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Protein

Aminodeoxychorismate synthase component 2

Gene

pabA

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. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by 6-diazo-5-oxo-L-norleucine (DON). The inhibition is competitive with glutamine, but uncompetitive with chorismate.1 Publication

Kineticsi

  1. KM=4.2 µM for chorismate (with the heterodimer PabA-PabB and glutamine as the amino donor at pH 7.5)1 Publication
  2. KM=18.6 µM for chorismate (with the heterodimer PabA-PabB and ammonia as the amino donor at pH 7.5)1 Publication

    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
    Active sitei79 – 7911 Publication
    Active sitei168 – 16811 Publication
    Active sitei170 – 17011 Publication

    GO - Molecular functioni

    • 4-amino-4-deoxychorismate synthase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Folate biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:PABASYN-COMPII-MONOMER.
    ECOL316407:JW3323-MONOMER.
    MetaCyc:PABASYN-COMPII-MONOMER.
    SABIO-RKP00903.
    UniPathwayiUPA00077; UER00149.

    Protein family/group databases

    MEROPSiC26.955.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminodeoxychorismate synthase component 2 (EC:2.6.1.85)
    Short name:
    ADC synthase
    Short name:
    ADCS
    Alternative name(s):
    4-amino-4-deoxychorismate synthase component 2
    Aminodeoxychorismate synthase, glutamine amidotransferase component
    Gene namesi
    Name:pabA
    Ordered Locus Names:b3360, JW3323
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10682. pabA.

    Pathology & Biotechi

    Disruption phenotypei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791C → S: 10000-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi168 – 1681H → Q: Loss of activity. 1 Publication
    Mutagenesisi170 – 1701E → A: 150-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi170 – 1701E → D: 4-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi170 – 1701E → K or Q: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 187187Aminodeoxychorismate synthase component 2PRO_0000056849Add
    BLAST

    Proteomic databases

    PaxDbiP00903.

    Interactioni

    Subunit structurei

    Monomer. Heterodimer consisting of two non-identical subunits: a glutamine amidotransferase subunit (PabA) and a aminodeoxychorismate synthase subunit (PabB).1 Publication

    Protein-protein interaction databases

    BioGridi4262475. 89 interactions.
    DIPiDIP-10433N.
    IntActiP00903. 6 interactions.
    STRINGi511145.b3360.

    Structurei

    3D structure databases

    ProteinModelPortaliP00903.
    SMRiP00903. Positions 1-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 187187Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4105DDQ. Bacteria.
    COG0512. LUCA.
    HOGENOMiHOG000025029.
    InParanoidiP00903.
    KOiK01664.
    OMAiPCSPDEA.
    OrthoDBiEOG6D5G6B.
    PhylomeDBiP00903.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR006221. TrpG/PapA_dom.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00903-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MILLIDNYDS FTWNLYQYFC ELGADVLVKR NDALTLADID ALKPQKIVIS
    60 70 80 90 100
    PGPCTPDEAG ISLDVIRHYA GRLPILGVCL GHQAMAQAFG GKVVRAAKVM
    110 120 130 140 150
    HGKTSPITHN GEGVFRGLAN PLTVTRYHSL VVEPDSLPAC FDVTAWSETR
    160 170 180
    EIMGIRHRQW DLEGVQFHPE SILSEQGHQL LANFLHR
    Length:187
    Mass (Da):20,772
    Last modified:July 21, 1986 - v1
    Checksum:i0E5F43499D5F55C6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M28363 Genomic DNA. Translation: AAA23774.1.
    K00030 Genomic DNA. Translation: AAA24260.1.
    M32354 Genomic DNA. Translation: AAA24264.1.
    U18997 Genomic DNA. Translation: AAA58157.1.
    U00096 Genomic DNA. Translation: AAC76385.1.
    AP009048 Genomic DNA. Translation: BAE77930.1.
    PIRiA01124. AGEC2.
    RefSeqiNP_417819.1. NC_000913.3.
    WP_000601847.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76385; AAC76385; b3360.
    BAE77930; BAE77930; BAE77930.
    GeneIDi947873.
    KEGGiecj:JW3323.
    eco:b3360.
    PATRICi32122154. VBIEscCol129921_3454.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M28363 Genomic DNA. Translation: AAA23774.1.
    K00030 Genomic DNA. Translation: AAA24260.1.
    M32354 Genomic DNA. Translation: AAA24264.1.
    U18997 Genomic DNA. Translation: AAA58157.1.
    U00096 Genomic DNA. Translation: AAC76385.1.
    AP009048 Genomic DNA. Translation: BAE77930.1.
    PIRiA01124. AGEC2.
    RefSeqiNP_417819.1. NC_000913.3.
    WP_000601847.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP00903.
    SMRiP00903. Positions 1-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262475. 89 interactions.
    DIPiDIP-10433N.
    IntActiP00903. 6 interactions.
    STRINGi511145.b3360.

    Protein family/group databases

    MEROPSiC26.955.

    Proteomic databases

    PaxDbiP00903.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76385; AAC76385; b3360.
    BAE77930; BAE77930; BAE77930.
    GeneIDi947873.
    KEGGiecj:JW3323.
    eco:b3360.
    PATRICi32122154. VBIEscCol129921_3454.

    Organism-specific databases

    EchoBASEiEB0676.
    EcoGeneiEG10682. pabA.

    Phylogenomic databases

    eggNOGiENOG4105DDQ. Bacteria.
    COG0512. LUCA.
    HOGENOMiHOG000025029.
    InParanoidiP00903.
    KOiK01664.
    OMAiPCSPDEA.
    OrthoDBiEOG6D5G6B.
    PhylomeDBiP00903.

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00149.
    BioCyciEcoCyc:PABASYN-COMPII-MONOMER.
    ECOL316407:JW3323-MONOMER.
    MetaCyc:PABASYN-COMPII-MONOMER.
    SABIO-RKP00903.

    Miscellaneous databases

    PROiP00903.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR006221. TrpG/PapA_dom.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence of Escherichia coli pabA and its evolutionary relationship to trp(G)D."
      Kaplan J.B., Nichols B.P.
      J. Mol. Biol. 168:451-468(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Chromosomal organization and expression of Escherichia coli pabA."
      Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.
      J. Bacteriol. 172:397-410(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli."
      Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T.
      J. Bacteriol. 171:4525-4529(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
    6. "Biosynthesis of 4-aminobenzoate in Escherichia coli."
      Huang M., Gibson F.
      J. Bacteriol. 102:767-773(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, NOMENCLATURE.
    7. "p-aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA."
      Roux B., Walsh C.T.
      Biochemistry 32:3763-3768(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-79; HIS-168 AND GLU-170, ACTIVE SITE.
    8. "Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli."
      Viswanathan V.K., Green J.M., Nichols B.P.
      J. Bacteriol. 177:5918-5923(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    9. "Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations affecting catalysis and subunit association."
      Rayl E.A., Green J.M., Nichols B.P.
      Biochim. Biophys. Acta 1295:81-88(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.

    Entry informationi

    Entry nameiPABA_ECOLI
    AccessioniPrimary (citable) accession number: P00903
    Secondary accession number(s): Q2M726
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: April 13, 2016
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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. 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.