ID HCAE_PHOLL Reviewed; 453 AA. AC Q7N4W0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 25-NOV-2008, entry version 33. DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase subunit alpha; DE EC=1.14.12.19; DE AltName: Full=Digoxigenin subunit alpha; GN Name=hcaE; OrderedLocusNames=plu2204; OS Photorhabdus luminescens subsp. laumondii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Photorhabdus. OX NCBI_TaxID=141679; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TT01; RX MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., RA Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., RA Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). 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 -!- COFACTOR: Binds 1 iron ion (By similarity). CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity). 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 alpha subunit family. CC -!- SIMILARITY: Contains 1 Rieske domain. 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; BX571866; CAE14497.1; -; Genomic_DNA. DR RefSeq; NP_929462.1; -. DR HSSP; P23094; 1EG9. DR GeneID; 2802209; -. DR GenomeReviews; BX470251_GR; plu2204. DR KEGG; plu:plu2204; -. DR PhotoList; plu2204; -. DR HOGENOM; Q7N4W0; -. DR BioCyc; PLUM243265:PLU2204-MON; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:HAMAP. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; 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:InterPro. DR HAMAP; MF_01648; -; 1. DR InterPro; IPR005806; Rieske_reg. DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C. DR InterPro; IPR001663; Rng_hydr_dOase-A. DR Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1. DR PANTHER; PTHR21266:SF2; Rng_hydr_dOase-A; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF00848; Ring_hydroxyl_A; 1. DR PRINTS; PR00090; RNGDIOXGNASE. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; FALSE_NEG. PE 3: Inferred from homology; KW 2Fe-2S; Aromatic hydrocarbons catabolism; Complete proteome; KW Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase. FT CHAIN 1 453 3-phenylpropionate/cinnamic acid FT dioxygenase subunit alpha. FT /FTId=PRO_0000333705. FT DOMAIN 43 141 Rieske. FT METAL 85 85 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 87 87 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 105 105 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 108 108 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 213 213 Iron (By similarity). FT METAL 218 218 Iron (By similarity). SQ SEQUENCE 453 AA; 51322 MW; 150ECAD0216477AE CRC64; MTLSKDSDIY RLIDARAGRV TPQIYIDPEL YQLELERIFG RCWLFLAHQS QIPNPGDFFN TYMGEDSVVV VRQKNGSVKA FLNQCRHRSM RVCYADSGNT RAFTCPYHGW SYGVDGRLID VPLEACAYPH GLCKEQWGLQ EVPCVENYKG LIFGNWDTTA PSLIDYLGDM AWYLDGVLDR REGGTEVIGG VQKWLINCNW KLPAEQFAGD QYHALFSHAS AVQVLSVKDG DDKKALGADQ TSRPVWETAK DAVQFAQNGH GCGFFLTEKP DANVWVDGAV ARYYRETYAE AEQRLGKVRA LRLAGHNNIF PTLSWLNGTA TMRVWHPRGP DQVEVWAFCI ADKAASPEVK AAFENSATRA FGPAGFLEQD DSENWVEIQK VLRGYKARNS TLCMEMRLGQ ERVRDDGIPG VTNYVFSETV ARGMYQRWAD LLTSETWDEI EEKSRVYQQE LVK //