ID HCAF_ECO24 Reviewed; 172 AA. AC A7ZPY2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 25-JAN-2012, entry version 31. 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=EcE24377A_2824; OS Escherichia coli O139:H28 (strain E24377A / ETEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331111; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E24377A / ETEC; RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic RT analysis of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). 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-phenylpropanoate + NADH + O(2) = 3-(cis-5,6- CC dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+). CC -!- CATALYTIC ACTIVITY: (2E)-3-phenylprop-2-enoate + NADH + O(2) = CC (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD(+). CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate 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; CP000800; ABV20129.1; -; Genomic_DNA. DR RefSeq; YP_001463861.1; NC_009801.1. DR ProteinModelPortal; A7ZPY2; -. DR SMR; A7ZPY2; 2-172. DR STRING; A7ZPY2; -. DR EnsemblBacteria; EBESCT00000020281; EBESCP00000019343; EBESCG00000019335. DR GeneID; 5589475; -. DR GenomeReviews; CP000800_GR; EcE24377A_2824. DR KEGG; ecw:EcE24377A_2824; -. DR PATRIC; 18294941; VBIEscCol31211_3103. DR eggNOG; COG5517; -. DR GeneTree; EBGT00050000011518; -. DR HOGENOM; HBG582498; -. DR OMA; DIFAGER; -. DR ProtClustDB; PRK10069; -. DR BioCyc; ECOL331111:ECE24377A_2824-MONOMER; -. DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:EC. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR HAMAP; MF_01649; HcaF; 1; -. DR InterPro; IPR023712; HcaF. DR InterPro; IPR000391; Rng_hydr_dOase-bsu. DR KO; K05709; -. 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_0000333710. SQ SEQUENCE 172 AA; 20579 MW; 83833B22A75BE546 CRC64; MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA QTRDRRKGVQ PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQISETDIP NVFAVRVNYL LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF //