ID   HCAF_ECOHS              Reviewed;         172 AA.
AC   A8A345;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=EcHS_A2691;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV06949.1; -; Genomic_DNA.
DR   RefSeq; WP_001276076.1; NC_009800.1.
DR   AlphaFoldDB; A8A345; -.
DR   SMR; A8A345; -.
DR   GeneID; 58390238; -.
DR   KEGG; ecx:EcHS_A2691; -.
DR   HOGENOM; CLU_102527_1_1_6; -.
DR   OMA; LQAHQFL; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001123; Chromosome.
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_0000333712"
SQ   SEQUENCE   172 AA;  20565 MW;  58203B22B5D97554 CRC64;
     MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA QTRDRRKGVQ
     PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQVSETDIP NVFAVRVNYL
     LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF