ID   HCAF_SHIBS              Reviewed;         172 AA.
AC   Q31XV1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=SBO_2563;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB67107.1; -; Genomic_DNA.
DR   RefSeq; WP_001276086.1; NC_007613.1.
DR   AlphaFoldDB; Q31XV1; -.
DR   SMR; Q31XV1; -.
DR   EnsemblBacteria; ABB67107; ABB67107; SBO_2563.
DR   KEGG; sbo:SBO_2563; -.
DR   HOGENOM; CLU_102527_1_1_6; -.
DR   OMA; LQAHQFL; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000007067; 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_0000333714"
SQ   SEQUENCE   172 AA;  20527 MW;  6696CD372BA12540 CRC64;
     MSAQVSLELH LRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA QTRDRRKGVQ
     PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQISETDIP NVFAVRVNYL
     LYQAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF