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Protein

Phenol hydroxylase

Gene
N/A
Organism
Trichosporon cutaneum (Yeast) (Oidium cutaneum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydroxylates phenol to catechol (PubMed:1429434, PubMed:4146224, PubMed:3203745, PubMed:2022646, PubMed:7858421, PubMed:7851397, PubMed:11591156). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols (PubMed:4146224, PubMed:17425111, PubMed:7851397).8 Publications

Catalytic activityi

Phenol + NADPH + O2 = catechol + NADP+ + H2O.8 Publications

Cofactori

FAD3 Publications

Enzyme regulationi

Inhibited by excess phenol (PubMed:4146224). Heavy metals such AsCuSO4, AgNO3, or HgCl2 severely inhibit activity (PubMed:4146224).1 Publication

Kineticsi

  1. KM=18 µM for phenol1 Publication
  2. KM=71 µM for NADPH1 Publication
  3. KM=53 µM for O21 Publication

    pH dependencei

    Optimum pH is 7.2-7.6.2 Publications

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.1 Publication

    Pathwayi: phenol degradation

    This protein is involved in the pathway phenol degradation, which is part of Aromatic compound metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway phenol degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei55SubstrateCombined sources2 Publications1
    Binding sitei118FADCombined sources2 Publications1
    Binding sitei290FADCombined sources2 Publications1
    Binding sitei290SubstrateCombined sources2 Publications1
    Binding sitei358FADCombined sources1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi18 – 19FADCombined sources2 Publications2
    Nucleotide bindingi43 – 45FADCombined sources2 Publications3
    Nucleotide bindingi51 – 56FADCombined sources2 Publications6
    Nucleotide bindingi368 – 372FADCombined sources2 Publications5

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionMonooxygenase, Oxidoreductase
    Biological processAromatic hydrocarbons catabolism
    LigandFAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14669.
    UniPathwayiUPA00728.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenol hydroxylase1 Publication (EC:1.14.13.78 Publications)
    Short name:
    PHHY1 Publication
    OrganismiTrichosporon cutaneum (Yeast) (Oidium cutaneum)
    Taxonomic identifieri5554 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTrichosporonalesTrichosporonaceaeCutaneotrichosporon

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi55D → N: Leads to a significant slower initial step of the oxidative half-reaction. 1 Publication1
    Mutagenesisi282R → M: Leads to a significant slower initial step of the oxidative half-reaction. 1 Publication1
    Mutagenesisi290Y → F: Leads to a slightly higher redox potential but is reduced by NADPH much slower. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00002140452 – 665Phenol hydroxylaseAdd BLAST664

    Proteomic databases

    PRIDEiP15245.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1665
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 14Combined sources11
    Helixi18 – 33Combined sources16
    Beta strandi39 – 42Combined sources4
    Beta strandi44 – 47Combined sources4
    Helixi59 – 66Combined sources8
    Turni67 – 69Combined sources3
    Helixi71 – 75Combined sources5
    Beta strandi83 – 89Combined sources7
    Beta strandi95 – 104Combined sources10
    Helixi118 – 133Combined sources16
    Beta strandi142 – 150Combined sources9
    Helixi152 – 154Combined sources3
    Beta strandi163 – 169Combined sources7
    Helixi172 – 174Combined sources3
    Beta strandi186 – 188Combined sources3
    Helixi192 – 200Combined sources9
    Beta strandi214 – 224Combined sources11
    Helixi231 – 236Combined sources6
    Beta strandi241 – 257Combined sources17
    Turni261 – 264Combined sources4
    Beta strandi265 – 270Combined sources6
    Beta strandi272 – 274Combined sources3
    Beta strandi276 – 281Combined sources6
    Beta strandi287 – 293Combined sources7
    Turni305 – 307Combined sources3
    Helixi310 – 321Combined sources12
    Beta strandi327 – 343Combined sources17
    Beta strandi347 – 349Combined sources3
    Turni350 – 352Combined sources3
    Beta strandi353 – 355Combined sources3
    Helixi357 – 359Combined sources3
    Helixi370 – 389Combined sources20
    Helixi395 – 399Combined sources5
    Helixi400 – 424Combined sources25
    Beta strandi429 – 432Combined sources4
    Beta strandi435 – 437Combined sources3
    Helixi439 – 453Combined sources15
    Helixi473 – 475Combined sources3
    Beta strandi489 – 492Combined sources4
    Turni493 – 496Combined sources4
    Beta strandi497 – 500Combined sources4
    Helixi501 – 504Combined sources4
    Beta strandi511 – 518Combined sources8
    Helixi523 – 537Combined sources15
    Helixi542 – 546Combined sources5
    Beta strandi555 – 565Combined sources11
    Helixi572 – 574Combined sources3
    Turni577 – 580Combined sources4
    Beta strandi587 – 591Combined sources5
    Beta strandi596 – 598Combined sources3
    Helixi603 – 607Combined sources5
    Turni611 – 613Combined sources3
    Beta strandi615 – 619Combined sources5
    Beta strandi623 – 629Combined sources7
    Helixi634 – 642Combined sources9
    Beta strandi649 – 651Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FOHX-ray2.40A/B/C/D2-665[»]
    1PN0X-ray1.70A/B/C/D1-665[»]
    ProteinModelPortaliP15245.
    SMRiP15245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15245.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PheA/TfdB FAD monooxygenase family.Curated

    Phylogenomic databases

    KOiK03380.

    Family and domain databases

    InterProiView protein in InterPro
    IPR002938. FAD-bd.
    IPR023753. FAD/NAD-binding_dom.
    IPR012941. Phe_hydrox_C_dim_dom.
    IPR012336. Thioredoxin-like_fold.
    PfamiView protein in Pfam
    PF01494. FAD_binding_3. 1 hit.
    PF07976. Phe_hydrox_dim. 1 hit.
    SUPFAMiSSF51905. SSF51905. 2 hits.
    SSF52833. SSF52833. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15245-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTKYSESYCD VLIVGAGPAG LMAARVLSEY VRQKPDLKVR IIDKRSTKVY
    60 70 80 90 100
    NGQADGLQCR TLESLKNLGL ADKILSEAND MSTIALYNPD ENGHIRRTDR
    110 120 130 140 150
    IPDTLPGISR YHQVVLHQGR IERHILDSIA EISDTRIKVE RPLIPEKMEI
    160 170 180 190 200
    DSSKAEDPEA YPVTMTLRYM SDHESTPLQF GHKTENSLFH SNLQTQEEED
    210 220 230 240 250
    ANYRLPEGKE AGEIETVHCK YVIGCDGGHS WVRRTLGFEM IGEQTDYIWG
    260 270 280 290 300
    VLDAVPASNF PDIRSPCAIH SAESGSIMII PRENNLVRFY VQLQARAEKG
    310 320 330 340 350
    GRVDRTKFTP EVVIANAKKI FHPYTFDVQQ LDWFTAYHIG QRVTEKFSKD
    360 370 380 390 400
    ERVFIAGDAC HTHSPKAGQG MNTSMMDTYN LGWKLGLVLT GRAKRDILKT
    410 420 430 440 450
    YEEERHAFAQ ALIDFDHQFS RLFSGRPAKD VADEMGVSMD VFKEAFVKGN
    460 470 480 490 500
    EFASGTAINY DENLVTDKKS SKQELAKNCV VGTRFKSQPV VRHSEGLWMH
    510 520 530 540 550
    FGDRLVTDGR FRIIVFAGKA TDATQMSRIK KFSAYLDSEN SVISLYTPKV
    560 570 580 590 600
    SDRNSRIDVI TIHSCHRDDI EMHDFPAPAL HPKWQYDFIY ADCDSWHHPH
    610 620 630 640 650
    PKSYQAWGVD ETKGAVVVVR PDGYTSLVTD LEGTAEIDRY FSGILVEPKE
    660
    KSGAQTEADW TKSTA
    Length:665
    Mass (Da):75,162
    Last modified:January 23, 2007 - v3
    Checksum:i1401BE35D38BFB71
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L04488 mRNA. Translation: AAA34202.1.
    PIRiS07772.

    Genome annotation databases

    KEGGiag:AAA34202.

    Similar proteinsi

    Entry informationi

    Entry nameiPHHY_TRICU
    AccessioniPrimary (citable) accession number: P15245
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: September 27, 2017
    This is version 110 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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