ID HCAF_SHISS Reviewed; 172 AA. AC Q3YZ14; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 05-MAY-2009, entry version 26. DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase subunit beta; DE EC=1.14.12.19; DE AltName: Full=Digoxigenin subunit beta; GN Name=hcaF; OrderedLocusNames=SSON_2621; 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: Part of the multicomponent 3-phenylpropionate CC dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic CC acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and CC cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively (By CC similarity). CC -!- CATALYTIC ACTIVITY: 3-phenylpropanoic acid + NADH + O(2) = cis-3- CC (2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol + NAD(+). CC -!- CATALYTIC ACTIVITY: Cinnamic acid + H(+) + NADH + O(2) = cis-3-(2- CC carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD(+). CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid CC degradation. CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the CC two subunits of the hydroxylase component (hcaE and hcaF), a CC ferredoxin (hcaC) and a ferredoxin reductase (hcaD) (By CC similarity). CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating CC dioxygenase beta subunit 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; AAZ89248.1; -; Genomic_DNA. DR RefSeq; YP_311483.1; -. DR GeneID; 3668241; -. DR GenomeReviews; CP000038_GR; SSON_2621. DR KEGG; ssn:SSON_2621; -. DR HOGENOM; Q3YZ14; -. DR OMA; Q3YZ14; DIFAGER. DR BioCyc; SSON300269:SSO_2621-MON; -. DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:HAMAP. DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01649; -; 1. DR InterPro; IPR000391; Rng_hydr_dOase-bsu. DR Pfam; PF00866; Ring_hydroxyl_B; 1. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; NAD; KW Oxidoreductase. FT CHAIN 1 172 3-phenylpropionate/cinnamic acid FT dioxygenase subunit beta. FT /FTId=PRO_0000333717. SQ SEQUENCE 172 AA; 20636 MW; 8958F95B6FF9E0D0 CRC64; MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLEQLDKEI RYTMRTTVNA QTRDRRKGVQ PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQISETDIP NVFAVRVNYL LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF //