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Protein

Phenol 2-monooxygenase

Gene
N/A
Organism
Trichosporon cutaneum (Yeast) (Oidium cutaneum)
Status
Reviewed-Annotation score: 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: phenol degradation

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 44FADSequence analysisAdd BLAST35
Nucleotide bindingi348 – 358FADSequence analysisAdd BLAST11

GO - Molecular functioni

GO - Biological processi

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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTrichosporonalesTrichosporonaceaeCutaneotrichosporon

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002140452 – 665Phenol 2-monooxygenaseAdd BLAST664

Proteomic databases

PRIDEiP15245.

Interactioni

Subunit structurei

Homodimer.

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

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR012941. Phe_hydrox_C_dim_dom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
PF07976. Phe_hydrox_dim. 1 hit.
[Graphical view]
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.

Cross-referencesi

Sequence databases

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

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...

Proteomic databases

PRIDEiP15245.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00728.
BioCyciMetaCyc:MONOMER-14669.

Miscellaneous databases

EvolutionaryTraceiP15245.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR012941. Phe_hydrox_C_dim_dom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
PF07976. Phe_hydrox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

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 30, 2016
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.