ID   HCAD_ECOSM              Reviewed;         400 AA.
AC   B1LNJ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=EcSMS35_2695;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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}.
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DR   EMBL; CP000970; ACB19396.1; -; Genomic_DNA.
DR   RefSeq; WP_000660760.1; NC_010498.1.
DR   AlphaFoldDB; B1LNJ8; -.
DR   SMR; B1LNJ8; -.
DR   EnsemblBacteria; ACB19396; ACB19396; EcSMS35_2695.
DR   KEGG; ecm:EcSMS35_2695; -.
DR   HOGENOM; CLU_003291_4_0_6; -.
DR   OMA; IATYPYH; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000007011; 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_1000186988"
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;  43799 MW;  493B8A232529ADCF CRC64;
     MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDEQHL PYERPPLSKS MLLEDSPQLQ
     SVLPAHWWQE NNVHLHSGVT IKTLGRDTRE LVLANGESWH WDQLFIATGA AARPLPLLDA
     LGERCFTLRH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRGCKV TVIELAATVM
     GRNAPPPVQH YLLQRHQQAG VRILLNNAIE HVVDGENVEL TLQSGETLRA DVVIYGIGIS
     ANDQLAREAN LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ
     IAASAMLGLP LPRLPPPWFW SDQYSDNLQF IGDMHGDDWL CRGNPETQKA IWFNLQNGVL
     IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL TDEDIALKSL