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P20586

- PHHY_PSEAE

UniProt

P20586 - PHHY_PSEAE

Protein

p-hydroxybenzoate hydroxylase

Gene

pobA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    4-hydroxybenzoate + NADPH + O2 = protocatechuate + NADP+ + H2O.

    Cofactori

    FAD.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 3229FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. 4-hydroxybenzoate 3-monooxygenase activity Source: UniProtKB-EC
    2. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

    1. benzoate catabolic process via hydroxylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    UniPathwayiUPA00156; UER00257.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    p-hydroxybenzoate hydroxylase (EC:1.14.13.2)
    Short name:
    PHBH
    Alternative name(s):
    4-hydroxybenzoate 3-monooxygenase
    Gene namesi
    Name:pobA
    Ordered Locus Names:PA0247
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA0247.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394p-hydroxybenzoate hydroxylasePRO_0000058381Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi208964.PA0247.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi12 – 2413
    Beta strandi28 – 314
    Helixi36 – 405
    Beta strandi47 – 493
    Helixi50 – 589
    Helixi63 – 686
    Beta strandi70 – 734
    Beta strandi75 – 795
    Beta strandi82 – 865
    Helixi88 – 925
    Beta strandi97 – 993
    Helixi102 – 11514
    Beta strandi119 – 1235
    Beta strandi125 – 1306
    Beta strandi134 – 1363
    Beta strandi138 – 1436
    Beta strandi146 – 1516
    Beta strandi153 – 1575
    Helixi166 – 1683
    Helixi171 – 1733
    Beta strandi175 – 19218
    Beta strandi195 – 1984
    Beta strandi200 – 2023
    Beta strandi209 – 2157
    Beta strandi218 – 2258
    Helixi231 – 2333
    Helixi236 – 24510
    Helixi249 – 2546
    Beta strandi260 – 27415
    Beta strandi276 – 2783
    Beta strandi281 – 2833
    Helixi285 – 2873
    Helixi293 – 2953
    Helixi298 – 31922
    Helixi322 – 3276
    Helixi328 – 35023
    Helixi358 – 37316
    Helixi375 – 38511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D7LX-ray2.20A1-394[»]
    1DOBX-ray2.00A1-394[»]
    1DOCX-ray2.00A1-394[»]
    1DODX-ray2.10A1-394[»]
    1DOEX-ray2.30A1-394[»]
    1IUSX-ray2.20A1-394[»]
    1IUTX-ray2.00A1-394[»]
    1IUUX-ray2.00A1-394[»]
    1IUVX-ray2.50A1-394[»]
    1IUWX-ray2.00A1-394[»]
    1IUXX-ray2.00A1-394[»]
    1K0IX-ray1.80A1-394[»]
    1K0JX-ray2.20A1-394[»]
    1K0LX-ray2.00A1-394[»]
    1PXAX-ray2.30A1-394[»]
    1PXBX-ray2.30A1-394[»]
    1PXCX-ray2.10A1-394[»]
    1YKJX-ray2.00A/B1-394[»]
    ProteinModelPortaliP20586.
    SMRiP20586. Positions 1-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20586.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG0654.
    HOGENOMiHOG000221233.
    KOiK00481.
    OMAiLAEWSDA.
    OrthoDBiEOG6PS5RW.
    PhylomeDBiP20586.

    Family and domain databases

    InterProiIPR012733. HB_mOase.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    [Graphical view]
    PfamiPF01494. FAD_binding_3. 1 hit.
    [Graphical view]
    PRINTSiPR00420. RNGMNOXGNASE.
    TIGRFAMsiTIGR02360. pbenz_hydroxyl. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P20586-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ    50
    GMVDLLREAG VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY 100
    GQTEVTRDLM EAREACGATT VYQAAEVRLH DLQGERPYVT FERDGERLRL 150
    DCDYIAGCDG FHGISRQSIP AERLKVFERV YPFGWLGLLA DTPPVSHELI 200
    YANHPRGFAL CSQRSATRSR YYVQVPLSEK VEDWSDERFW TELKARLPSE 250
    VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN 300
    LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL 350
    HRFPDTDAFS QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE 394
    Length:394
    Mass (Da):44,324
    Last modified:February 1, 1991 - v1
    Checksum:i1E7232854D9EC792
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23173 Genomic DNA. Translation: AAA88455.1.
    AE004091 Genomic DNA. Translation: AAG03636.1.
    PIRiJT0384. WHPSBA.
    RefSeqiNP_248938.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG03636; AAG03636; PA0247.
    GeneIDi882128.
    KEGGipae:PA0247.
    PATRICi19834710. VBIPseAer58763_0257.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23173 Genomic DNA. Translation: AAA88455.1 .
    AE004091 Genomic DNA. Translation: AAG03636.1 .
    PIRi JT0384. WHPSBA.
    RefSeqi NP_248938.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D7L X-ray 2.20 A 1-394 [» ]
    1DOB X-ray 2.00 A 1-394 [» ]
    1DOC X-ray 2.00 A 1-394 [» ]
    1DOD X-ray 2.10 A 1-394 [» ]
    1DOE X-ray 2.30 A 1-394 [» ]
    1IUS X-ray 2.20 A 1-394 [» ]
    1IUT X-ray 2.00 A 1-394 [» ]
    1IUU X-ray 2.00 A 1-394 [» ]
    1IUV X-ray 2.50 A 1-394 [» ]
    1IUW X-ray 2.00 A 1-394 [» ]
    1IUX X-ray 2.00 A 1-394 [» ]
    1K0I X-ray 1.80 A 1-394 [» ]
    1K0J X-ray 2.20 A 1-394 [» ]
    1K0L X-ray 2.00 A 1-394 [» ]
    1PXA X-ray 2.30 A 1-394 [» ]
    1PXB X-ray 2.30 A 1-394 [» ]
    1PXC X-ray 2.10 A 1-394 [» ]
    1YKJ X-ray 2.00 A/B 1-394 [» ]
    ProteinModelPortali P20586.
    SMRi P20586. Positions 1-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA0247.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG03636 ; AAG03636 ; PA0247 .
    GeneIDi 882128.
    KEGGi pae:PA0247.
    PATRICi 19834710. VBIPseAer58763_0257.

    Organism-specific databases

    PseudoCAPi PA0247.

    Phylogenomic databases

    eggNOGi COG0654.
    HOGENOMi HOG000221233.
    KOi K00481.
    OMAi LAEWSDA.
    OrthoDBi EOG6PS5RW.
    PhylomeDBi P20586.

    Enzyme and pathway databases

    UniPathwayi UPA00156 ; UER00257 .

    Miscellaneous databases

    EvolutionaryTracei P20586.

    Family and domain databases

    InterProi IPR012733. HB_mOase.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    [Graphical view ]
    Pfami PF01494. FAD_binding_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00420. RNGMNOXGNASE.
    TIGRFAMsi TIGR02360. pbenz_hydroxyl. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa."
      Entsch B., Nan Y., Weaich K., Scott K.F.
      Gene 71:279-291(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    4. "pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis."
      Gatti D.L., Entsch B., Ballou D.P., Ludwig M.L.
      Biochemistry 35:567-578(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    5. "Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants."
      Lah M.S., Palfey B.A., Schreuder H.A., Ludwig M.L.
      Biochemistry 33:1555-1564(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS.

    Entry informationi

    Entry nameiPHHY_PSEAE
    AccessioniPrimary (citable) accession number: P20586
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 108 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3