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)

P15245

- PH2M_TRICU

UniProt

P15245 - PH2M_TRICU

Protein

Phenol 2-monooxygenase

Gene
N/A
Organism
Trichosporon cutaneum (Yeast) (Oidium cutaneum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Hydroxylates phenol to catechol. Phenol is the best substrate, but the enzyme also accepts simple hydroxyl-, amino-, halogen- or methyl-substituted phenols.

    Catalytic activityi

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

    Cofactori

    FAD.

    Enzyme regulationi

    Inhibited by excess phenol.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 4435FADSequence AnalysisAdd
    BLAST
    Nucleotide bindingi348 – 35811FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. phenol 2-monooxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. phenol-containing compound catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14669.
    UniPathwayiUPA00728.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenol 2-monooxygenase (EC:1.14.13.7)
    Alternative name(s):
    Phenol hydroxylase
    OrganismiTrichosporon cutaneum (Yeast) (Oidium cutaneum)
    Taxonomic identifieri5554 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesmitosporic TremellalesTrichosporon

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 665664Phenol 2-monooxygenasePRO_0000214045Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1411
    Helixi18 – 3316
    Beta strandi39 – 424
    Beta strandi44 – 474
    Helixi59 – 668
    Turni67 – 693
    Helixi71 – 755
    Beta strandi83 – 897
    Beta strandi95 – 10410
    Helixi118 – 13316
    Beta strandi142 – 1509
    Helixi152 – 1543
    Beta strandi163 – 1697
    Helixi172 – 1743
    Beta strandi186 – 1883
    Helixi192 – 2009
    Beta strandi214 – 22411
    Helixi231 – 2366
    Beta strandi241 – 25717
    Turni261 – 2644
    Beta strandi265 – 2706
    Beta strandi272 – 2743
    Beta strandi276 – 2816
    Beta strandi287 – 2937
    Helixi310 – 32112
    Beta strandi327 – 34317
    Beta strandi347 – 3493
    Turni350 – 3523
    Beta strandi353 – 3553
    Helixi357 – 3593
    Helixi370 – 38920
    Helixi395 – 3995
    Helixi400 – 42425
    Beta strandi429 – 4324
    Beta strandi435 – 4373
    Helixi439 – 45315
    Helixi473 – 4753
    Beta strandi489 – 4924
    Turni493 – 4964
    Beta strandi497 – 5004
    Helixi501 – 5044
    Beta strandi511 – 5188
    Helixi523 – 53715
    Helixi542 – 5465
    Beta strandi555 – 56511
    Helixi572 – 5743
    Turni577 – 5804
    Beta strandi587 – 5915
    Beta strandi596 – 5983
    Helixi603 – 6075
    Turni611 – 6133
    Beta strandi615 – 6195
    Beta strandi623 – 6297
    Helixi634 – 6429
    Beta strandi649 – 6513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FOHX-ray2.40A/B/C/D2-665[»]
    1PN0X-ray1.70A/B/C/D1-665[»]
    ProteinModelPortaliP15245.
    SMRiP15245. Positions 2-665.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15245.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PheA/TfdB FAD monooxygenase family.Curated

    Family and domain databases

    InterProiIPR002938. mOase_FAD-bd.
    IPR012941. Phe_hydrox_C_dim.
    IPR003042. Rng_hydrolase-like.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF01494. FAD_binding_3. 1 hit.
    PF07976. Phe_hydrox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00420. RNGMNOXGNASE.
    SUPFAMiSSF52833. 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

    MTKYSESYCD VLIVGAGPAG LMAARVLSEY VRQKPDLKVR IIDKRSTKVY    50
    NGQADGLQCR TLESLKNLGL ADKILSEAND MSTIALYNPD ENGHIRRTDR 100
    IPDTLPGISR YHQVVLHQGR IERHILDSIA EISDTRIKVE RPLIPEKMEI 150
    DSSKAEDPEA YPVTMTLRYM SDHESTPLQF GHKTENSLFH SNLQTQEEED 200
    ANYRLPEGKE AGEIETVHCK YVIGCDGGHS WVRRTLGFEM IGEQTDYIWG 250
    VLDAVPASNF PDIRSPCAIH SAESGSIMII PRENNLVRFY VQLQARAEKG 300
    GRVDRTKFTP EVVIANAKKI FHPYTFDVQQ LDWFTAYHIG QRVTEKFSKD 350
    ERVFIAGDAC HTHSPKAGQG MNTSMMDTYN LGWKLGLVLT GRAKRDILKT 400
    YEEERHAFAQ ALIDFDHQFS RLFSGRPAKD VADEMGVSMD VFKEAFVKGN 450
    EFASGTAINY DENLVTDKKS SKQELAKNCV VGTRFKSQPV VRHSEGLWMH 500
    FGDRLVTDGR FRIIVFAGKA TDATQMSRIK KFSAYLDSEN SVISLYTPKV 550
    SDRNSRIDVI TIHSCHRDDI EMHDFPAPAL HPKWQYDFIY ADCDSWHHPH 600
    PKSYQAWGVD ETKGAVVVVR PDGYTSLVTD LEGTAEIDRY FSGILVEPKE 650
    KSGAQTEADW TKSTA 665
    Length:665
    Mass (Da):75,162
    Last modified:January 23, 2007 - v3
    Checksum:i1401BE35D38BFB71
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04488 mRNA. Translation: AAA34202.1.
    PIRiS07772.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04488 mRNA. Translation: AAA34202.1 .
    PIRi S07772.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FOH X-ray 2.40 A/B/C/D 2-665 [» ]
    1PN0 X-ray 1.70 A/B/C/D 1-665 [» ]
    ProteinModelPortali P15245.
    SMRi P15245. Positions 2-665.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00728 .
    BioCyci MetaCyc:MONOMER-14669.

    Miscellaneous databases

    EvolutionaryTracei P15245.

    Family and domain databases

    InterProi IPR002938. mOase_FAD-bd.
    IPR012941. Phe_hydrox_C_dim.
    IPR003042. Rng_hydrolase-like.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF01494. FAD_binding_3. 1 hit.
    PF07976. Phe_hydrox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00420. RNGMNOXGNASE.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli."
      Kalin M., Neujahr H.Y., Weissmahr R.N., Sejlitz T., Johl R., Fiechter A., Reiser J.
      J. Bacteriol. 174:7112-7120(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 46490.
    2. "Amino acid sequences around the pyridoxal-5'-phosphate-binding sites of phenol hydroxylase."
      Sejlitz T., Wernstedt C., Engstroem A., Neujahr H.N.
      Eur. J. Biochem. 187:225-228(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-64; 299-311 AND 352-377.
      Strain: ATCC 46490.
    3. "The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis."
      Enroth C., Neujahr H.Y., Schneider G., Lindqvist Y.
      Structure 6:605-617(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
      Strain: ATCC 46490.

    Entry informationi

    Entry nameiPH2M_TRICU
    AccessioniPrimary (citable) accession number: P15245
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 92 of the entry and version 3 of the sequence. [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

    External Data

    Dasty 3