HCAC_ECOLI
ID HCAC_ECOLI Reviewed; 106 AA.
AC P0ABW0; O08099; P77266;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit;
GN Name=hcaC; Synonyms=hcaA3, phdB, yfhW; OrderedLocusNames=b2540, JW2524;
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. This protein seems to be a
CC 2Fe-2S ferredoxin.
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 -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000305}.
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DR EMBL; Y11070; CAA71950.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75593.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16443.1; -; Genomic_DNA.
DR PIR; C65031; C65031.
DR RefSeq; NP_417035.1; NC_000913.3.
DR RefSeq; WP_001080102.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0ABW0; -.
DR SMR; P0ABW0; -.
DR BioGRID; 4261575; 12.
DR ComplexPortal; CPX-5161; 3-phenylpropionate/cinnamic acid dioxygenase.
DR IntAct; P0ABW0; 4.
DR STRING; 511145.b2540; -.
DR PaxDb; P0ABW0; -.
DR EnsemblBacteria; AAC75593; AAC75593; b2540.
DR EnsemblBacteria; BAA16443; BAA16443; BAA16443.
DR GeneID; 66673572; -.
DR GeneID; 947015; -.
DR KEGG; ecj:JW2524; -.
DR KEGG; eco:b2540; -.
DR PATRIC; fig|1411691.4.peg.4194; -.
DR EchoBASE; EB3231; -.
DR eggNOG; COG2146; Bacteria.
DR HOGENOM; CLU_055690_5_2_6; -.
DR InParanoid; P0ABW0; -.
DR OMA; TLECWLH; -.
DR PhylomeDB; P0ABW0; -.
DR BioCyc; EcoCyc:HCAC-MON; -.
DR BioCyc; MetaCyc:HCAC-MON; -.
DR BRENDA; 3.7.1.14; 2026.
DR UniPathway; UPA00714; -.
DR PRO; PR:P0ABW0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009334; C:3-phenylpropionate dioxygenase complex; IC:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IMP:EcoCyc.
DR Gene3D; 2.102.10.10; -; 1.
DR HAMAP; MF_01650; HcaC; 1.
DR InterPro; IPR023739; HcaC.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Transport.
FT CHAIN 1..106
FT /note="3-phenylpropionate/cinnamic acid dioxygenase
FT ferredoxin subunit"
FT /id="PRO_0000201688"
FT DOMAIN 4..99
FT /note="Rieske"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
SQ SEQUENCE 106 AA; 11329 MW; B83149F4126BB72D CRC64;
MNRIYACPVA DVPEGEALRI DTSPVIALFN VGGEFYAIND RCSHGNASMS EGYLEDDATV
ECPLHAASFC LKTGKALCLP ATDPLTTYPV HVEGGDIFID LPEAQP
