HCAD_ECOLI
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 03-AUG-2022, entry version 162.
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; OrderedLocusNames=b2542, JW2526;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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 K-
RT 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}.
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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; P77650; -.
DR PRIDE; P77650; -.
DR EnsemblBacteria; AAC75595; AAC75595; b2542.
DR EnsemblBacteria; BAA16445; BAA16445; BAA16445.
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; IATYPYH; -.
DR PhylomeDB; P77650; -.
DR BioCyc; EcoCyc:HCAD-MON; -.
DR BioCyc; MetaCyc:HCAD-MON; -.
DR UniPathway; UPA00714; -.
DR PRO; PR:P77650; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009334; C:3-phenylpropionate dioxygenase complex; IC: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; -; 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 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
