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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-Experimental evidence at protein leveli

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

Catalytic activityi

Chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate.2 Publications

Cofactori

Mg2+1 Publication

Enzyme 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

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

    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 2 (pabA), Aminodeoxychorismate synthase component 1 (pabB)
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361Tryptophan1 Publication
    Active sitei258 – 2581Proton donor
    Active sitei274 – 2741N6-(4-deoxychorismate)-lysine intermediate

    GO - Molecular functioni

    • 4-amino-4-deoxychorismate synthase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • oxo-acid-lyase activity Source: InterPro

    GO - Biological processi

    • folic acid biosynthetic process Source: UniProtKB-KW
    • tetrahydrofolate biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Folate biosynthesis

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciEcoCyc:PABASYN-COMPI-MONOMER.
    ECOL316407:JW1801-MONOMER.
    MetaCyc:PABASYN-COMPI-MONOMER.
    BRENDAi2.6.1.85. 2026.
    SABIO-RKP05041.
    UniPathwayiUPA00077; UER00149.

    Names & Taxonomyi

    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
    Gene namesi
    Name:pabB
    Ordered Locus Names:b1812, JW1801
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10683. pabB.

    Pathology & Biotechi

    Disruption phenotypei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581E → A: The reaction is extremely slow. 1 Publication
    Mutagenesisi258 – 2581E → D: The reaction is extremely slow. 1 Publication
    Mutagenesisi274 – 2741K → 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 Publications
    Mutagenesisi274 – 2741K → R: Absence of covalent intermediate. 2 Publications
    Mutagenesisi274 – 2741K → R: Reduced catalytic efficiency. 2 Publications
    Mutagenesisi275 – 2751G → S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA. 1 Publication
    Mutagenesisi311 – 3111R → K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA. 1 Publication
    Mutagenesisi316 – 3161R → H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA. 1 Publication
    Mutagenesisi322 – 3221S → T: Complete loss of aminodeoxychorismate synthase activity. 1 Publication
    Mutagenesisi339 – 3391H → W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Aminodeoxychorismate synthase component 1PRO_0000154136Add
    BLAST

    Proteomic databases

    PaxDbiP05041.
    PRIDEiP05041.

    Interactioni

    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

    BioGridi4260345. 170 interactions.
    DIPiDIP-10434N.
    IntActiP05041. 6 interactions.
    STRINGi511145.b1812.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115Combined sources
    Helixi17 – 226Combined sources
    Turni23 – 275Combined sources
    Beta strandi32 – 354Combined sources
    Helixi42 – 443Combined sources
    Beta strandi46 – 505Combined sources
    Beta strandi54 – 607Combined sources
    Beta strandi63 – 686Combined sources
    Beta strandi71 – 755Combined sources
    Helixi79 – 8911Combined sources
    Beta strandi104 – 1107Combined sources
    Helixi112 – 1176Combined sources
    Beta strandi133 – 14614Combined sources
    Turni147 – 1504Combined sources
    Beta strandi151 – 1588Combined sources
    Helixi160 – 16910Combined sources
    Beta strandi185 – 1884Combined sources
    Helixi190 – 20516Combined sources
    Beta strandi212 – 22413Combined sources
    Helixi226 – 23712Combined sources
    Beta strandi241 – 2466Combined sources
    Beta strandi251 – 2566Combined sources
    Beta strandi261 – 2644Combined sources
    Beta strandi267 – 2704Combined sources
    Beta strandi273 – 2786Combined sources
    Turni297 – 3015Combined sources
    Helixi302 – 31413Combined sources
    Turni315 – 3173Combined sources
    Beta strandi324 – 33310Combined sources
    Beta strandi335 – 34713Combined sources
    Helixi354 – 3618Combined sources
    Helixi365 – 3673Combined sources
    Beta strandi369 – 3713Combined sources
    Helixi372 – 38211Combined sources
    Beta strandi383 – 3853Combined sources
    Turni388 – 3914Combined sources
    Beta strandi392 – 3987Combined sources
    Beta strandi403 – 4064Combined sources
    Beta strandi410 – 4156Combined sources
    Beta strandi418 – 42710Combined sources
    Helixi433 – 45119Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K0EX-ray2.00A/B1-453[»]
    1K0GX-ray2.05A/B1-453[»]
    ProteinModelPortaliP05041.
    SMRiP05041. Positions 3-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05041.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 464Tryptophan binding
    Regioni240 – 2423Tryptophan binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CRQ. Bacteria.
    COG0147. LUCA.
    HOGENOMiHOG000025142.
    InParanoidiP05041.
    KOiK01665.
    OMAiSHQPWAM.
    PhylomeDBiP05041.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR019999. Anth_synth_I-like.
    IPR006805. Anth_synth_I_N.
    IPR015890. Chorismate_C.
    IPR005802. Para-NH2Bz_synth_comp_1.
    [Graphical view]
    PfamiPF04715. Anth_synt_I_N. 1 hit.
    PF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    PRINTSiPR00095. ANTSNTHASEI.
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00553. pabB. 1 hit.

    Sequencei

    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
    Checksum:iDBF17DD5E17289D8
    GO

    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.

    Genome annotation databases

    EnsemblBacteriaiAAC74882; AAC74882; b1812.
    BAA15619; BAA15619; BAA15619.
    GeneIDi946337.
    KEGGiecj:JW1801.
    eco:b1812.
    PATRICi32118943. VBIEscCol129921_1889.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K0EX-ray2.00A/B1-453[»]
    1K0GX-ray2.05A/B1-453[»]
    ProteinModelPortaliP05041.
    SMRiP05041. Positions 3-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260345. 170 interactions.
    DIPiDIP-10434N.
    IntActiP05041. 6 interactions.
    STRINGi511145.b1812.

    Proteomic databases

    PaxDbiP05041.
    PRIDEiP05041.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74882; AAC74882; b1812.
    BAA15619; BAA15619; BAA15619.
    GeneIDi946337.
    KEGGiecj:JW1801.
    eco:b1812.
    PATRICi32118943. VBIEscCol129921_1889.

    Organism-specific databases

    EchoBASEiEB0677.
    EcoGeneiEG10683. pabB.

    Phylogenomic databases

    eggNOGiENOG4105CRQ. Bacteria.
    COG0147. LUCA.
    HOGENOMiHOG000025142.
    InParanoidiP05041.
    KOiK01665.
    OMAiSHQPWAM.
    PhylomeDBiP05041.

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00149.
    BioCyciEcoCyc:PABASYN-COMPI-MONOMER.
    ECOL316407:JW1801-MONOMER.
    MetaCyc:PABASYN-COMPI-MONOMER.
    BRENDAi2.6.1.85. 2026.
    SABIO-RKP05041.

    Miscellaneous databases

    EvolutionaryTraceiP05041.
    PROiP05041.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR019999. Anth_synth_I-like.
    IPR006805. Anth_synth_I_N.
    IPR015890. Chorismate_C.
    IPR005802. Para-NH2Bz_synth_comp_1.
    [Graphical view]
    PfamiPF04715. Anth_synt_I_N. 1 hit.
    PF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    PRINTSiPR00095. ANTSNTHASEI.
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00553. pabB. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPABB_ECOLI
    AccessioniPrimary (citable) accession number: P05041
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: September 7, 2016
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.