HCAD_ECOSE
ID HCAD_ECOSE Reviewed; 400 AA.
AC B6I5B5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component {ECO:0000255|HAMAP-Rule:MF_01651};
DE EC=1.18.1.3 {ECO:0000255|HAMAP-Rule:MF_01651};
GN Name=hcaD {ECO:0000255|HAMAP-Rule:MF_01651}; OrderedLocusNames=ECSE_2829;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
CC -!- FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase,
CC that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into
CC 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-
CC dihydrodiol (CI-dihydrodiol), respectively. {ECO:0000255|HAMAP-
CC Rule:MF_01651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01651};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01651};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01651}.
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_01651}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000255|HAMAP-Rule:MF_01651}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009240; BAG78353.1; -; Genomic_DNA.
DR RefSeq; WP_000660797.1; NC_011415.1.
DR AlphaFoldDB; B6I5B5; -.
DR SMR; B6I5B5; -.
DR EnsemblBacteria; BAG78353; BAG78353; ECSE_2829.
DR GeneID; 66673570; -.
DR KEGG; ecy:ECSE_2829; -.
DR HOGENOM; CLU_003291_4_0_6; -.
DR OMA; IATYPYH; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000008199; Chromosome.
DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01651; HcaD; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR023744; HcaD.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..400
FT /note="3-phenylpropionate/cinnamic acid dioxygenase
FT ferredoxin--NAD(+) reductase component"
FT /id="PRO_1000186987"
FT BINDING 5..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01651"
FT BINDING 146..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01651"
SQ SEQUENCE 400 AA; 43964 MW; F5A1A7CF4F1DF2A6 CRC64;
MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ
QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIATGA AARPLPLLDA
LGERCFTLRH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRRCKV TVIELAATVM
GRNAPPPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS
ANEQLAREAN LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ
IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA IWFNLQNGVL
IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL