ID   HCAE_SHISS              Reviewed;         453 AA.
AC   Q3YZ15;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=SSON_2620;
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   -!- 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.
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DR   EMBL; CP000038; AAZ89247.1; -; Genomic_DNA.
DR   RefSeq; YP_311482.1; -.
DR   GeneID; 3668240; -.
DR   GenomeReviews; CP000038_GR; SSON_2620.
DR   KEGG; ssn:SSON_2620; -.
DR   HOGENOM; Q3YZ15; -.
DR   OMA; Q3YZ15; LEMEFIF.
DR   BioCyc; SSON300269:SSO_2620-MON; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   HAMAP; MF_01648; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
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; 1.
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_0000333709.
FT   DOMAIN       44    142       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;  51109 MW;  02535BF5F47643FD CRC64;
     MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKPGDFFN
     TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNT RAFTCPYHGW SYGINGELID
     VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLRDYLGDI AWYLDGMLDR
     REGGTEIVGG VQKWVINCNW KFPAEQFASD QYHALFSHAS AVQVLGAKDD GSDKRLGDGQ
     TARPVWETAK DALQFGQDGH GSGFFFTEKP DANVWVDGAV SSYYRETYAE AEQRLGEVRA
     LRLAGHNNIF PTLSWLNGTA TLRVWHPRGP DQVEVWAFCI TDKAASDEVK AAFENSATRA
     FGPAGFLEQD DSENWCEIQK LLKGHRARNS KLCLEMGLGQ EKRRDDGIPG ITNYIFSETA
     ARGMYQRWAD LLSSESWQEV LDKTAAYQQE VMK
//