ID   HCAF_ECO8A              Reviewed;         172 AA.
AC   B7M7P2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase subunit beta {ECO:0000255|HAMAP-Rule:MF_01649};
DE            EC=1.14.12.19 {ECO:0000255|HAMAP-Rule:MF_01649};
GN   Name=hcaF {ECO:0000255|HAMAP-Rule:MF_01649}; OrderedLocusNames=ECIAI1_2591;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase.
CC       Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-
CC       phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-
CC       dihydrodiol (CI-dihydrodiol), respectively. {ECO:0000255|HAMAP-
CC       Rule:MF_01649}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpropanoate + H(+) + NADH + O2 = 3-(cis-5,6-
CC         dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+);
CC         Xref=Rhea:RHEA:20357, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:51057, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:60087; EC=1.14.12.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01649};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamate + H(+) + NADH + O2 = (2E)-3-(cis-5,6-
CC         dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD(+);
CC         Xref=Rhea:RHEA:25058, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15669, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:61451; EC=1.14.12.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01649};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01649}.
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC       subunits of the hydroxylase component (HcaE and HcaF), a ferredoxin
CC       (HcaC) and a ferredoxin reductase (HcaD). {ECO:0000255|HAMAP-
CC       Rule:MF_01649}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000255|HAMAP-Rule:MF_01649}.
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DR   EMBL; CU928160; CAQ99430.1; -; Genomic_DNA.
DR   RefSeq; WP_001276072.1; NC_011741.1.
DR   AlphaFoldDB; B7M7P2; -.
DR   SMR; B7M7P2; -.
DR   GeneID; 66673573; -.
DR   KEGG; ecr:ECIAI1_2591; -.
DR   HOGENOM; CLU_102527_1_1_6; -.
DR   OMA; LQAHQFL; -.
DR   UniPathway; UPA00714; -.
DR   GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR   HAMAP; MF_01649; HcaF; 1.
DR   InterPro; IPR023712; HcaF.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR   PANTHER; PTHR41534; PTHR41534; 1.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..172
FT                   /note="3-phenylpropionate/cinnamic acid dioxygenase subunit
FT                   beta"
FT                   /id="PRO_1000186975"
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