ID   HCAD_ECO24              Reviewed;         400 AA.
AC   A7ZPY5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   04-NOV-2026, entry version 102.
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};
GN   OrderedLocusNames=EcE24377A_2827;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(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=2 reduced [2Fe-2S]-[ferredoxin] + NAD(+) + H(+) = 2 oxidized
CC         [2Fe-2S]-[ferredoxin] + NADH; 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000800; ABV18229.1; -; Genomic_DNA.
DR   RefSeq; WP_000660792.1; NC_009801.1.
DR   AlphaFoldDB; A7ZPY5; -.
DR   SMR; A7ZPY5; -.
DR   KEGG; ecw:EcE24377A_2827; -.
DR   HOGENOM; CLU_003291_4_0_6; -.
DR   OMA; AAECPHK; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:TreeGrafter.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.30.390.30:FF:000010; 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component; 1.
DR   FunFam; 3.50.50.60:FF:000088; 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   HAMAP; MF_01651; HcaD; 1.
DR   InterPro; IPR050446; FAD-oxidoreductase/Apoptosis.
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   InterPro; IPR053382; Ring-hydroxylating_dioxygenase.
DR   NCBIfam; NF042949; 3PPDioc_HcaD; 1.
DR   NCBIfam; NF007286; hcaD; 1.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..400
FT                   /note="3-phenylpropionate/cinnamic acid dioxygenase
FT                   ferredoxin--NAD(+) reductase component"
FT                   /id="PRO_0000333724"
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;  44008 MW;  281F7C3E44173AAE CRC64;
     MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ
     QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIATGA AARPLPLLDA
     LGERCFTLRH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRRCKV TVIELAATVM
     GRNAPLPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS
     ANEQLAREAN LDTANGIVID EVCRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ
     IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA IWFNLQNGVL
     IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL
//