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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

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
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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04488 mRNA. Translation: AAA34202.1 .
PIRi S07772.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 94 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