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UniProtKB/Swiss-Prot entry P47228


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

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Entry information
Entry name BPHC_BURXL
Primary accession number P47228
Secondary accession number Q13FT6
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 70)
Name and origin of the protein
Protein name Biphenyl-2,3-diol 1,2-dioxygenase
Synonyms EC 1.13.11.39
23OHBP oxygenase
2,3-dihydroxybiphenyl dioxygenase
DHBD
Gene name
Name: bphC
OrderedLocusNames: Bxeno_C1125
ORFNames: Bxe_C1191
From
Burkholderia xenovorans (strain LB400) [TaxID: 266265] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(93)90345-4; PubMed=8344527 [NCBI, ExPASy, EBI, Israel, Japan]
Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.;
"Genetic analysis of a Pseudomonas locus encoding a pathway for biphenyl/polychlorinated biphenyl degradation.";
Gene 130:47-55(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0606924103; PubMed=17030797 [NCBI, ExPASy, EBI, Israel, Japan]
Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility.";
Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
[3]
PROTEIN SEQUENCE OF 2-32, SUBSTRATE CHARACTERIZATION, PRELIMINARY CRYSTALLIZATION, AND SUBUNIT.
PubMed=8428946 [NCBI, ExPASy, EBI, Israel, Japan]
Eltis L.D., Hofmann B., Hecht H.J., Luensdorf H., Timmis K.N.;
"Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.";
J. Biol. Chem. 268:2727-2732(1993).
[4]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=7481800 [NCBI, ExPASy, EBI, Israel, Japan]
Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T.;
"Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad.";
Science 270:976-980(1995).
[5]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1074/jbc.273.52.34887; PubMed=9857017 [NCBI, ExPASy, EBI, Israel, Japan]
Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D.;
"Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol.";
J. Biol. Chem. 273:34887-34895(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
X66122; CAA46910.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000272; ABE37053.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0815; JN0815.
RefSeq YP_556403.1; -.
3D structure databases
PDB
1HAN; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
1KMY; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1KND; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
1KNF; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
1LGT; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
1LKD; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HAN; -.
1KMY; -.
1KND; -.
1KNF; -.
1LGT; -.
1LKD; -.
ModBase P47228.
Enzyme and pathway databases
BioCyc BXEN266265:BXE_C1191-MON; -.
Family and domain databases
InterPro IPR017626; DiOHbiphenyl_dOase.
IPR004360; Glyas_bleo-R_dOase.
IPR000486; Xdiol_dOase_1_2.
Graphical view of domain structure.
Pfam PF00903; Glyoxalase; 2.
Pfam graphical view of domain structure.
ProDom PD002334; Gly_diox; 2.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00082; EXTRADIOL_DIOXYGENAS; 1.
BLOCKS P47228.
Genome annotation databases
GeneID 4010703; -.
GenomeReviews CP000272_GR; Bxeno_C1125.
KEGG bxe:Bxe_C1191; -.
Phylogenomic databases
HOGENOM P47228; -.
Other
LinkHub P47228; -.
Genome annotation databases
CMR P47228; Bxeno_C1125.
Other
ProtoNet P47228.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   298  297     Biphenyl-2,3-diol 1,2-dioxygenase. PRO_0000085033
METAL   146   146        Iron. 
METAL   210   210        Iron. 
METAL   260   260        Iron. 
STRAND   3    14  12      
HELIX   16    25  10      
STRAND   30    35  6      
STRAND   38    47  10      
STRAND   49    54  6      
STRAND   59    69  11      
HELIX   70    82  13      
HELIX   92    98  7      
STRAND   101   107  7      
STRAND   113   118  6      
STRAND   131   133  3      
HELIX   140   142  3      
STRAND   146   150  5      
HELIX   154   163  10      
STRAND   168   176  9      
STRAND   178   180  3      
STRAND   182   194  13      
STRAND   196   200  5      
STRAND   205   217  13      
HELIX   218   229  12      
TURN   230   232  3      
STRAND   234   244  11      
STRAND   247   252  6      
STRAND   258   263  6      
STRAND   275   278  4      
STRAND   280   284  5      
Sequence information
Length: 298 AA [This is the length of the unprocessed precursor] Molecular weight: 32471 Da [This is the MW of the unprocessed precursor] CRC64: ADC0E4709E193FAB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSIRSLGYMG FAVSDVAAWR SFLTQKLGLM EAGTTDNGDL FRIDSRAWRI AVQQGEVDDL 

        70         80         90        100        110        120 
AFAGYEVADA AGLAQMADKL KQAGIAVTTG DASLARRRGV TGLITFADPF GLPLEIYYGA 

       130        140        150        160        170        180 
SEVFEKPFLP GAAVSGFLTG EQGLGHFVRC VPDSDKALAF YTDVLGFQLS DVIDMKMGPD 

       190        200        210        220        230        240 
VTVPAYFLHC NERHHTLAIA AFPLPKRIHH FMLEVASLDD VGFAFDRVDA DGLITSTLGR 

       250        260        270        280        290 
HTNDHMVSFY ASTPSGVEVE YGWSARTVDR SWVVVRHDSP SMWGHKSVRD KAAARNKA 

P47228 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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