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Entry version 164 (17 Jun 2020)
Sequence version 1 (13 Aug 1987)
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Protein

Aminodeoxychorismate synthase component 1

Gene

pabB

Organism
Escherichia coli (strain K12)
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

Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia.3 Publications

Miscellaneous

In this enzymatic reaction the C4 hydroxy group of chorismate is replaced by addition of a nucleophile at the C2 position. The nucleophile is the epsilon-amino group of lysine 274 transiently binds to C2 of chorismate (PubMed:16605270). PabB contains a tryptophan (Trp) molecule deeply embedded in a binding pocket. Trp which cannot be dissociated without denaturation of PabB, may play a structural role in the enzyme since it has no effect on the enzymic synthesis of aminodeoxychorismate (PubMed:11841211).2 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 '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+1 Publication

<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

Inhibited by 6-diazo-5-oxo-L-norleucine (DON). The inhibition is competitive with glutamine but uncompetitive with chorismate. Also inhibited by 2-fluorochorismate.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

  1. KM=4.2 µM for chorismate (with PabA and glutamine as the amino donor at pH 7.5)3 Publications
  2. KM=18.6 µM for chorismate (with PabA and ammonia as the amino donor at pH 7.5)3 Publications
  3. KM=71 µM for chorismate3 Publications
  4. KM=75 µM for chorismate (with PabA)3 Publications
  5. KM=379 µM for chorismate (with PabA and ammonia)3 Publications
  6. KM=388 µM for chorismate (with ammonia)3 Publications

    <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: tetrahydrofolate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 4-aminobenzoate from chorismate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Aminodeoxychorismate synthase component 1 (pabB), Aminodeoxychorismate synthase component 2 (pabA)
    2. Aminodeoxychorismate lyase (pabC)
    This subpathway is part of the pathway tetrahydrofolate 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 4-aminobenzoate from chorismate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

    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 sitei36Tryptophan1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei258Proton donor1
    Active sitei274N6-(4-deoxychorismate)-lysine intermediate1

    <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 functionTransferase
    Biological processFolate biosynthesis
    LigandMagnesium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:PABASYN-COMPI-MONOMER
    ECOL316407:JW1801-MONOMER
    MetaCyc:PABASYN-COMPI-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.6.1.85 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P05041

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

    More...
    UniPathwayi
    UPA00077;UER00149

    <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:
    Aminodeoxychorismate synthase component 1 (EC:2.6.1.85)
    Short name:
    ADC synthase
    Short name:
    ADCS
    Alternative name(s):
    4-amino-4-deoxychorismate synthase component 1
    <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:pabB
    Ordered Locus Names:b1812, JW1801
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    <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 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

    Cells lacking this gene do not produce 4-aminobenzoate.1 Publication

    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>Mutagenesisi258E → A: The reaction is extremely slow. 1 Publication1
    Mutagenesisi258E → D: The reaction is extremely slow. 1 Publication1
    Mutagenesisi274K → A: Absence of covalent intermediate. Addition of ammonia allows the formation of the covalent intermediate and shows that ammonia can replace the function of K-274. Reduced catalytic efficiency. 2 Publications1
    Mutagenesisi274K → R: Absence of covalent intermediate. 2 Publications1
    Mutagenesisi274K → R: Reduced catalytic efficiency. 2 Publications1
    Mutagenesisi275G → S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA. 1 Publication1
    Mutagenesisi311R → K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA. 1 Publication1
    Mutagenesisi316R → H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA. 1 Publication1
    Mutagenesisi322S → T: Complete loss of aminodeoxychorismate synthase activity. 1 Publication1
    Mutagenesisi339H → W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB01942 Formic acid

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001541361 – 453Aminodeoxychorismate synthase component 1Add BLAST453

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P05041

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

    More...
    PaxDbi
    P05041

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P05041

    <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. Heterodimer consisting of two non-identical subunits: a glutamine amidotransferase subunit (PabA) and a aminodeoxychorismate synthase subunit (PabB).

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4260345, 170 interactors
    850694, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-10434N

    Protein interaction database and analysis system

    More...
    IntActi
    P05041, 6 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1812

    <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

    1453
    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
    P05041

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P05041

    <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>Regioni43 – 46Tryptophan binding4
    Regioni240 – 242Tryptophan binding3

    <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
    ENOG4105CRQ Bacteria
    COG0147 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_006493_7_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P05041

    KEGG Orthology (KO)

    More...
    KOi
    K01665

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P05041

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.60.120.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005802 ADC_synth_comp_1
    IPR005801 ADC_synthase
    IPR019999 Anth_synth_I-like
    IPR006805 Anth_synth_I_N
    IPR015890 Chorismate_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04715 Anth_synt_I_N, 1 hit
    PF00425 Chorismate_bind, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00095 ANTSNTHASEI

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56322 SSF56322, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00553 pabB, 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.

    P05041-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTLSPAVIT LLWRQDAAEF YFSRLSHLPW AMLLHSGYAD HPYSRFDIVV
    60 70 80 90 100
    AEPICTLTTF GKETVVSESE KRTTTTDDPL QVLQQVLDRA DIRPTHNEDL
    110 120 130 140 150
    PFQGGALGLF GYDLGRRFES LPEIAEQDIV LPDMAVGIYD WALIVDHQRH
    160 170 180 190 200
    TVSLLSHNDV NARRAWLESQ QFSPQEDFTL TSDWQSNMTR EQYGEKFRQV
    210 220 230 240 250
    QEYLHSGDCY QVNLAQRFHA TYSGDEWQAF LQLNQANRAP FSAFLRLEQG
    260 270 280 290 300
    AILSLSPERF ILCDNSEIQT RPIKGTLPRL PDPQEDSKQA VKLANSAKDR
    310 320 330 340 350
    AENLMIVDLM RNDIGRVAVA GSVKVPELFV VEPFPAVHHL VSTITAQLPE
    360 370 380 390 400
    QLHASDLLRA AFPGGSITGA PKVRAMEIID ELEPQRRNAW CGSIGYLSFC
    410 420 430 440 450
    GNMDTSITIR TLTAINGQIF CSAGGGIVAD SQEEAEYQET FDKVNRILKQ

    LEK
    Length:453
    Mass (Da):50,970
    Last modified:August 13, 1987 - 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:iDBF17DD5E17289D8
    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
    K02673 Genomic DNA Translation: AAA24266.1
    U00096 Genomic DNA Translation: AAC74882.1
    AP009048 Genomic DNA Translation: BAA15619.1
    U07762 Genomic DNA Translation: AAC43282.1
    U07748 Genomic DNA Translation: AAC43269.1
    U07749 Genomic DNA Translation: AAC43270.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A30251 AGEC1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416326.1, NC_000913.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74882; AAC74882; b1812
    BAA15619; BAA15619; BAA15619

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946337

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1801
    eco:b1812

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|511145.12.peg.1889

    <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
    K02673 Genomic DNA Translation: AAA24266.1
    U00096 Genomic DNA Translation: AAC74882.1
    AP009048 Genomic DNA Translation: BAA15619.1
    U07762 Genomic DNA Translation: AAC43282.1
    U07748 Genomic DNA Translation: AAC43269.1
    U07749 Genomic DNA Translation: AAC43270.1
    PIRiA30251 AGEC1
    RefSeqiNP_416326.1, NC_000913.3

    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
    1K0EX-ray2.00A/B1-453[»]
    1K0GX-ray2.05A/B1-453[»]
    SMRiP05041
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260345, 170 interactors
    850694, 1 interactor
    DIPiDIP-10434N
    IntActiP05041, 6 interactors
    STRINGi511145.b1812

    Chemistry databases

    DrugBankiDB01942 Formic acid

    Proteomic databases

    jPOSTiP05041
    PaxDbiP05041
    PRIDEiP05041

    Genome annotation databases

    EnsemblBacteriaiAAC74882; AAC74882; b1812
    BAA15619; BAA15619; BAA15619
    GeneIDi946337
    KEGGiecj:JW1801
    eco:b1812
    PATRICifig|511145.12.peg.1889

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0677

    Phylogenomic databases

    eggNOGiENOG4105CRQ Bacteria
    COG0147 LUCA
    HOGENOMiCLU_006493_7_2_6
    InParanoidiP05041
    KOiK01665
    PhylomeDBiP05041

    Enzyme and pathway databases

    UniPathwayiUPA00077;UER00149
    BioCyciEcoCyc:PABASYN-COMPI-MONOMER
    ECOL316407:JW1801-MONOMER
    MetaCyc:PABASYN-COMPI-MONOMER
    BRENDAi2.6.1.85 2026
    SABIO-RKiP05041

    Miscellaneous databases

    EvolutionaryTraceiP05041

    Protein Ontology

    More...
    PROi
    PR:P05041

    Family and domain databases

    Gene3Di3.60.120.10, 1 hit
    InterProiView protein in InterPro
    IPR005802 ADC_synth_comp_1
    IPR005801 ADC_synthase
    IPR019999 Anth_synth_I-like
    IPR006805 Anth_synth_I_N
    IPR015890 Chorismate_C
    PfamiView protein in Pfam
    PF04715 Anth_synt_I_N, 1 hit
    PF00425 Chorismate_bind, 1 hit
    PRINTSiPR00095 ANTSNTHASEI
    SUPFAMiSSF56322 SSF56322, 1 hit
    TIGRFAMsiTIGR00553 pabB, 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 nameiPABB_ECOLI
    <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: P05041
    <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: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: June 17, 2020
    This is version 164 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, Direct protein sequencing, 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
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