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UniProtKB/Swiss-Prot entry P47233


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

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Entry information
Entry name BPHC3_RHOGO
Primary accession number P47233
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 47)
Name and origin of the protein
Protein name Biphenyl-2,3-diol 1,2-dioxygenase 3
Synonyms EC 1.13.11.39
Biphenyl-2,3-diol 1,2-dioxygenase III
23OHBP oxygenase III
2,3-dihydroxybiphenyl dioxygenase III
DHBD III
Gene name
Name: bphC3
From
Rhodococcus globerulus [TaxID: 33008] 
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Nocardiaceae; Rhodococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=P6;
PubMed=8126007 [NCBI, ExPASy, EBI, Israel, Japan]
Asturias J.A., Eltis L.D., Prucha M., Timmis K.N.;
"Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases.";
J. Biol. Chem. 269:7807-7815(1994).
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
X75635; CAA53299.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D53419; D53419.
3D structure databases
HSSP O05205; 1KMZ. [HSSP ENTRY / PDB]
ModBase P47233.
Ontologies
GO
GO:0018583; Molecular function: biphenyl-2,3-diol 1,2-dioxygenase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR004360; Glyas_bleo-R_dOase.
IPR000486; Xdiol_dOase_1_2.
Graphical view of domain structure.
Pfam PF00903; Glyoxalase; 1.
Pfam graphical view of domain structure.
ProDom PD002334; Gly_diox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00082; EXTRADIOL_DIOXYGENAS; 1.
BLOCKS P47233.
Other
ProtoNet P47233.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   190  189     Biphenyl-2,3-diol 1,2-dioxygenase 3. PRO_0000085039
METAL   9     9        Iron (By similarity). 
METAL   73    73        Iron (By similarity). 
METAL   121   121        Iron (By similarity). 
Sequence information
Length: 190 AA [This is the length of the unprocessed precursor] Molecular weight: 21191 Da [This is the MW of the unprocessed precursor] CRC64: 5CA026ED8D13C7E2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVTPRLAHF VLQTNQLPAM TQWYIDVLGA HVVYENPAMC FLTTDEEHHR VALFGPPGGG 

        70         80         90        100        110        120 
LPERTPATVG LAHTAFTFPT LGDLIDKYLQ LRDKGIEPRV PVQHGVTTSL YYRDPDGNMV 

       130        140        150        160        170        180 
ELQIDNFATP EESTDYMHGE EYTTDTIGPS FNPLALAEAY KAGVPESELT TRAWALKTEQ 

       190 
INVMERMLTP 

P47233 in FASTA format

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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

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