ID   HCAE_ECOLI              Reviewed;         453 AA.
AC   P0ABR5; P77590; P78203; Q47139;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
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; Synonyms=digA, hcaA, hcaA1, phdC1, yfhU;
GN   OrderedLocusNames=b2538, JW2522;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Turlin E., Gasser F., Biville F.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS.
RC   STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX   MEDLINE=98269008; PubMed=9603882;
RA   Diaz E., Ferrandez A., Garcia J.L.;
RT   "Characterization of the hca cluster encoding the dioxygenolytic
RT   pathway for initial catabolism of 3-phenylpropionic acid in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 180:2915-2923(1998).
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.
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 2Fe-2S cluster (Probable).
CC   -!- COFACTOR: Binds 1 iron ion (Probable).
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).
CC   -!- INTERACTION:
CC       P0A6F5:groL; NbExp=1; IntAct=EBI-1115311, EBI-543750;
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; Z37966; CAA86018.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75591.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16441.1; -; Genomic_DNA.
DR   PIR; A65031; A65031.
DR   RefSeq; AP_003124.1; -.
DR   RefSeq; NP_417033.1; -.
DR   HSSP; P23094; 1O7N.
DR   IntAct; P0ABR5; 5.
DR   GeneID; 946998; -.
DR   GenomeReviews; AP009048_GR; JW2522.
DR   GenomeReviews; U00096_GR; b2538.
DR   KEGG; ecj:JW2522; -.
DR   KEGG; eco:b2538; -.
DR   EchoBASE; EB3229; -.
DR   EcoGene; EG13456; hcaE.
DR   HOGENOM; P0ABR5; -.
DR   OMA; P0ABR5; LEMEFIF.
DR   BioCyc; EcoCyc:PHENYLPRODIOXY-MON; -.
DR   BioCyc; MetaCyc:PHENYLPRODIOXY-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:0005515; F:protein binding; IPI:IntAct.
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   1: Evidence at protein level;
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_0000085061.
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).
FT   CONFLICT     20     20       V -> A (in Ref. 1; CAA86018).
FT   CONFLICT    384    453       GHRARNSKLCLEMGLGQEKRRDDGIPGITNYIFSETAARGM
FT                                YQRWADLLSSESWQEVLDKTAAYQQEVMK -> ATAPATAN
FT                                CVWKWGLVRKSAATTAFLALLTISFQKLPLVECTNAGPIF
FT                                (in Ref. 1; CAA86018).
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
//