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P15245

- PH2M_TRICU

UniProt

P15245 - PH2M_TRICU

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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

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 – 4435FAD Reviewed prediction
Add
BLAST
Nucleotide bindingi348 – 35811FAD Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 665664Phenol 2-monooxygenase
PRO_0000214045Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP15245.

Family & Domainsi

Sequence similaritiesi

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 16, 2013
This is version 91 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

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