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HCAF_SHIFL
ID   HCAF_SHIFL              Reviewed;         172 AA.
AC   Q83K38; Q7C0G3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
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};
GN   OrderedLocusNames=SF2586, S2758;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44085.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17910.1; -; Genomic_DNA.
DR   RefSeq; NP_708378.1; NC_004337.2.
DR   RefSeq; WP_001276076.1; NZ_WPGW01000021.1.
DR   AlphaFoldDB; Q83K38; -.
DR   SMR; Q83K38; -.
DR   STRING; 198214.SF2586; -.
DR   EnsemblBacteria; AAN44085; AAN44085; SF2586.
DR   EnsemblBacteria; AAP17910; AAP17910; S2758.
DR   GeneID; 1025645; -.
DR   GeneID; 58390238; -.
DR   KEGG; sfl:SF2586; -.
DR   KEGG; sfx:S2758; -.
DR   PATRIC; fig|198214.7.peg.3086; -.
DR   HOGENOM; CLU_102527_1_1_6; -.
DR   OMA; LQAHQFL; -.
DR   OrthoDB; 1736098at2; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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;
KW   Reference proteome.
FT   CHAIN           1..172
FT                   /note="3-phenylpropionate/cinnamic acid dioxygenase subunit
FT                   beta"
FT                   /id="PRO_0000333715"
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
 
 
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