ID MHPB_SHISS Reviewed; 314 AA. AC Q3Z586; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase; DE EC=1.13.11.16; GN Name=mhpB; OrderedLocusNames=SSON_0295; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). 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; CP000038; AAZ87076.1; -; Genomic_DNA. DR RefSeq; YP_309311.1; -. DR GeneID; 3669105; -. DR GenomeReviews; CP000038_GR; SSON_0295. DR KEGG; ssn:SSON_0295; -. DR HOGENOM; Q3Z586; -. DR OMA; Q3Z586; PLNPEWD. DR BioCyc; SSON300269:SSO_0295-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 1 314 2,3-dihydroxyphenylpropionate/2,3- FT dihydroxicinnamic acid 1,2-dioxygenase. FT /FTId=PRO_0000337669. FT ACT_SITE 115 115 Proton donor (By similarity). FT ACT_SITE 179 179 Proton acceptor (By similarity). SQ SEQUENCE 314 AA; 34196 MW; E1D5A8574E5DFE05 CRC64; MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE WIAGFGSLSA RTEN //