ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P15245

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PH2M_TRICU
Primary accession number P15245
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 70)
Name and origin of the protein
Protein name Phenol 2-monooxygenase
Synonyms EC 1.14.13.7
Phenol hydroxylase
Gene name None
From
Trichosporon cutaneum (Yeast) [TaxID: 5554] 
Taxonomy Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; Tremellales; Trichosporon.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 46490;
PubMed=1429434 [NCBI, ExPASy, EBI, Israel, Japan]
Kalin M., Neujahr H.Y., Weissmahr R.N., Sejlitz T., Johl R., Fiechter A., Reiser J.;
"Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli.";
J. Bacteriol. 174:7112-7120(1992).
[2]
 PROTEIN SEQUENCE OF 30-64; 299-311 AND 352-377.
STRAIN=ATCC 46490;
PubMed=2298204 [NCBI, ExPASy, EBI, Israel, Japan]
Sejlitz T., Wernstedt C., Engstroem A., Neujahr H.N.;
"Amino acid sequences around the pyridoxal-5'-phosphate-binding sites of phenol hydroxylase.";
Eur. J. Biochem. 187:225-228(1990).
[3]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
STRAIN=ATCC 46490;
DOI=10.1016/S0969-2126(98)00062-8; PubMed=9634698 [NCBI, ExPASy, EBI, Israel, Japan]
Enroth C., Neujahr H.Y., Schneider G., Lindqvist Y.;
"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.";
Structure 6:605-617(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L04488; AAA34202.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S07772; S07772.
3D structure databases
PDB
1FOH; X-ray; 2.40 A; A/B/C/D=1-665.[ExPASy / RCSB / EBI]
1PN0; X-ray; 1.70 A; A/B/C/D=1-665.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FOH; -.
1PN0; -.
ModBase P15245.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0018662; Molecular function: phenol 2-monooxygenase activity (inferred from electronic annotation from EC).
GO:0019439; Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002938; mOase_FAD_bd.
IPR012941; Phe_hydrox_C_dim.
IPR003042; Rng_hydrolase.
Graphical view of domain structure.
Pfam PF01494; FAD_binding_3; 1.
PF07976; Phe_hydrox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00420; RNGMNOXGNASE.
Other
LinkHub P15245; -.
ProtoNet P15245.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aromatic hydrocarbons catabolism; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   665  664     Phenol 2-monooxygenase. PRO_0000214045
NP_BIND   10    44  35     FAD (Potential). 
NP_BIND   348   358  11     FAD (Potential). 
STRAND   4    14  11      
HELIX   18    33  16      
STRAND   39    42  4      
STRAND   44    47  4      
HELIX   59    67  9      
HELIX   71    75  5      
STRAND   83    89  7      
STRAND   95   104  10      
HELIX   118   132  15      
TURN   133   135  3      
STRAND   142   150  9      
HELIX   152   154  3      
STRAND   163   169  7      
HELIX   172   174  3      
STRAND   186   188  3      
HELIX   192   200  9      
STRAND   214   224  11      
HELIX   231   236  6      
STRAND   241   258  18      
TURN   261   264  4      
STRAND   265   270  6      
STRAND   272   274  3      
STRAND   276   281  6      
STRAND   287   292  6      
HELIX   310   321  12      
STRAND   326   343  18      
STRAND   347   349  3      
TURN   350   352  3      
STRAND   353   355  3      
HELIX   357   359  3      
HELIX   370   389  20      
HELIX   395   398  4      
HELIX   399   424  26      
STRAND   429   432  4      
STRAND   435   437  3      
HELIX   439   453  15      
HELIX   473   475  3      
STRAND   489   492  4      
TURN   493   495  3      
STRAND   498   500  3      
HELIX   501   504  4      
STRAND   511   519  9      
HELIX   523   537  15      
HELIX   542   546  5      
STRAND   555   565  11      
HELIX   572   574  3      
TURN   577   580  4      
STRAND   587   591  5      
STRAND   596   598  3      
HELIX   603   607  5      
TURN   611   613  3      
STRAND   614   619  6      
STRAND   623   629  7      
HELIX   634   642  9      
STRAND   649   651  3      
Sequence information
Length: 665 AA [This is the length of the unprocessed precursor] Molecular weight: 75162 Da [This is the MW of the unprocessed precursor] CRC64: 1401BE35D38BFB71 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTKYSESYCD VLIVGAGPAG LMAARVLSEY VRQKPDLKVR IIDKRSTKVY NGQADGLQCR 

        70         80         90        100        110        120 
TLESLKNLGL ADKILSEAND MSTIALYNPD ENGHIRRTDR IPDTLPGISR YHQVVLHQGR 

       130        140        150        160        170        180 
IERHILDSIA EISDTRIKVE RPLIPEKMEI DSSKAEDPEA YPVTMTLRYM SDHESTPLQF 

       190        200        210        220        230        240 
GHKTENSLFH SNLQTQEEED ANYRLPEGKE AGEIETVHCK YVIGCDGGHS WVRRTLGFEM 

       250        260        270        280        290        300 
IGEQTDYIWG VLDAVPASNF PDIRSPCAIH SAESGSIMII PRENNLVRFY VQLQARAEKG 

       310        320        330        340        350        360 
GRVDRTKFTP EVVIANAKKI FHPYTFDVQQ LDWFTAYHIG QRVTEKFSKD ERVFIAGDAC 

       370        380        390        400        410        420 
HTHSPKAGQG MNTSMMDTYN LGWKLGLVLT GRAKRDILKT YEEERHAFAQ ALIDFDHQFS 

       430        440        450        460        470        480 
RLFSGRPAKD VADEMGVSMD VFKEAFVKGN EFASGTAINY DENLVTDKKS SKQELAKNCV 

       490        500        510        520        530        540 
VGTRFKSQPV VRHSEGLWMH FGDRLVTDGR FRIIVFAGKA TDATQMSRIK KFSAYLDSEN 

       550        560        570        580        590        600 
SVISLYTPKV SDRNSRIDVI TIHSCHRDDI EMHDFPAPAL HPKWQYDFIY ADCDSWHHPH 

       610        620        630        640        650        660 
PKSYQAWGVD ETKGAVVVVR PDGYTSLVTD LEGTAEIDRY FSGILVEPKE KSGAQTEADW 


TKSTA
P15245 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!