ID   HCAF_ECOLI              Reviewed;         172 AA.
AC   Q47140; P77508;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   05-MAY-2009, entry version 65.
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; Synonyms=digB, hcaA2, hcaB, phdC2, yfhV;
GN   OrderedLocusNames=b2539, JW2523;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC   STRAIN=K12;
RA   Turlin E., Gasser F., Biville F.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-172, AND FUNCTION IN
RP   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   -!- 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   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase beta subunit family.
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DR   EMBL; U00096; AAC75592.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16442.1; -; Genomic_DNA.
DR   EMBL; Z37966; CAA86019.1; -; Genomic_DNA.
DR   EMBL; Y11070; CAA71949.1; -; Genomic_DNA.
DR   PIR; B65031; B65031.
DR   RefSeq; AP_003125.1; -.
DR   RefSeq; NP_417034.1; -.
DR   GeneID; 946997; -.
DR   GenomeReviews; AP009048_GR; JW2523.
DR   GenomeReviews; U00096_GR; b2539.
DR   KEGG; ecj:JW2523; -.
DR   KEGG; eco:b2539; -.
DR   EchoBASE; EB3230; -.
DR   EcoGene; EG13457; hcaF.
DR   HOGENOM; Q47140; -.
DR   OMA; Q47140; DIFAGER.
DR   BioCyc; EcoCyc:HCAA2-MON; -.
DR   BioCyc; MetaCyc:HCAA2-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   1: Evidence at protein level;
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_0000085077.
FT   CONFLICT     11     11       H -> Y (in Ref. 4; CAA86019).
FT   CONFLICT     49     49       N -> D (in Ref. 4; CAA86019).
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
//