HCAF_ECOLU
ID HCAF_ECOLU Reviewed; 172 AA.
AC B7N6C6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=ECUMN_2859;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
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; CU928163; CAR14035.1; -; Genomic_DNA.
DR RefSeq; WP_001276064.1; NC_011751.1.
DR RefSeq; YP_002413561.1; NC_011751.1.
DR AlphaFoldDB; B7N6C6; -.
DR SMR; B7N6C6; -.
DR STRING; 585056.ECUMN_2859; -.
DR EnsemblBacteria; CAR14035; CAR14035; ECUMN_2859.
DR KEGG; eum:ECUMN_2859; -.
DR PATRIC; fig|585056.7.peg.3046; -.
DR HOGENOM; CLU_102527_1_1_6; -.
DR OMA; LQAHQFL; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000007097; 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_1000186978"
SQ SEQUENCE 172 AA; 20606 MW; 812827558F44D279 CRC64;
MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA QTRDRRKGIQ
PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQVNETDIP NVFAVRVNYL
LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF