ID MHPB2_DECAR Reviewed; 317 AA. AC Q47GC9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase 2; DE EC=1.13.11.16; GN Name=mhpB2; OrderedLocusNames=Daro_1353; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Dechloromonas. OX NCBI_TaxID=159087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.; RT "Complete sequence of Dechloromonas aromatica RCB."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative CC cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3- CC dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2- CC hydroxy-6-ketononatrienedioate, respectively (By similarity). CC -!- CATALYTIC ACTIVITY: 3-(2,3-dihydroxyphenyl)propanoate + O(2) = 2- CC hydroxy-6-oxonona-2,4-diene-1,9-dioate. CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxicinnamic acid + O(2) = 2-hydroxy- CC 6-oxonona-2,4,7-triene-1,9-dioate. CC -!- COFACTOR: Fe(2+) ion (By similarity). CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid CC degradation. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the ligB/mhpB extradiol dioxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000089; AAZ46102.1; -; Genomic_DNA. DR RefSeq; YP_284572.1; -. DR GeneID; 3569243; -. DR GenomeReviews; CP000089_GR; Daro_1353. DR KEGG; dar:Daro_1353; -. DR NMPDR; fig|159087.4.peg.1140; -. DR HOGENOM; Q47GC9; -. DR OMA; Q47GC9; INWIELM. DR BioCyc; DARO159087:DARO_1353-MON; -. DR GO; GO:0008669; F:2,3-dihydroxy-phenylpropionate 1,2-dioxygen...; IEA:HAMAP. DR GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase acti...; IEA:EC. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01653; -; 1. DR InterPro; IPR004183; Xdiol_dOase_3B. DR Pfam; PF02900; LigB; 1. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; KW Iron; Oxidoreductase. FT CHAIN 1 317 2,3-dihydroxyphenylpropionate/2,3- FT dihydroxicinnamic acid 1,2-dioxygenase 2. FT /FTId=PRO_0000337649. FT ACT_SITE 115 115 Proton donor (By similarity). FT ACT_SITE 179 179 Proton acceptor (By similarity). SQ SEQUENCE 317 AA; 34499 MW; 2AE4707EA6D0BE23 CRC64; MAALLQCISH SPMKGYVDPS PAIVSDVEVA IARMRKELVD FDPEVIFLFA PDHYNGFFLD VMPQFCVGIA ATSVGDYRTT PGPINVPREI ARSCAEHLIS NDIDVAISYR MQVDHGMVQP LEELMGGLNA YPVVPLFVNG VAPPLISIRR ARLFGAAVGE YAKKLNKRCL FIGSGGLSHN PPVPQIDTAT EEFAEFLIAG RNPSPERRAA RQQRTKDAAI RFAAGDSQLH PINSVWDEAF MADLVNQDWG ALDAYRNSEI TEQAGISTHE AKSWVAAHAA MNAATSGGYM AEVRYYKAIP EWIVGYGAMA GSAEQAT //