ID HCAD_ECOLI Reviewed; 400 AA. AC P77650; O08100; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 168. DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component; DE EC=1.18.1.3; GN Name=hcaD; Synonyms=hcaA4, phdA, yfhY; GN OrderedLocusNames=b2542, JW2526; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140; RX PubMed=9603882; DOI=10.1128/jb.180.11.2915-2923.1998; RA Diaz E., Ferrandez A., Garcia J.L.; RT "Characterization of the hca cluster encoding the dioxygenolytic pathway RT for initial catabolism of 3-phenylpropionic acid in Escherichia coli RT K-12."; RL J. Bacteriol. 180:2915-2923(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of RT its sequence features."; RL DNA Res. 4:91-113(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). 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. 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; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation. 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). CC -!- INTERACTION: CC P77650; P0A6Z6: nikR; NbExp=2; IntAct=EBI-1129389, EBI-562488; CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase CC ferredoxin reductase family. {ECO:0000305}. 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; Y11070; CAA71952.1; -; Genomic_DNA. DR EMBL; U00096; AAC75595.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16445.1; -; Genomic_DNA. DR PIR; E65031; E65031. DR RefSeq; NP_417037.1; NC_000913.3. DR RefSeq; WP_000660788.1; NZ_LN832404.1. DR AlphaFoldDB; P77650; -. DR SMR; P77650; -. DR BioGRID; 4259462; 12. DR BioGRID; 849801; 5. DR ComplexPortal; CPX-5161; 3-phenylpropionate/cinnamic acid dioxygenase. DR IntAct; P77650; 7. DR STRING; 511145.b2542; -. DR PaxDb; 511145-b2542; -. DR EnsemblBacteria; AAC75595; AAC75595; b2542. DR GeneID; 945427; -. DR KEGG; ecj:JW2526; -. DR KEGG; eco:b2542; -. DR PATRIC; fig|1411691.4.peg.4192; -. DR EchoBASE; EB3233; -. DR eggNOG; COG0446; Bacteria. DR HOGENOM; CLU_003291_4_0_6; -. DR InParanoid; P77650; -. DR OMA; RCTHYGA; -. DR OrthoDB; 9800167at2; -. DR PhylomeDB; P77650; -. DR BioCyc; EcoCyc:HCAD-MONOMER; -. DR BioCyc; MetaCyc:HCAD-MONOMER; -. DR UniPathway; UPA00714; -. DR PRO; PR:P77650; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0009334; C:3-phenylpropionate dioxygenase complex; NAS:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central. DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IMP:EcoCyc. 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; 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 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 1: Evidence at protein level; 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_0000167661" FT BINDING 5..36 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" FT BINDING 146..174 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255" SQ SEQUENCE 400 AA; 43978 MW; F5A1A06C4F1DFF36 CRC64; MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIATGA AARPLPLLDA LGERCFTLRH AGDAARLREV LQPERSVVII 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 //