Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28305

- PABC_ECOLI

UniProt

P28305 - PABC_ECOLI

Protein

Aminodeoxychorismate lyase

Gene

pabC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.2 Publications

    Catalytic activityi

    4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate.1 Publication

    Cofactori

    Pyridoxal phosphate.3 Publications

    Pathwayi

    GO - Molecular functioni

    1. 4-amino-4-deoxychorismate lyase activity Source: UniProtKB
    2. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. folic acid biosynthetic process Source: UniProtKB-KW
    2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Folate biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:ADCLY-MONOMER.
    ECOL316407:JW1082-MONOMER.
    MetaCyc:ADCLY-MONOMER.
    BRENDAi4.1.3.38. 2026.
    UniPathwayiUPA00077; UER00150.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminodeoxychorismate lyase (EC:4.1.3.38)
    Alternative name(s):
    4-amino-4-deoxychorismate lyase
    Short name:
    ADC lyase
    Short name:
    ADCL
    Gene namesi
    Name:pabC
    Ordered Locus Names:b1096, JW1082
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11493. pabC.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to produce PABA.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 269269Aminodeoxychorismate lyasePRO_0000103305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei140 – 1401N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PRIDEiP28305.

    Expressioni

    Gene expression databases

    GenevestigatoriP28305.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    DIPiDIP-10435N.
    IntActiP28305. 8 interactions.
    STRINGi511145.b1096.

    Structurei

    Secondary structure

    1
    269
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43
    Beta strandi7 – 104
    Helixi17 – 215
    Beta strandi24 – 329
    Helixi39 – 5214
    Helixi60 – 7415
    Beta strandi76 – 849
    Beta strandi101 – 1077
    Helixi112 – 1198
    Beta strandi121 – 1255
    Turni134 – 1374
    Helixi145 – 15410
    Turni155 – 1584
    Beta strandi160 – 1667
    Beta strandi169 – 1735
    Beta strandi175 – 1839
    Beta strandi186 – 1905
    Beta strandi193 – 1975
    Helixi200 – 21112
    Beta strandi212 – 2198
    Helixi223 – 2275
    Beta strandi230 – 2356
    Beta strandi237 – 2393
    Beta strandi241 – 2477
    Helixi256 – 26611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ET0X-ray2.20A1-269[»]
    1I2KX-ray1.79A1-269[»]
    1I2LX-ray2.30A1-269[»]
    ProteinModelPortaliP28305.
    SMRiP28305. Positions 1-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28305.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0115.
    HOGENOMiHOG000276707.
    KOiK02619.
    OMAiIEGVYSN.
    OrthoDBiEOG67MF3R.
    PhylomeDBiP28305.

    Family and domain databases

    InterProiIPR017824. Aminodeoxychorismate_lyase_IV.
    IPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    [Graphical view]
    PANTHERiPTHR11825. PTHR11825. 1 hit.
    PfamiPF01063. Aminotran_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56752. SSF56752. 1 hit.
    TIGRFAMsiTIGR03461. pabC_Proteo. 1 hit.
    PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28305-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLINGHKQE SLAVSDRATQ FGDGCFTTAR VIDGKVSLLS AHIQRLQDAC    50
    QRLMISCDFW PQLEQEMKTL AAEQQNGVLK VVISRGSGGR GYSTLNSGPA 100
    TRILSVTAYP AHYDRLRNEG ITLALSPVRL GRNPHLAGIK HLNRLEQVLI 150
    RSHLEQTNAD EALVLDSEGW VTECCAANLF WRKGNVVYTP RLDQAGVNGI 200
    MRQFCIRLLA QSSYQLVEVQ ASLEESLQAD EMVICNALMP VMPVCACGDV 250
    SFSSATLYEY LAPLCERPN 269
    Length:269
    Mass (Da):29,715
    Last modified:December 1, 1992 - v1
    Checksum:i4BC186083F5E999E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93135 Genomic DNA. Translation: AAA24267.1.
    U00096 Genomic DNA. Translation: AAC74180.1.
    AP009048 Genomic DNA. Translation: BAA35904.1.
    PIRiA42954.
    RefSeqiNP_415614.1. NC_000913.3.
    YP_489364.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74180; AAC74180; b1096.
    BAA35904; BAA35904; BAA35904.
    GeneIDi12930426.
    946647.
    KEGGiecj:Y75_p1066.
    eco:b1096.
    PATRICi32117433. VBIEscCol129921_1139.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93135 Genomic DNA. Translation: AAA24267.1 .
    U00096 Genomic DNA. Translation: AAC74180.1 .
    AP009048 Genomic DNA. Translation: BAA35904.1 .
    PIRi A42954.
    RefSeqi NP_415614.1. NC_000913.3.
    YP_489364.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ET0 X-ray 2.20 A 1-269 [» ]
    1I2K X-ray 1.79 A 1-269 [» ]
    1I2L X-ray 2.30 A 1-269 [» ]
    ProteinModelPortali P28305.
    SMRi P28305. Positions 1-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10435N.
    IntActi P28305. 8 interactions.
    STRINGi 511145.b1096.

    Chemistry

    BindingDBi P28305.
    ChEMBLi CHEMBL1075099.

    Proteomic databases

    PRIDEi P28305.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74180 ; AAC74180 ; b1096 .
    BAA35904 ; BAA35904 ; BAA35904 .
    GeneIDi 12930426.
    946647.
    KEGGi ecj:Y75_p1066.
    eco:b1096.
    PATRICi 32117433. VBIEscCol129921_1139.

    Organism-specific databases

    EchoBASEi EB1456.
    EcoGenei EG11493. pabC.

    Phylogenomic databases

    eggNOGi COG0115.
    HOGENOMi HOG000276707.
    KOi K02619.
    OMAi IEGVYSN.
    OrthoDBi EOG67MF3R.
    PhylomeDBi P28305.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00150 .
    BioCyci EcoCyc:ADCLY-MONOMER.
    ECOL316407:JW1082-MONOMER.
    MetaCyc:ADCLY-MONOMER.
    BRENDAi 4.1.3.38. 2026.

    Miscellaneous databases

    EvolutionaryTracei P28305.
    PROi P28305.

    Gene expression databases

    Genevestigatori P28305.

    Family and domain databases

    InterProi IPR017824. Aminodeoxychorismate_lyase_IV.
    IPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    [Graphical view ]
    PANTHERi PTHR11825. PTHR11825. 1 hit.
    Pfami PF01063. Aminotran_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56752. SSF56752. 1 hit.
    TIGRFAMsi TIGR03461. pabC_Proteo. 1 hit.
    PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme."
      Green J.M., Merkel W.K., Nichols B.P.
      J. Bacteriol. 174:5317-5323(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, COFACTOR.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "p-aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC."
      Green J.M., Nichols B.P.
      J. Biol. Chem. 266:12971-12975(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21.
    6. "p-aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase."
      Ye Q.-Z., Liu J., Walsh C.T.
      Proc. Natl. Acad. Sci. U.S.A. 87:9391-9395(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    7. "Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli."
      Nakai T., Mizutani H., Miyahara I., Hirotsu K., Takeda S., Jhee K.-H., Yoshimura T., Esaki N.
      J. Biochem. 128:29-38(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.
    8. "Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes."
      Parsons J.F., Jensen P.Y., Pachikara A.S., Howard A.J., Eisenstein E., Ladner J.E.
      Biochemistry 41:2198-2208(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiPABC_ECOLI
    AccessioniPrimary (citable) accession number: P28305
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 120 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

    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

    External Data

    Dasty 3