HCAF_PHOLL
ID HCAF_PHOLL Reviewed; 180 AA.
AC Q7N4V9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=plu2205;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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; BX571866; CAE14498.1; -; Genomic_DNA.
DR RefSeq; WP_011146457.1; NC_005126.1.
DR AlphaFoldDB; Q7N4V9; -.
DR SMR; Q7N4V9; -.
DR STRING; 243265.plu2205; -.
DR EnsemblBacteria; CAE14498; CAE14498; plu2205.
DR GeneID; 24166434; -.
DR KEGG; plu:plu2205; -.
DR eggNOG; COG5517; Bacteria.
DR HOGENOM; CLU_102527_1_1_6; -.
DR OMA; LQAHQFL; -.
DR OrthoDB; 1736098at2; -.
DR BioCyc; PLUM243265:PLU_RS11010-MON; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000002514; 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..180
FT /note="3-phenylpropionate/cinnamic acid dioxygenase subunit
FT beta"
FT /id="PRO_0000333713"
SQ SEQUENCE 180 AA; 21783 MW; 3F29E545C70C1065 CRC64;
MKELIVNQEK RVSPELHYEI SQFLYYEIAL LDEWRFRDWL ELLSEDLSYT MRTIVNAQTR
DRRKSIQPPT TWLFNDNKFQ LERRIARLET GMAWAEEPPS RTRHLLTNLV ITETDLPDQF
HVQSNYLLYR SQKERDEVFY VGKRLDCVRR NPKTDSWLIC KREITLDQAV LTFHNLSVLF