HCAD_ECO24
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 03-AUG-2022, entry version 90.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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; CP000800; ABV18229.1; -; Genomic_DNA.
DR RefSeq; WP_000660792.1; NC_009801.1.
DR AlphaFoldDB; A7ZPY5; -.
DR SMR; A7ZPY5; -.
DR EnsemblBacteria; ABV18229; ABV18229; EcE24377A_2827.
DR KEGG; ecw:EcE24377A_2827; -.
DR HOGENOM; CLU_003291_4_0_6; -.
DR OMA; IATYPYH; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000001122; 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_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