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Protein

p-aminobenzoyl-glutamate hydrolase subunit A

Gene

abgA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p-aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified.2 Publications

Cofactori

Mn2+1 Publication

Kineticsi

  1. KM=60 µM for PABA-GLU (at pH 8.5)1 Publication

    GO - Molecular functioni

    • para-aminobenzoyl-glutamate hydrolase activity Source: UniProtKB
    • protein heterodimerization activity Source: EcoliWiki

    GO - Biological processi

    • folic acid catabolic process Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:G6670-MONOMER.
    ECOL316407:JW5205-MONOMER.
    MetaCyc:G6670-MONOMER.

    Protein family/group databases

    MEROPSiM20.020.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    p-aminobenzoyl-glutamate hydrolase subunit A (EC:3.5.1.-)
    Alternative name(s):
    PABA-GLU hydrolase
    Short name:
    PGH
    Gene namesi
    Name:abgA
    Synonyms:ydaJ
    Ordered Locus Names:b1338, JW5205
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13352. abgA.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436p-aminobenzoyl-glutamate hydrolase subunit APRO_0000061958Add
    BLAST

    Proteomic databases

    EPDiP77357.
    PaxDbiP77357.
    PRIDEiP77357.

    Expressioni

    Inductioni

    Could be transcriptionally regulated by AbgR.1 Publication

    Interactioni

    Subunit structurei

    Forms a heterodimer with AbgB.1 Publication

    GO - Molecular functioni

    • protein heterodimerization activity Source: EcoliWiki

    Protein-protein interaction databases

    BioGridi4261854. 1 interaction.
    IntActiP77357. 1 interaction.
    STRINGi511145.b1338.

    Structurei

    3D structure databases

    ProteinModelPortaliP77357.
    SMRiP77357. Positions 4-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M20 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CH2. Bacteria.
    COG1473. LUCA.
    HOGENOMiHOG000241405.
    InParanoidiP77357.
    KOiK12940.
    OMAiTKIDIRY.
    OrthoDBiEOG6BW4VH.
    PhylomeDBiP77357.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR017439. Amidohydrolase.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005962. Pept_M20D_amidohydro. 1 hit.
    SUPFAMiSSF55031. SSF55031. 1 hit.
    TIGRFAMsiTIGR01891. amidohydrolases. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P77357-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MESLNQFVNS LAPKLSHWRR DFHHYAESGW VEFRTATLVA EELHQLGYSL
    60 70 80 90 100
    ALGREVVNES SRMGLPDEFT LQREFERARQ QGALAQWIAA FEGGFTGIVA
    110 120 130 140 150
    TLDTGRPGPV MAFRVDMDAL DLSEEQDVSH RPYRDGFASC NAGMMHACGH
    160 170 180 190 200
    DGHTAIGLGL AHTLKQFESG LHGVIKLIFQ PAEEGTRGAR AMVDAGVVDD
    210 220 230 240 250
    VDYFTAVHIG TGVPAGTVVC GSDNFMATTK FDAHFTGTAA HAGAKPEDGH
    260 270 280 290 300
    NALLAAAQAT LALHAIAPHS EGASRVNVGV MQAGSGRNVV PASALLKVET
    310 320 330 340 350
    RGASDVINQY VFDRAQQAIQ GAATMYGVGV ETRLMGAATA SSPSPQWVAW
    360 370 380 390 400
    LQSQAAQVAG VNQAIERVEA PAGSEDATLM MARVQQHQGQ ASYVVFGTQL
    410 420 430
    AAGHHNEKFD FDEQVLAIAV ETLARTALNF PWTRGI
    Length:436
    Mass (Da):46,588
    Last modified:January 11, 2001 - v2
    Checksum:iCAA22D6925D61F56
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74420.2.
    AP009048 Genomic DNA. Translation: BAA14940.2.
    PIRiE64883.
    RefSeqiNP_415854.4. NC_000913.3.
    WP_000444929.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74420; AAC74420; b1338.
    BAA14940; BAA14940; BAA14940.
    GeneIDi945742.
    KEGGiecj:JW5205.
    eco:b1338.
    PATRICi32117952. VBIEscCol129921_1396.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74420.2.
    AP009048 Genomic DNA. Translation: BAA14940.2.
    PIRiE64883.
    RefSeqiNP_415854.4. NC_000913.3.
    WP_000444929.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP77357.
    SMRiP77357. Positions 4-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261854. 1 interaction.
    IntActiP77357. 1 interaction.
    STRINGi511145.b1338.

    Protein family/group databases

    MEROPSiM20.020.

    Proteomic databases

    EPDiP77357.
    PaxDbiP77357.
    PRIDEiP77357.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74420; AAC74420; b1338.
    BAA14940; BAA14940; BAA14940.
    GeneIDi945742.
    KEGGiecj:JW5205.
    eco:b1338.
    PATRICi32117952. VBIEscCol129921_1396.

    Organism-specific databases

    EchoBASEiEB3135.
    EcoGeneiEG13352. abgA.

    Phylogenomic databases

    eggNOGiENOG4105CH2. Bacteria.
    COG1473. LUCA.
    HOGENOMiHOG000241405.
    InParanoidiP77357.
    KOiK12940.
    OMAiTKIDIRY.
    OrthoDBiEOG6BW4VH.
    PhylomeDBiP77357.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6670-MONOMER.
    ECOL316407:JW5205-MONOMER.
    MetaCyc:G6670-MONOMER.

    Miscellaneous databases

    PROiP77357.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR017439. Amidohydrolase.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005962. Pept_M20D_amidohydro. 1 hit.
    SUPFAMiSSF55031. SSF55031. 1 hit.
    TIGRFAMsiTIGR01891. amidohydrolases. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Purification and characterization of the folate catabolic enzyme p-aminobenzoyl-glutamate hydrolase from Escherichia coli."
      Green J.M., Hollandsworth R., Pitstick L., Carter E.L.
      J. Bacteriol. 192:2407-2413(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION AS A PABA-GLU HYDROLASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR.
    5. "Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli."
      Hussein M.J., Green J.M., Nichols B.P.
      J. Bacteriol. 180:6260-6268(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "Escherichia coli abg genes enable uptake and cleavage of the folate catabolite p-aminobenzoyl-glutamate."
      Carter E.L., Jager L., Gardner L., Hall C.C., Willis S., Green J.M.
      J. Bacteriol. 189:3329-3334(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PABA-GLU HYDROLASE.

    Entry informationi

    Entry nameiABGA_ECOLI
    AccessioniPrimary (citable) accession number: P77357
    Secondary accession number(s): P76847
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 11, 2001
    Last modified: March 16, 2016
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. Peptidase families
      Classification of peptidase families and list of entries
    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.