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Entry version 34 (08 May 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Pantothenate synthetase

Gene

panC

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 condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.1 Publication

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism.
Was identified as a high-confidence drug target.

<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

Pantothenate exhibits uncompetitive inhibition toward both D-pantoate and ATP, and non-competitive inhibition toward beta-alanine. AMPCPP exhibits competitive inhibition toward ATP, uncompetitive inhibition toward beta-alanine, and non-competitive inhibition toward D-pantoate. The enzyme is most active in the presence of magnesium or manganese. Other divalent cations (cobalt, nickel, zinc) are less effective.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=130 µM for D-pantoate2 Publications
  2. KM=800 µM for beta-alanine2 Publications
  3. KM=2600 µM for ATP2 Publications
  4. KM=25.4 mM for 2-mercaptoethylamine2 Publications
  5. KM=36 mM for carbamate2 Publications
  6. KM=72 mM for 5-aminovalerate2 Publications
  7. KM=79 mM for methylamine2 Publications
  8. KM=84 mM for glycine2 Publications
  9. KM=93 mM for ethylamine2 Publications
  10. KM=103 mM for taurine2 Publications
  11. KM=108 mM for glycolate2 Publications
  12. KM=335 mM for gamma-aminobutyrate2 Publications
  13. KM=580 mM for gamma-amino-beta-hydroxybutyrate2 Publications

    <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: (R)-pantothenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Pantothenate synthetase (panC)
    This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei47Proton donor1
    <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 sitei72Beta-alanine1
    Binding sitei72Pantoate1
    <p>This subsection of the ‘Function’ 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 bindingi88Magnesium1
    Metal bindingi89Magnesium; via amide nitrogen1
    Metal bindingi92Magnesium1
    Binding sitei164Pantoate1
    Binding sitei187ATP; via amide nitrogen and carbonyl oxygen1 Publication1

    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 bindingi40 – 47ATP1 Publication8
    Nucleotide bindingi158 – 161ATP1 Publication4
    Nucleotide bindingi195 – 198ATP1 Publication4

    <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 processPantothenate biosynthesis, Virulence
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MTBH37RV:G185E-7881-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.3.2.1 3445

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

    More...
    UniPathwayi
    UPA00028;UER00005

    <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:
    Pantothenate synthetase (EC:6.3.2.1)
    Short name:
    PS
    Alternative name(s):
    Pantoate--beta-alanine ligase
    Pantoate-activating enzyme
    <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:panC
    Ordered Locus Names:Rv3602c
    ORF Names:MTCY07H7B.20
    <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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium 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
    Rv3602c

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Subcutaneous immunization with the double panD and panC bacterial disruption mutant protects mice for over a year against subsequent virulent M.tuberculosis (strain Erdman) infections; mice show mild lung inflammation and fibrosis despite a chronic bacterila infection. This is a promising attenuated vaccine strain.1 Publication

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Simultaneous disruption of panD and panC gives a mutant unable to grow in the absence of panothenate. The double mutant has a highly attenuated disease response in BALB/c and SCID mice; immunocompromised BALB/c SCID mice survive on average 36 weeks as opposed to 5 weeks for mice infected with wild-type bacteria, while immunocompetent BALB/c mice survive indefinitely. In wild-type mice bacteria grow for 3 weeks then undergo a steady decline, bacteria persist over 8 months in SCID mice (PubMed:12219086). The double mutant is sensitive to PZA but not POA in liquid culture, beta-alanine but not pantothenate antagonize the effect of PZA at pH 5.8 (PubMed:25246400).2 Publications

    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>Mutagenesisi44H → A: More than 1000-fold reduction in activity and 52-fold decrease in adenylate formation. 1 Publication1
    Mutagenesisi47H → A: More than 1000-fold reduction in activity and 60-fold decrease in adenylate formation. 10-fold decrease in the affinity for ATP. 1 Publication1
    Mutagenesisi69N → A: More than 1000-fold reduction in activity and 50-fold decrease in adenylate formation. 1 Publication1
    Mutagenesisi72Q → A: More than 1000-fold reduction in activity and 45-fold decrease in adenylate formation. 1 Publication1
    Mutagenesisi77E → G: No effect. 1 Publication1
    Mutagenesisi160K → A: More than 1000-fold reduction in activity and 50-fold decrease in the affinity for ATP. 1 Publication1
    Mutagenesisi160K → C: More than 1000-fold reduction in activity and 120-fold decrease in adenylate formation. The enzymatic activity and the affinity for beta-alanine can be increased 10- and 3-fold, respectively, by alkylation of cysteine of mutant C-160. 1 Publication1
    Mutagenesisi164Q → A: 50-fold reduction in activity and slight reduction in the affinity for beta-alanine. 30- and 40-fold decrease in adenylate formation and pantothenate formation, respectively. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL6069

    <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 sources1 Publication
    <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_00001282452 – 309Pantothenate synthetaseAdd BLAST308

    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-acetylthreonineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

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

    More...
    PaxDbi
    P9WIL5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P9WIL5

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P9WIL5

    <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.Rv3602c

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P9WIL5

    <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

    1309
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1MOPX-ray1.60A/B3-300[»]
    1N2BX-ray1.70A/B3-300[»]
    1N2EX-ray1.60A/B3-300[»]
    1N2GX-ray1.80A/B3-300[»]
    1N2HX-ray2.00A/B3-300[»]
    1N2IX-ray1.70A/B3-300[»]
    1N2JX-ray1.80A/B3-300[»]
    1N2OX-ray2.10A/B3-300[»]
    2A7XX-ray1.70A3-300[»]
    2A84X-ray1.55A3-300[»]
    2A86X-ray1.85A/B3-300[»]
    2A88X-ray1.70A3-300[»]
    3COVX-ray1.50A/B3-300[»]
    3COWX-ray1.80A/B3-300[»]
    3COYX-ray2.03A/B3-300[»]
    3COZX-ray2.00A/B3-300[»]
    3IMCX-ray1.60A/B3-300[»]
    3IMEX-ray2.39A/B3-300[»]
    3IMGX-ray1.80A/B3-300[»]
    3IOBX-ray1.80A/B3-300[»]
    3IOCX-ray2.50A/B3-300[»]
    3IODX-ray1.75A/B3-300[»]
    3IOEX-ray1.95A/B3-300[»]
    3ISJX-ray2.20A/B3-300[»]
    3IUBX-ray1.50A/B3-301[»]
    3IUEX-ray1.73A/B3-301[»]
    3IVCX-ray2.13A/B3-301[»]
    3IVGX-ray1.95A/B3-301[»]
    3IVXX-ray1.73A/B3-301[»]
    3LE8X-ray1.70A/B3-300[»]
    4DDHX-ray2.07A/B3-301[»]
    4DDKX-ray1.75A/B3-301[»]
    4DDMX-ray1.83A/B3-301[»]
    4DE5X-ray2.25A/B3-301[»]
    4EF6X-ray1.94A/B3-300[»]
    4EFKX-ray1.70A/B3-300[»]
    4FZJX-ray1.63A/B3-301[»]
    4G5FX-ray2.33A/B3-309[»]
    4G5YX-ray1.80A/B3-300[»]

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

    More...
    SMRi
    P9WIL5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the pantothenate synthetase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108IAA Bacteria
    COG0414 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K01918

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FVNPSQF

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WIL5

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00560 PanC, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.620, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00158 PanC, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003721 Pantoate_ligase
    IPR014729 Rossmann-like_a/b/a_fold

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR21299:SF1 PTHR21299:SF1, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02569 Pantoate_ligase, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00018 panC, 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.

    <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.

    P9WIL5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTIPAFHPGE LNVYSAPGDV ADVSRALRLT GRRVMLVPTM GALHEGHLAL
    60 70 80 90 100
    VRAAKRVPGS VVVVSIFVNP MQFGAGEDLD AYPRTPDDDL AQLRAEGVEI
    110 120 130 140 150
    AFTPTTAAMY PDGLRTTVQP GPLAAELEGG PRPTHFAGVL TVVLKLLQIV
    160 170 180 190 200
    RPDRVFFGEK DYQQLVLIRQ LVADFNLDVA VVGVPTVREA DGLAMSSRNR
    210 220 230 240 250
    YLDPAQRAAA VALSAALTAA AHAATAGAQA ALDAARAVLD AAPGVAVDYL
    260 270 280 290 300
    ELRDIGLGPM PLNGSGRLLV AARLGTTRLL DNIAIEIGTF AGTDRPDGYR

    AILESHWRN
    Length:309
    Mass (Da):32,678
    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:iEB51DBE3485F970A
    GO

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 32545 Da from positions 2 - 309. Determined by ESI. 1 Publication

    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: CCP46425.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    C70955

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_218119.1, NC_000962.3
    WP_003419526.1, NZ_NVQJ01000056.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP46425; CCP46425; Rv3602c

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    885459

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv3602c
    mtv:RVBD_3602c

    <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: CCP46425.1
    PIRiC70955
    RefSeqiNP_218119.1, NC_000962.3
    WP_003419526.1, NZ_NVQJ01000056.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MOPX-ray1.60A/B3-300[»]
    1N2BX-ray1.70A/B3-300[»]
    1N2EX-ray1.60A/B3-300[»]
    1N2GX-ray1.80A/B3-300[»]
    1N2HX-ray2.00A/B3-300[»]
    1N2IX-ray1.70A/B3-300[»]
    1N2JX-ray1.80A/B3-300[»]
    1N2OX-ray2.10A/B3-300[»]
    2A7XX-ray1.70A3-300[»]
    2A84X-ray1.55A3-300[»]
    2A86X-ray1.85A/B3-300[»]
    2A88X-ray1.70A3-300[»]
    3COVX-ray1.50A/B3-300[»]
    3COWX-ray1.80A/B3-300[»]
    3COYX-ray2.03A/B3-300[»]
    3COZX-ray2.00A/B3-300[»]
    3IMCX-ray1.60A/B3-300[»]
    3IMEX-ray2.39A/B3-300[»]
    3IMGX-ray1.80A/B3-300[»]
    3IOBX-ray1.80A/B3-300[»]
    3IOCX-ray2.50A/B3-300[»]
    3IODX-ray1.75A/B3-300[»]
    3IOEX-ray1.95A/B3-300[»]
    3ISJX-ray2.20A/B3-300[»]
    3IUBX-ray1.50A/B3-301[»]
    3IUEX-ray1.73A/B3-301[»]
    3IVCX-ray2.13A/B3-301[»]
    3IVGX-ray1.95A/B3-301[»]
    3IVXX-ray1.73A/B3-301[»]
    3LE8X-ray1.70A/B3-300[»]
    4DDHX-ray2.07A/B3-301[»]
    4DDKX-ray1.75A/B3-301[»]
    4DDMX-ray1.83A/B3-301[»]
    4DE5X-ray2.25A/B3-301[»]
    4EF6X-ray1.94A/B3-300[»]
    4EFKX-ray1.70A/B3-300[»]
    4FZJX-ray1.63A/B3-301[»]
    4G5FX-ray2.33A/B3-309[»]
    4G5YX-ray1.80A/B3-300[»]
    SMRiP9WIL5
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3602c

    Chemistry databases

    BindingDBiP9WIL5
    ChEMBLiCHEMBL6069

    PTM databases

    iPTMnetiP9WIL5

    Proteomic databases

    PaxDbiP9WIL5
    PRIDEiP9WIL5

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP46425; CCP46425; Rv3602c
    GeneIDi885459
    KEGGimtu:Rv3602c
    mtv:RVBD_3602c

    Organism-specific databases

    TubercuListiRv3602c

    Phylogenomic databases

    eggNOGiENOG4108IAA Bacteria
    COG0414 LUCA
    KOiK01918
    OMAiFVNPSQF
    PhylomeDBiP9WIL5

    Enzyme and pathway databases

    UniPathwayi
    UPA00028;UER00005

    BioCyciMTBH37RV:G185E-7881-MONOMER
    BRENDAi6.3.2.1 3445

    Family and domain databases

    CDDicd00560 PanC, 1 hit
    Gene3Di3.40.50.620, 1 hit
    HAMAPiMF_00158 PanC, 1 hit
    InterProiView protein in InterPro
    IPR003721 Pantoate_ligase
    IPR014729 Rossmann-like_a/b/a_fold
    PANTHERiPTHR21299:SF1 PTHR21299:SF1, 1 hit
    PfamiView protein in Pfam
    PF02569 Pantoate_ligase, 1 hit
    TIGRFAMsiTIGR00018 panC, 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 nameiPANC_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: P9WIL5
    Secondary accession number(s): L0TG74, O06280, P0A5R0
    <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: May 8, 2019
    This is version 34 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, 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
    4. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
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