Jun 2021)
Sequence version 1 (09 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

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

Gene

fadD32

Organism
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
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 (By similarity).

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 (By similarity).

Can use decanoate (C10), dodecanoate (C12) and tetradecanoate (C14) (PubMed:23364516, PubMed:26900152).

By similarity2 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

The acyl-AMP ligase activity is inhibited by the alkylphosphate ester of AMP, adenosine 50-dodecylphosphate (AMPC12) (PubMed:23364516, PubMed:26900152). Also inhibited by eicosyl-AMP (AMPC20) (PubMed:26900152).2 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 16.1 min(-1) with decanoate as substrate (PubMed:23364516). kcat is 11.2 min(-1) with dodecanoate as substrate (PubMed:23364516). kcat is 4.2 min(-1) with tetradecanoate as substrate (PubMed:23364516).1 Publication
  1. KM=259.0 µM for decanoate1 Publication
  2. KM=25.9 µM for dodecanoate1 Publication
  3. KM=5.2 µM for tetradecanoate1 Publication
  4. KM=76.0 µM for ATP1 Publication
  5. KM=112 µM for ATP1 Publication

    pH dependencei

    Optimum pH is 7.5.1 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: mycolic acid biosynthesis

    This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.By similarity
    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 sitei342ATP; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei346ATP; via amide nitrogenCombined sources1 Publication1
    Binding sitei469ATPCombined sources1 Publication1
    Binding sitei483ATPCombined sources1 Publication1

    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 bindingi187 – 192ATPCombined sources1 Publication6

    <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
    MSME246196:G1H7P-6360-MONOMER

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

    More...
    UniPathwayi
    UPA00915

    <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:6.2.1.20By similarity)
    Short name:
    FAALCurated
    Alternative name(s):
    Acyl-AMP synthetaseCurated
    <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:fadD32Imported
    Ordered Locus Names:MSMEG_6393Imported, MSMEI_6225Imported
    <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>OrganismiMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
    <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 identifieri246196 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
    <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
    • UP000006158 <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
    • UP000000757 Componenti: Chromosome

    <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_00004514631 – 630Long-chain-fatty-acid--AMP ligase FadD32Add BLAST630

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    A0R618

    <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.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    246196.MSMEI_6225

    <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

    1630
    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
    A0R618

    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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Consists of two globular domains connected by a flexible linker. ATP binds in a cleft at the interface between the N- and C-terminal domains and its binding induces significant local conformational changes.1 Publication

    <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

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NGRNIWP

    Database of Orthologous Groups

    More...
    OrthoDBi
    572620at2

    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.

    A0R618-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPFHNPFIKD GQIKFPDGSS IVAHVERWAK VRGDKLAYRF LDFSTERDGV
    60 70 80 90 100
    PRDLTWAQFS ARNRAVAARL QQVTQPGDRV AILCPQNLDY LVAFFGALYA
    110 120 130 140 150
    GRIAVPLFDP SEPGHVGRLH AVLDNCHPSA ILTTTEAAEG VRKFFRTRPA
    160 170 180 190 200
    NQRPRVIAVD AVPDDVASTW VNPDEPDETT IAYLQYTSGS TRIPTGVQIT
    210 220 230 240 250
    HLNLATNVVQ VIEALEGEEG DRGLSWLPFF HDMGLITALL APMIGHYFTF
    260 270 280 290 300
    MTPAAFVRRP ERWIRELARK EGDTGGTISV APNFAFDHAA ARGVPKPGSP
    310 320 330 340 350
    PLDLSNVKAV LNGSEPISAA TVRRFNEAFG PFGFPPKAIK PSYGLAEATL
    360 370 380 390 400
    FVSTTPSAEE PKIITVDRDQ LNSGRIVEVD ADSPKAVAQA SAGKVGIAEW
    410 420 430 440 450
    AVIVDAESAT ELPDGQVGEI WISGQNMGTG YWGKPEESVA TFQNILKSRT
    460 470 480 490 500
    NPSHAEGATD DATWVRTGDY GAFYDGDLYI TGRVKDLVII DGRNHYPQDL
    510 520 530 540 550
    EYSAQEASKA IRTGYVAAFS VPANQLPDEV FENAHSGIKR DPDDTSEQLV
    560 570 580 590 600
    IVAERAPGAH KLDIGPITDD IRAAIAVRHG VTVRDVLLTA AGAIPRTSSG
    610 620 630
    KIGRRACRAA YLDGSLRAGK VANDFPDATD
    Length:630
    Mass (Da):68,229
    Last modified:January 9, 2007 - 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:i71627AEAD5FA8772
    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
    CP000480 Genomic DNA Translation: ABK74035.1
    CP001663 Genomic DNA Translation: AFP42651.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011731257.1, NZ_SIJM01000013.1
    YP_890606.1, NC_008596.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABK74035; ABK74035; MSMEG_6393
    AFP42651; AFP42651; MSMEI_6225

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    msg:MSMEI_6225
    msm:MSMEG_6393

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|246196.19.peg.6220

    <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
    CP000480 Genomic DNA Translation: ABK74035.1
    CP001663 Genomic DNA Translation: AFP42651.1
    RefSeqiWP_011731257.1, NZ_SIJM01000013.1
    YP_890606.1, NC_008596.1

    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
    5D6JX-ray2.25A1-630[»]
    5D6NX-ray2.40A1-484[»]
    5EY8X-ray3.50A/B/C/D/E/F/G/H1-630[»]
    5ICRX-ray2.25A/B/C/D1-630[»]
    SMRiA0R618
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEI_6225

    Proteomic databases

    PRIDEiA0R618

    Genome annotation databases

    EnsemblBacteriaiABK74035; ABK74035; MSMEG_6393
    AFP42651; AFP42651; MSMEI_6225
    KEGGimsg:MSMEI_6225
    msm:MSMEG_6393
    PATRICifig|246196.19.peg.6220

    Phylogenomic databases

    eggNOGiCOG0318, Bacteria
    OMAiNGRNIWP
    OrthoDBi572620at2

    Enzyme and pathway databases

    UniPathwayiUPA00915
    BioCyciMSME246196:G1H7P-6360-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_MYCS2
    <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: A0R618
    Secondary accession number(s): I7GFQ6
    <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: December 2, 2020
    Last sequence update: January 9, 2007
    Last modified: June 2, 2021
    This is version 99 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
    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