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UniProtKB/Swiss-Prot entry P17297


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

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Entry information
Entry name BPHC_PSES1
Primary accession number P17297
Secondary accession number Q52441
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 73)
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
From
Pseudomonas sp. (strain KKS102) [TaxID: 307] 
Taxonomy Bacteria; Proteobacteria.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2540155 [NCBI, ExPASy, EBI, Israel, Japan]
Kimbara K., Hashimoto T., Fukuda M., Koana T., Takagi M., Oishi M., Yano K.;
"Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102.";
J. Bacteriol. 171:2740-2747(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
DOI=10.1006/bbrc.1994.2008; PubMed=8048958 [NCBI, ExPASy, EBI, Israel, Japan]
Fukuda M., Yasukochi Y., Kikuchi Y., Nagata Y., Kimbara K., Horiuchi H., Takagi M., Yano K.;
"Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls.";
Biochem. Biophys. Res. Commun. 202:850-856(1994).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1006/jmbi.1996.0060; PubMed=8636975 [NCBI, ExPASy, EBI, Israel, Japan]
Senda T., Sugiyama K., Narita H., Yamamoto T., Kimbara K., Fukuda M., Sato M., Yano K., Mitsui Y.;
"Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102.";
J. Mol. Biol. 255:735-752(1996).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/S0162-0134(00)00172-0; PubMed=11293547 [NCBI, ExPASy, EBI, Israel, Japan]
Uragami Y., Senda T., Sugimoto K., Sato N., Nagarajan V., Masai E., Fukuda M., Mitsui Y.;
"Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase.";
J. Inorg. Biochem. 83:269-279(2001).
[5]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF NATIVE ENZYME; SUBSTRATE COMPLEXES AND H145A MUTANT.
DOI=10.1016/S0022-2836(02)00673-3; PubMed=12206778 [NCBI, ExPASy, EBI, Israel, Japan]
Sato N., Uragami Y., Nishizaki T., Takahashi Y., Sazaki G., Sugimoto K., Nonaka T., Masai E., Fukuda M., Senda T.;
"Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase.";
J. Mol. Biol. 321:621-636(2002).
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
M26433; AAA25750.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D17319; BAA04141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32312; DAPSPC.
3D structure databases
PDB
1DHY; X-ray; 2.30 A; A=1-293.[ExPASy / RCSB / EBI]
1EIL; X-ray; 2.00 A; A=1-293.[ExPASy / RCSB / EBI]
1EIQ; X-ray; 2.00 A; A=1-293.[ExPASy / RCSB / EBI]
1EIR; X-ray; 2.00 A; A=1-293.[ExPASy / RCSB / EBI]
1KW3; X-ray; 1.45 A; B=1-293.[ExPASy / RCSB / EBI]
1KW6; X-ray; 1.45 A; B=1-293.[ExPASy / RCSB / EBI]
1KW8; X-ray; 2.00 A; B=1-293.[ExPASy / RCSB / EBI]
1KW9; X-ray; 1.95 A; B=1-293.[ExPASy / RCSB / EBI]
1KWB; X-ray; 2.00 A; B=1-293.[ExPASy / RCSB / EBI]
1KWC; X-ray; 2.10 A; B=1-293.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DHY; -.
1EIL; -.
1EIQ; -.
1EIR; -.
1KW3; -.
1KW6; -.
1KW8; -.
1KW9; -.
1KWB; -.
1KWC; -.
ModBase P17297.
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.
PD000977; Xdiol_dioxygnse; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00082; EXTRADIOL_DIOXYGENAS; 1.
BLOCKS P17297.
Other
LinkHub P17297; -.
ProtoNet P17297.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   293  292     Biphenyl-2,3-diol 1,2-dioxygenase. PRO_0000085035
METAL   146   146        Iron. 
METAL   210   210        Iron. 
METAL   261   261        Iron. 
STRAND   5    14  10      
HELIX   16    25  10      
STRAND   30    35  6      
STRAND   38    47  10      
STRAND   49    54  6      
STRAND   59    66  8      
HELIX   70    83  14      
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   178  11      
STRAND   181   194  14      
STRAND   196   200  5      
STRAND   205   217  13      
HELIX   218   230  13      
STRAND   238   244  7      
STRAND   247   252  6      
STRAND   259   264  6      
STRAND   277   279  3      
STRAND   281   285  5      
Sequence information
Length: 293 AA [This is the length of the unprocessed precursor] Molecular weight: 32245 Da [This is the MW of the unprocessed precursor] CRC64: 53EF1B24502E3B24 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSIERLGYLG FAVKDVPAWD HFLTKSVGLM AAGSAGDAAL YRADQRAWRI AVQPGELDDL 

        70         80         90        100        110        120 
AYAGLEVDDA AALERMADKL RQAGVAFTRG DEALMQQRKV MGLLCLQDPF GLPLEIYYGP 

       130        140        150        160        170        180 
AEIFHEPFLP SAPVSGFVTG DQGIGHFVRC VPDTAKAMAF YTEVLGFVLS DIIDIQMGPE 

       190        200        210        220        230        240 
TSVPAHFLHC NGRHHTIALA AFPIPKRIHH FMLQANTIDD VGYAFDRLDA AGRITSLLGR 

       250        260        270        280        290 
HTNDQTLSFY ADTPSPMIEV EFGWGPRTVD SSWTVARHSR TAMWGHKSVR GQR 

P17297 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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