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UniProtKB/Swiss-Prot entry P17295


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

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Entry information
Entry name MHPB_RALEU
Primary accession number P17295
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 42)
Name and origin of the protein
Protein name 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
Synonym EC 1.13.11.16
Gene name
Name: mhpB
Synonyms: mcpI
From
Ralstonia eutropha (Alcaligenes eutrophus) [TaxID: 106590] 
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JMP222;
DOI=10.1093/nar/18.11.3405; PubMed=2356133 [NCBI, ExPASy, EBI, Israel, Japan]
Kabisch M., Fortnagel P.;
"Nucleotide sequence of metapyrocatechase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222.";
Nucleic Acids Res. 18:3405-3405(1990).
[2]
FUNCTION IN CATABOLISM OF 3-HYDROXY DERIVATIVES OF PHENYLPROPIONIC ACID, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8752345 [NCBI, ExPASy, EBI, Israel, Japan]
Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H.;
"Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases.";
J. Bacteriol. 178:5249-5256(1996).
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
X52414; CAA36665.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S10154; S10154.
3D structure databases
ModBase P17295.
Ontologies
GO
GO:0008669; Molecular function: 2,3-dihydroxy-phenylpropionate 1,2-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019439; Biological process: aromatic compound catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01653; -; 1.
PBIL [Tree]
InterPro IPR004183; Xdiol_dOase_3B.
Graphical view of domain structure.
Gene3D G3DSA:3.40.830.10; Xdiol_dOase_3B; 1.
Pfam PF02900; LigB; 1.
Pfam graphical view of domain structure.
BLOCKS P17295.
Other
ProtoNet P17295.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   313  313     2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase. PRO_0000085102
ACT_SITE   115   115        Proton donor (By similarity). 
ACT_SITE   179   179        Proton acceptor (By similarity). 
Sequence information
Length: 313 AA [This is the length of the unprocessed precursor] Molecular weight: 33143 Da [This is the MW of the unprocessed precursor] CRC64: E1506B3785E9D0F9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPIQLECLSH TPLHGYVDPA PEVVAEVERV QAAARDRVRA FDPELVVVFA PDHFNGFFYD 

        70         80         90        100        110        120 
VMPPFCIGAA ATAIGDFKSL AGKLPVPADL ALSLAESVMA ADIDVALSHR MQVDHGCADA 

       130        140        150        160        170        180 
LAALTGSLHR YPVIPVFINS VAPPMATLRR ARLLGDAVGR FLSRAGKRVL VVGSGGISHE 

       190        200        210        220        230        240 
PPVPELAGAS EEVAERLIAG RNPSPESAAR QARTVAAAKS FVAGDSHLHP LNPEWDRAFL 

       250        260        270        280        290        300 
SLLASGELTA VDGMTNDAIT RDGGKSAHEI RTWVAAFGAL AAYGPYRASL DFYRAIPEWI 

       310 
AGFATMHAEP AAV 

P17295 in FASTA format

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